IL-32 Antibody

IL-32 is stabilized by deubiquitinases. (A) JJN3 cells were stimulated with PR619 (30 μM during normoxia and hypoxia before the sample was harvested at indicated time points. The figure shows representative WB of IL-32 protein levels of n = 3 independent experiments. (B) JJN3 cells were incubated overnight in hypoxia before they were moved to normoxia for 4 h with and without PR619 stimulation. Cells were harvested, and lysates were processed in the presence of a NEM-DUB inhibitor. Ubiqutinylated and nonubiqutinylated 27 kDA IL-32 proteins were assessed by WB. (C) JJN3 cells were stimulated with a panel of DUB inhibitors (see Supplementary Table S1 for concentrations) for 4 h, and IL-32 protein levels were analyzed by WB. Shown here is the representative WB of n = 3 independent experiments. (D) Human primary T cells isolated from healthy blood donors were treated with CHX (5 µg/ml), MG132 (20 µM), and PR619 (30 µM) and harvested at the indicated time points. Shown here is the representative WB from experiments with n = 3 donors. (E) Human primary T cells isolated from healthy blood donors were cultured overnight in hypoxia before IL-32 protein levels were assessed by WB. A representative WB from experiments with three different donors is shown here. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 protein half-life is regulated by the oxygen sensor ADO. (A) JJN-3 cells were transfected with ADO- and nontargeting Ctrl siRNA. After 24 h, the cells were seeded and cultured overnight in normoxia or hypoxia before being treated with 5 μg/ml CHX and the IL-32 CHX chase assay in normoxia and hypoxia. One representative WB of IL-32 and ADO siRNA-treated cells of n = 5 independent experiments is shown. (B) JJN-3 cells were transfected with ADO and nontargeting Ctrl siRNA. After being transfected for 24 h, the cells were cultured overnight in hypoxia before being treated with 5 µg/ml CHX and reoxygenized in normoxic culture conditions. Cells were harvested at indicated time points. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

TLR-induced NF kappa B signaling promotes IL-32 expression in MM cells. (A) RPMI-8226 cells were stimulated with TLR agonists (for concentrations, see methods) for 4 and 24 hours and IL-32 mRNA expression was assessed by qPCR. The figure shows mean ± SEM of 3 independent experiments. (B) RPMI-8226 cells were stimulated with TLR agonists for 4 and 24 hours and IL-32 protein expression was evaluated by western blot. The figure shows representative western blot of 3 independent experiments. (C) RPMI-8226 cells were harvested at different time-points following LPS stimulation (0.1 µg/mL) and IL-32 mRNA expression was analyzed by qPCR (mean ± SD) and (D) IL-32 protein expression by western blot (E) RPMI-8226 TLR4 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. Figure shows representative western blot (n=3) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (F) RPMI-8226 TLR9 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. The figure shows representative western blot (n=2) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (G) RPMI-8226 cells were stimulated with LPS (0.1 µg/mL) and NG25 (2 µM) or IKK VII (10 µM) for 4 hours. IL-32 mRNA expression (mean ± SEM, n=3) was assessed by qPCR. (H) RPMI-8226 cells were stimulated with LPS, NG25 and IKK VII (concentrations as above) for 4 hours. The figure shows representative western blot (n=3) of IL-32 protein expression. P-values in (A) and (G) are calculated by one-way ANOVA with Dunnett´s multiple comparison test. *p≤ 0.05, **p ≤ 0.001, ****p ≤ 0.0001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36875074), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is degraded through the ubiquitin-proteasome pathway. (A, B) JJN3 cells were treated with 20 µM MG-132 and harvested at the indicated time points. IL-32 protein levels were analyzed by (A) Western blotting, and (B) IL-32 mRNA was assessed by qPCR using GAPDH as housekeeping gene. The bars show the mean RQ of IL-32 ± SD. (C) Confocal images of JJN3 cells treated for 4 h with 100 nM carfilzomib and stained with IL-32 antibody (green) and Hoechst (blue). (D) JJN3 cells were transfected with HA-ubiquitin plasmid and incubated in hypoxia overnight before the cells were harvested and IL-32 immunoprecipitation was performed. Protein levels of HA-ubiquitin, IL-32, and GAPDH loading control were evaluated on WB. Total lysate and IP samples from the same membrane are shown with different brightness/contrast. (E) JJN3 cells were incubated overnight in hypoxia before they were stimulated with MG-132 for 4 h and harvested for TUBE assay of ubiquitinylated proteins. The presence of IL-32 and ubiquitin protein in TUBE pulldown was assessed by WB. DUB treatment for reversal of polyubiqutinylation was included to validate ubiquitin/TUBE pulldown. Total lysate and TUBE samples from the same membrane are shown with different brightness/contrast. (F) JJN3 cells were stimulated with 2 μM TAK234 before the cells were harvested, and IL-32 levels were analyzed by WB. (A–F) One representative experiment out of three is shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 protein half-life is regulated by the oxygen sensor ADO. (A) JJN-3 cells were transfected with ADO- and nontargeting Ctrl siRNA. After 24 h, the cells were seeded and cultured overnight in normoxia or hypoxia before being treated with 5 μg/ml CHX and the IL-32 CHX chase assay in normoxia and hypoxia. One representative WB of IL-32 and ADO siRNA-treated cells of n = 5 independent experiments is shown. (B) JJN-3 cells were transfected with ADO and nontargeting Ctrl siRNA. After being transfected for 24 h, the cells were cultured overnight in hypoxia before being treated with 5 µg/ml CHX and reoxygenized in normoxic culture conditions. Cells were harvested at indicated time points. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is stabilized by deubiquitinases. (A) JJN3 cells were stimulated with PR619 (30 μM during normoxia and hypoxia before the sample was harvested at indicated time points. The figure shows representative WB of IL-32 protein levels of n = 3 independent experiments. (B) JJN3 cells were incubated overnight in hypoxia before they were moved to normoxia for 4 h with and without PR619 stimulation. Cells were harvested, and lysates were processed in the presence of a NEM-DUB inhibitor. Ubiqutinylated and nonubiqutinylated 27 kDA IL-32 proteins were assessed by WB. (C) JJN3 cells were stimulated with a panel of DUB inhibitors (see Supplementary Table S1 for concentrations) for 4 h, and IL-32 protein levels were analyzed by WB. Shown here is the representative WB of n = 3 independent experiments. (D) Human primary T cells isolated from healthy blood donors were treated with CHX (5 µg/ml), MG132 (20 µM), and PR619 (30 µM) and harvested at the indicated time points. Shown here is the representative WB from experiments with n = 3 donors. (E) Human primary T cells isolated from healthy blood donors were cultured overnight in hypoxia before IL-32 protein levels were assessed by WB. A representative WB from experiments with three different donors is shown here. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is degraded through the ubiquitin-proteasome pathway. (A, B) JJN3 cells were treated with 20 µM MG-132 and harvested at the indicated time points. IL-32 protein levels were analyzed by (A) Western blotting, and (B) IL-32 mRNA was assessed by qPCR using GAPDH as housekeeping gene. The bars show the mean RQ of IL-32 ± SD. (C) Confocal images of JJN3 cells treated for 4 h with 100 nM carfilzomib and stained with IL-32 antibody (green) and Hoechst (blue). (D) JJN3 cells were transfected with HA-ubiquitin plasmid and incubated in hypoxia overnight before the cells were harvested and IL-32 immunoprecipitation was performed. Protein levels of HA-ubiquitin, IL-32, and GAPDH loading control were evaluated on WB. Total lysate and IP samples from the same membrane are shown with different brightness/contrast. (E) JJN3 cells were incubated overnight in hypoxia before they were stimulated with MG-132 for 4 h and harvested for TUBE assay of ubiquitinylated proteins. The presence of IL-32 and ubiquitin protein in TUBE pulldown was assessed by WB. DUB treatment for reversal of polyubiqutinylation was included to validate ubiquitin/TUBE pulldown. Total lysate and TUBE samples from the same membrane are shown with different brightness/contrast. (F) JJN3 cells were stimulated with 2 μM TAK234 before the cells were harvested, and IL-32 levels were analyzed by WB. (A–F) One representative experiment out of three is shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is degraded through the ubiquitin-proteasome pathway. (A, B) JJN3 cells were treated with 20 µM MG-132 and harvested at the indicated time points. IL-32 protein levels were analyzed by (A) Western blotting, and (B) IL-32 mRNA was assessed by qPCR using GAPDH as housekeeping gene. The bars show the mean RQ of IL-32 ± SD. (C) Confocal images of JJN3 cells treated for 4 h with 100 nM carfilzomib and stained with IL-32 antibody (green) and Hoechst (blue). (D) JJN3 cells were transfected with HA-ubiquitin plasmid and incubated in hypoxia overnight before the cells were harvested and IL-32 immunoprecipitation was performed. Protein levels of HA-ubiquitin, IL-32, and GAPDH loading control were evaluated on WB. Total lysate and IP samples from the same membrane are shown with different brightness/contrast. (E) JJN3 cells were incubated overnight in hypoxia before they were stimulated with MG-132 for 4 h and harvested for TUBE assay of ubiquitinylated proteins. The presence of IL-32 and ubiquitin protein in TUBE pulldown was assessed by WB. DUB treatment for reversal of polyubiqutinylation was included to validate ubiquitin/TUBE pulldown. Total lysate and TUBE samples from the same membrane are shown with different brightness/contrast. (F) JJN3 cells were stimulated with 2 μM TAK234 before the cells were harvested, and IL-32 levels were analyzed by WB. (A–F) One representative experiment out of three is shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is stabilized by deubiquitinases. (A) JJN3 cells were stimulated with PR619 (30 μM during normoxia and hypoxia before the sample was harvested at indicated time points. The figure shows representative WB of IL-32 protein levels of n = 3 independent experiments. (B) JJN3 cells were incubated overnight in hypoxia before they were moved to normoxia for 4 h with and without PR619 stimulation. Cells were harvested, and lysates were processed in the presence of a NEM-DUB inhibitor. Ubiqutinylated and nonubiqutinylated 27 kDA IL-32 proteins were assessed by WB. (C) JJN3 cells were stimulated with a panel of DUB inhibitors (see Supplementary Table S1 for concentrations) for 4 h, and IL-32 protein levels were analyzed by WB. Shown here is the representative WB of n = 3 independent experiments. (D) Human primary T cells isolated from healthy blood donors were treated with CHX (5 µg/ml), MG132 (20 µM), and PR619 (30 µM) and harvested at the indicated time points. Shown here is the representative WB from experiments with n = 3 donors. (E) Human primary T cells isolated from healthy blood donors were cultured overnight in hypoxia before IL-32 protein levels were assessed by WB. A representative WB from experiments with three different donors is shown here. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

TLR-induced NF kappa B signaling promotes IL-32 expression in MM cells. (A) RPMI-8226 cells were stimulated with TLR agonists (for concentrations, see methods) for 4 and 24 hours and IL-32 mRNA expression was assessed by qPCR. The figure shows mean ± SEM of 3 independent experiments. (B) RPMI-8226 cells were stimulated with TLR agonists for 4 and 24 hours and IL-32 protein expression was evaluated by western blot. The figure shows representative western blot of 3 independent experiments. (C) RPMI-8226 cells were harvested at different time-points following LPS stimulation (0.1 µg/mL) and IL-32 mRNA expression was analyzed by qPCR (mean ± SD) and (D) IL-32 protein expression by western blot (E) RPMI-8226 TLR4 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. Figure shows representative western blot (n=3) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (F) RPMI-8226 TLR9 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. The figure shows representative western blot (n=2) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (G) RPMI-8226 cells were stimulated with LPS (0.1 µg/mL) and NG25 (2 µM) or IKK VII (10 µM) for 4 hours. IL-32 mRNA expression (mean ± SEM, n=3) was assessed by qPCR. (H) RPMI-8226 cells were stimulated with LPS, NG25 and IKK VII (concentrations as above) for 4 hours. The figure shows representative western blot (n=3) of IL-32 protein expression. P-values in (A) and (G) are calculated by one-way ANOVA with Dunnett´s multiple comparison test. *p≤ 0.05, **p ≤ 0.001, ****p ≤ 0.0001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36875074), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 has a high protein turnover. (A) JJN-3 cells were treated with CHX and harvested at the indicated time points. IL-32 protein levels were analyzed by WB. (B) Kinetics of IL-32 degradation in JJN3- cells. IL-32 protein signal intensity was quantified and normalized to loading control in n = 6 CHX chase experiments. The mean ±SEM is shown here. (C) JJN-3 cells were treated with 5 μg/ml CHX and 20 μM MG132 alone and in combination and harvested at the indicated time points. The figure shows one representative WB from n = 3 independent experiments. (D) Signal intensities of IL-32 and beta -actin were quantified from n = 3 independent experiments performed as in (C), and the values from treated samples at each time point were normalized relative to the control sample. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

TLR-induced NF kappa B signaling promotes IL-32 expression in MM cells. (A) RPMI-8226 cells were stimulated with TLR agonists (for concentrations, see methods) for 4 and 24 hours and IL-32 mRNA expression was assessed by qPCR. The figure shows mean ± SEM of 3 independent experiments. (B) RPMI-8226 cells were stimulated with TLR agonists for 4 and 24 hours and IL-32 protein expression was evaluated by western blot. The figure shows representative western blot of 3 independent experiments. (C) RPMI-8226 cells were harvested at different time-points following LPS stimulation (0.1 µg/mL) and IL-32 mRNA expression was analyzed by qPCR (mean ± SD) and (D) IL-32 protein expression by western blot (E) RPMI-8226 TLR4 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. Figure shows representative western blot (n=3) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (F) RPMI-8226 TLR9 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. The figure shows representative western blot (n=2) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (G) RPMI-8226 cells were stimulated with LPS (0.1 µg/mL) and NG25 (2 µM) or IKK VII (10 µM) for 4 hours. IL-32 mRNA expression (mean ± SEM, n=3) was assessed by qPCR. (H) RPMI-8226 cells were stimulated with LPS, NG25 and IKK VII (concentrations as above) for 4 hours. The figure shows representative western blot (n=3) of IL-32 protein expression. P-values in (A) and (G) are calculated by one-way ANOVA with Dunnett´s multiple comparison test. *p≤ 0.05, **p ≤ 0.001, ****p ≤ 0.0001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36875074), licensed under a CC-BY license. Not internally tested by R&D Systems.

TLR-induced NF kappa B signaling promotes IL-32 expression in MM cells. (A) RPMI-8226 cells were stimulated with TLR agonists (for concentrations, see methods) for 4 and 24 hours and IL-32 mRNA expression was assessed by qPCR. The figure shows mean ± SEM of 3 independent experiments. (B) RPMI-8226 cells were stimulated with TLR agonists for 4 and 24 hours and IL-32 protein expression was evaluated by western blot. The figure shows representative western blot of 3 independent experiments. (C) RPMI-8226 cells were harvested at different time-points following LPS stimulation (0.1 µg/mL) and IL-32 mRNA expression was analyzed by qPCR (mean ± SD) and (D) IL-32 protein expression by western blot (E) RPMI-8226 TLR4 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. Figure shows representative western blot (n=3) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (F) RPMI-8226 TLR9 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. The figure shows representative western blot (n=2) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (G) RPMI-8226 cells were stimulated with LPS (0.1 µg/mL) and NG25 (2 µM) or IKK VII (10 µM) for 4 hours. IL-32 mRNA expression (mean ± SEM, n=3) was assessed by qPCR. (H) RPMI-8226 cells were stimulated with LPS, NG25 and IKK VII (concentrations as above) for 4 hours. The figure shows representative western blot (n=3) of IL-32 protein expression. P-values in (A) and (G) are calculated by one-way ANOVA with Dunnett´s multiple comparison test. *p≤ 0.05, **p ≤ 0.001, ****p ≤ 0.0001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36875074), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is stabilized by deubiquitinases. (A) JJN3 cells were stimulated with PR619 (30 μM during normoxia and hypoxia before the sample was harvested at indicated time points. The figure shows representative WB of IL-32 protein levels of n = 3 independent experiments. (B) JJN3 cells were incubated overnight in hypoxia before they were moved to normoxia for 4 h with and without PR619 stimulation. Cells were harvested, and lysates were processed in the presence of a NEM-DUB inhibitor. Ubiqutinylated and nonubiqutinylated 27 kDA IL-32 proteins were assessed by WB. (C) JJN3 cells were stimulated with a panel of DUB inhibitors (see Supplementary Table S1 for concentrations) for 4 h, and IL-32 protein levels were analyzed by WB. Shown here is the representative WB of n = 3 independent experiments. (D) Human primary T cells isolated from healthy blood donors were treated with CHX (5 µg/ml), MG132 (20 µM), and PR619 (30 µM) and harvested at the indicated time points. Shown here is the representative WB from experiments with n = 3 donors. (E) Human primary T cells isolated from healthy blood donors were cultured overnight in hypoxia before IL-32 protein levels were assessed by WB. A representative WB from experiments with three different donors is shown here. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 has a high protein turnover. (A) JJN-3 cells were treated with CHX and harvested at the indicated time points. IL-32 protein levels were analyzed by WB. (B) Kinetics of IL-32 degradation in JJN3- cells. IL-32 protein signal intensity was quantified and normalized to loading control in n = 6 CHX chase experiments. The mean ±SEM is shown here. (C) JJN-3 cells were treated with 5 μg/ml CHX and 20 μM MG132 alone and in combination and harvested at the indicated time points. The figure shows one representative WB from n = 3 independent experiments. (D) Signal intensities of IL-32 and beta -actin were quantified from n = 3 independent experiments performed as in (C), and the values from treated samples at each time point were normalized relative to the control sample. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 protein half-life is regulated by the oxygen sensor ADO. (A) JJN-3 cells were transfected with ADO- and nontargeting Ctrl siRNA. After 24 h, the cells were seeded and cultured overnight in normoxia or hypoxia before being treated with 5 μg/ml CHX and the IL-32 CHX chase assay in normoxia and hypoxia. One representative WB of IL-32 and ADO siRNA-treated cells of n = 5 independent experiments is shown. (B) JJN-3 cells were transfected with ADO and nontargeting Ctrl siRNA. After being transfected for 24 h, the cells were cultured overnight in hypoxia before being treated with 5 µg/ml CHX and reoxygenized in normoxic culture conditions. Cells were harvested at indicated time points. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is stabilized by deubiquitinases. (A) JJN3 cells were stimulated with PR619 (30 μM during normoxia and hypoxia before the sample was harvested at indicated time points. The figure shows representative WB of IL-32 protein levels of n = 3 independent experiments. (B) JJN3 cells were incubated overnight in hypoxia before they were moved to normoxia for 4 h with and without PR619 stimulation. Cells were harvested, and lysates were processed in the presence of a NEM-DUB inhibitor. Ubiqutinylated and nonubiqutinylated 27 kDA IL-32 proteins were assessed by WB. (C) JJN3 cells were stimulated with a panel of DUB inhibitors (see Supplementary Table S1 for concentrations) for 4 h, and IL-32 protein levels were analyzed by WB. Shown here is the representative WB of n = 3 independent experiments. (D) Human primary T cells isolated from healthy blood donors were treated with CHX (5 µg/ml), MG132 (20 µM), and PR619 (30 µM) and harvested at the indicated time points. Shown here is the representative WB from experiments with n = 3 donors. (E) Human primary T cells isolated from healthy blood donors were cultured overnight in hypoxia before IL-32 protein levels were assessed by WB. A representative WB from experiments with three different donors is shown here. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 has a high protein turnover. (A) JJN-3 cells were treated with CHX and harvested at the indicated time points. IL-32 protein levels were analyzed by WB. (B) Kinetics of IL-32 degradation in JJN3- cells. IL-32 protein signal intensity was quantified and normalized to loading control in n = 6 CHX chase experiments. The mean ±SEM is shown here. (C) JJN-3 cells were treated with 5 μg/ml CHX and 20 μM MG132 alone and in combination and harvested at the indicated time points. The figure shows one representative WB from n = 3 independent experiments. (D) Signal intensities of IL-32 and beta -actin were quantified from n = 3 independent experiments performed as in (C), and the values from treated samples at each time point were normalized relative to the control sample. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is degraded through the ubiquitin-proteasome pathway. (A, B) JJN3 cells were treated with 20 µM MG-132 and harvested at the indicated time points. IL-32 protein levels were analyzed by (A) Western blotting, and (B) IL-32 mRNA was assessed by qPCR using GAPDH as housekeeping gene. The bars show the mean RQ of IL-32 ± SD. (C) Confocal images of JJN3 cells treated for 4 h with 100 nM carfilzomib and stained with IL-32 antibody (green) and Hoechst (blue). (D) JJN3 cells were transfected with HA-ubiquitin plasmid and incubated in hypoxia overnight before the cells were harvested and IL-32 immunoprecipitation was performed. Protein levels of HA-ubiquitin, IL-32, and GAPDH loading control were evaluated on WB. Total lysate and IP samples from the same membrane are shown with different brightness/contrast. (E) JJN3 cells were incubated overnight in hypoxia before they were stimulated with MG-132 for 4 h and harvested for TUBE assay of ubiquitinylated proteins. The presence of IL-32 and ubiquitin protein in TUBE pulldown was assessed by WB. DUB treatment for reversal of polyubiqutinylation was included to validate ubiquitin/TUBE pulldown. Total lysate and TUBE samples from the same membrane are shown with different brightness/contrast. (F) JJN3 cells were stimulated with 2 μM TAK234 before the cells were harvested, and IL-32 levels were analyzed by WB. (A–F) One representative experiment out of three is shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 has a high protein turnover. (A) JJN-3 cells were treated with CHX and harvested at the indicated time points. IL-32 protein levels were analyzed by WB. (B) Kinetics of IL-32 degradation in JJN3- cells. IL-32 protein signal intensity was quantified and normalized to loading control in n = 6 CHX chase experiments. The mean ±SEM is shown here. (C) JJN-3 cells were treated with 5 μg/ml CHX and 20 μM MG132 alone and in combination and harvested at the indicated time points. The figure shows one representative WB from n = 3 independent experiments. (D) Signal intensities of IL-32 and beta -actin were quantified from n = 3 independent experiments performed as in (C), and the values from treated samples at each time point were normalized relative to the control sample. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is degraded through the ubiquitin-proteasome pathway. (A, B) JJN3 cells were treated with 20 µM MG-132 and harvested at the indicated time points. IL-32 protein levels were analyzed by (A) Western blotting, and (B) IL-32 mRNA was assessed by qPCR using GAPDH as housekeeping gene. The bars show the mean RQ of IL-32 ± SD. (C) Confocal images of JJN3 cells treated for 4 h with 100 nM carfilzomib and stained with IL-32 antibody (green) and Hoechst (blue). (D) JJN3 cells were transfected with HA-ubiquitin plasmid and incubated in hypoxia overnight before the cells were harvested and IL-32 immunoprecipitation was performed. Protein levels of HA-ubiquitin, IL-32, and GAPDH loading control were evaluated on WB. Total lysate and IP samples from the same membrane are shown with different brightness/contrast. (E) JJN3 cells were incubated overnight in hypoxia before they were stimulated with MG-132 for 4 h and harvested for TUBE assay of ubiquitinylated proteins. The presence of IL-32 and ubiquitin protein in TUBE pulldown was assessed by WB. DUB treatment for reversal of polyubiqutinylation was included to validate ubiquitin/TUBE pulldown. Total lysate and TUBE samples from the same membrane are shown with different brightness/contrast. (F) JJN3 cells were stimulated with 2 μM TAK234 before the cells were harvested, and IL-32 levels were analyzed by WB. (A–F) One representative experiment out of three is shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

TLR-induced NF kappa B signaling promotes IL-32 expression in MM cells. (A) RPMI-8226 cells were stimulated with TLR agonists (for concentrations, see methods) for 4 and 24 hours and IL-32 mRNA expression was assessed by qPCR. The figure shows mean ± SEM of 3 independent experiments. (B) RPMI-8226 cells were stimulated with TLR agonists for 4 and 24 hours and IL-32 protein expression was evaluated by western blot. The figure shows representative western blot of 3 independent experiments. (C) RPMI-8226 cells were harvested at different time-points following LPS stimulation (0.1 µg/mL) and IL-32 mRNA expression was analyzed by qPCR (mean ± SD) and (D) IL-32 protein expression by western blot (E) RPMI-8226 TLR4 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. Figure shows representative western blot (n=3) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (F) RPMI-8226 TLR9 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. The figure shows representative western blot (n=2) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (G) RPMI-8226 cells were stimulated with LPS (0.1 µg/mL) and NG25 (2 µM) or IKK VII (10 µM) for 4 hours. IL-32 mRNA expression (mean ± SEM, n=3) was assessed by qPCR. (H) RPMI-8226 cells were stimulated with LPS, NG25 and IKK VII (concentrations as above) for 4 hours. The figure shows representative western blot (n=3) of IL-32 protein expression. P-values in (A) and (G) are calculated by one-way ANOVA with Dunnett´s multiple comparison test. *p≤ 0.05, **p ≤ 0.001, ****p ≤ 0.0001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36875074), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is degraded through the ubiquitin-proteasome pathway. (A, B) JJN3 cells were treated with 20 µM MG-132 and harvested at the indicated time points. IL-32 protein levels were analyzed by (A) Western blotting, and (B) IL-32 mRNA was assessed by qPCR using GAPDH as housekeeping gene. The bars show the mean RQ of IL-32 ± SD. (C) Confocal images of JJN3 cells treated for 4 h with 100 nM carfilzomib and stained with IL-32 antibody (green) and Hoechst (blue). (D) JJN3 cells were transfected with HA-ubiquitin plasmid and incubated in hypoxia overnight before the cells were harvested and IL-32 immunoprecipitation was performed. Protein levels of HA-ubiquitin, IL-32, and GAPDH loading control were evaluated on WB. Total lysate and IP samples from the same membrane are shown with different brightness/contrast. (E) JJN3 cells were incubated overnight in hypoxia before they were stimulated with MG-132 for 4 h and harvested for TUBE assay of ubiquitinylated proteins. The presence of IL-32 and ubiquitin protein in TUBE pulldown was assessed by WB. DUB treatment for reversal of polyubiqutinylation was included to validate ubiquitin/TUBE pulldown. Total lysate and TUBE samples from the same membrane are shown with different brightness/contrast. (F) JJN3 cells were stimulated with 2 μM TAK234 before the cells were harvested, and IL-32 levels were analyzed by WB. (A–F) One representative experiment out of three is shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is stabilized by deubiquitinases. (A) JJN3 cells were stimulated with PR619 (30 μM during normoxia and hypoxia before the sample was harvested at indicated time points. The figure shows representative WB of IL-32 protein levels of n = 3 independent experiments. (B) JJN3 cells were incubated overnight in hypoxia before they were moved to normoxia for 4 h with and without PR619 stimulation. Cells were harvested, and lysates were processed in the presence of a NEM-DUB inhibitor. Ubiqutinylated and nonubiqutinylated 27 kDA IL-32 proteins were assessed by WB. (C) JJN3 cells were stimulated with a panel of DUB inhibitors (see Supplementary Table S1 for concentrations) for 4 h, and IL-32 protein levels were analyzed by WB. Shown here is the representative WB of n = 3 independent experiments. (D) Human primary T cells isolated from healthy blood donors were treated with CHX (5 µg/ml), MG132 (20 µM), and PR619 (30 µM) and harvested at the indicated time points. Shown here is the representative WB from experiments with n = 3 donors. (E) Human primary T cells isolated from healthy blood donors were cultured overnight in hypoxia before IL-32 protein levels were assessed by WB. A representative WB from experiments with three different donors is shown here. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 protein half-life is regulated by the oxygen sensor ADO. (A) JJN-3 cells were transfected with ADO- and nontargeting Ctrl siRNA. After 24 h, the cells were seeded and cultured overnight in normoxia or hypoxia before being treated with 5 μg/ml CHX and the IL-32 CHX chase assay in normoxia and hypoxia. One representative WB of IL-32 and ADO siRNA-treated cells of n = 5 independent experiments is shown. (B) JJN-3 cells were transfected with ADO and nontargeting Ctrl siRNA. After being transfected for 24 h, the cells were cultured overnight in hypoxia before being treated with 5 µg/ml CHX and reoxygenized in normoxic culture conditions. Cells were harvested at indicated time points. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

TLR-induced NF kappa B signaling promotes IL-32 expression in MM cells. (A) RPMI-8226 cells were stimulated with TLR agonists (for concentrations, see methods) for 4 and 24 hours and IL-32 mRNA expression was assessed by qPCR. The figure shows mean ± SEM of 3 independent experiments. (B) RPMI-8226 cells were stimulated with TLR agonists for 4 and 24 hours and IL-32 protein expression was evaluated by western blot. The figure shows representative western blot of 3 independent experiments. (C) RPMI-8226 cells were harvested at different time-points following LPS stimulation (0.1 µg/mL) and IL-32 mRNA expression was analyzed by qPCR (mean ± SD) and (D) IL-32 protein expression by western blot (E) RPMI-8226 TLR4 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. Figure shows representative western blot (n=3) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (F) RPMI-8226 TLR9 WT (mock) and KO cell lines were stimulated with LPS and CpG for 24 hours. The figure shows representative western blot (n=2) of IL-32 protein and qPCR analysis of IL-32 mRNA (mean ± SD, n=1) (G) RPMI-8226 cells were stimulated with LPS (0.1 µg/mL) and NG25 (2 µM) or IKK VII (10 µM) for 4 hours. IL-32 mRNA expression (mean ± SEM, n=3) was assessed by qPCR. (H) RPMI-8226 cells were stimulated with LPS, NG25 and IKK VII (concentrations as above) for 4 hours. The figure shows representative western blot (n=3) of IL-32 protein expression. P-values in (A) and (G) are calculated by one-way ANOVA with Dunnett´s multiple comparison test. *p≤ 0.05, **p ≤ 0.001, ****p ≤ 0.0001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36875074), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is stabilized by deubiquitinases. (A) JJN3 cells were stimulated with PR619 (30 μM during normoxia and hypoxia before the sample was harvested at indicated time points. The figure shows representative WB of IL-32 protein levels of n = 3 independent experiments. (B) JJN3 cells were incubated overnight in hypoxia before they were moved to normoxia for 4 h with and without PR619 stimulation. Cells were harvested, and lysates were processed in the presence of a NEM-DUB inhibitor. Ubiqutinylated and nonubiqutinylated 27 kDA IL-32 proteins were assessed by WB. (C) JJN3 cells were stimulated with a panel of DUB inhibitors (see Supplementary Table S1 for concentrations) for 4 h, and IL-32 protein levels were analyzed by WB. Shown here is the representative WB of n = 3 independent experiments. (D) Human primary T cells isolated from healthy blood donors were treated with CHX (5 µg/ml), MG132 (20 µM), and PR619 (30 µM) and harvested at the indicated time points. Shown here is the representative WB from experiments with n = 3 donors. (E) Human primary T cells isolated from healthy blood donors were cultured overnight in hypoxia before IL-32 protein levels were assessed by WB. A representative WB from experiments with three different donors is shown here. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

IL-32 is stabilized by deubiquitinases. (A) JJN3 cells were stimulated with PR619 (30 μM during normoxia and hypoxia before the sample was harvested at indicated time points. The figure shows representative WB of IL-32 protein levels of n = 3 independent experiments. (B) JJN3 cells were incubated overnight in hypoxia before they were moved to normoxia for 4 h with and without PR619 stimulation. Cells were harvested, and lysates were processed in the presence of a NEM-DUB inhibitor. Ubiqutinylated and nonubiqutinylated 27 kDA IL-32 proteins were assessed by WB. (C) JJN3 cells were stimulated with a panel of DUB inhibitors (see Supplementary Table S1 for concentrations) for 4 h, and IL-32 protein levels were analyzed by WB. Shown here is the representative WB of n = 3 independent experiments. (D) Human primary T cells isolated from healthy blood donors were treated with CHX (5 µg/ml), MG132 (20 µM), and PR619 (30 µM) and harvested at the indicated time points. Shown here is the representative WB from experiments with n = 3 donors. (E) Human primary T cells isolated from healthy blood donors were cultured overnight in hypoxia before IL-32 protein levels were assessed by WB. A representative WB from experiments with three different donors is shown here. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37313466), licensed under a CC-BY license. Not internally tested by R&D Systems.

• Reactivity: Hu
• Applications: WB
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Unconjugated
• Concentration: LYOPH

IL-32 Antibody Summary

• Immunogen: E. coli-derived recombinant human IL‑32 alpha
  Cys2-Lys131
  Accession # NP_001012651
• Specificity: Detects human IL-32 in direct ELISAs and Western blots.
• Source: N/A
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Gene: IL32
• Purity Statement: Antigen Affinity-purified

Applications/Dilutions

• Dilutions:
  • Western Blot 0.1 ug/mL

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
• Preservative: No Preservative
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute at 0.2 mg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for IL-32 Antibody

• IL32
• IL-32
• IL-32alpha
• IL-32beta
• interleukin 32
• interleukin-32 theta
• interleukin-32
• natural killer cell transcript 4
• Natural killer cells protein 4
• NK4
• NK4IL-32delta
• TAIF
• TAIFa
• TAIFb
• TAIFc
• TAIFd
• TAIFIL-32gamma
• Tumor necrosis factor alpha-inducing factor

Background

Interleukin 32 (IL-32) is an N-glycosylated cytokine that is upregulated by inflammatory stimulation in monocytes, NK cells, epithelial cells, and pancreatic myofibroblasts (1-5). It cooperates with these stimuli to promote the expression of other proinflammatory molecules such as TNF-alpha , IL-6, IL-1 beta , IL-1 alpha , and CXCL8/IL‑8 (5-7). The longest of several IL-32 splicing variants is the 20-25 kDa gamma isoform which is also known as natural killer cell transcript 4 (NK4) (8, 9). The alpha isoform (IL-32 alpha ) lacks a portion of the putative signal peptide as well as 57 aa from the C-terminal region. IL-32 alpha is less potent than IL-32 beta , gamma , or δ at inducing the expression of proinflammatory molecules in peripheral blood mononuclear cells (PBMC) (8, 10). Neutrophil-derived Proteinase 3 (PR3) cleaves IL-32 alpha between Thr57 and Val58, a cleavage site that is retained in other IL-32 isoforms (11). The N-terminal fragment of PR3-cleaved IL-32 alpha shows increased potency at inducing CXCL2/MIP-2 and CXCL8 expression in PBMC relative to uncleaved IL-32 alpha (11, 12). IL-32 is highly expressed by colonic epithelial cells in inflammatory bowel disease and Crohn’s disease, rheumatoid arthritis synovium, and ductal epithelial cells in chronic pancreatitis and pancreatic cancer (5, 13-15). IL-32 inhibits HIV-1 replication in vitro, and it is elevated in the serum of HIV-1 patients (16, 17).

1. Netea, M.G. et al. (2006) PloS Med. 3:e277.
2. Nold-Petry, C.A. et al. (2009) Proc. Natl. Acad. Sci. USA 106:3883.
3. Li, W. et al. (2009) Eur. J. Immunol. 39:1019.
4. Nishida, A. et al. (2008) Am. J. Physiol. Gastrointest. Liver Physiol. 294:G831.
5. Shoda, H. et al. (2006) Arthritis Res. Ther. 8:R166.
6. Netea, M.G. et al. (2005) Proc. Natl. Acad. Sci. USA 102:16309.
7. Hong, J. et al. (2010) Cytokine 49:171.
8. Kim, S-H. et al. (2005) Immunity 22:131.
9. Dahl, C.A. et al. (1992) J. Immunol. 148:597.
10. Choi, J-D. et al. (2009) Immunology 126:535.
11. Novick, D. et al. (2006) Proc. Natl. Acad. Sci. USA 103:3316.
12. Kim, S. et al. (2008) BMB Rep. 41:814.
13. Shioya, M. et al. (2007) Clin. Exp. Immunol. 149:480.
14. Joosten, L.A.B. et al. (2006) Proc. Natl. Acad. Sci. USA 103:3298.
15. Nishida, A. et al. (2009) J. Biol. Chem. 284:17868.
16. Rasool, S.T. et al. (2008) Immunol. Lett. 117:161.
17. Nold, M.F. et al. (2008) J. Immunol. 181:557.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for IL-32 Antibody (AF3040)(18)

Publications using AF3040

• Martin Kastnes, Kristin Roseth Aass, Siri Anshushaug Bouma, Charlotte Årseth, Muhammad Zahoor, Mariia Yurchenko et al. The pro-tumorigenic cytokine IL-32 has a high turnover in multiple myeloma cells due to proteolysis regulated by oxygen-sensing cysteine dioxygenase and deubiquitinating enzymes Frontiers in Oncology 5/29/2023 [PMID: 37313466]
• Kristin Roseth Aass, Synne Stokke Tryggestad, Robin Mjelle, Martin H. Kastnes, Tonje Marie Vikene Nedal, Kristine Misund et al. IL-32 is induced by activation of toll-like receptors in multiple myeloma cells Frontiers in Immunology 2/16/2023 [PMID: 36875074]
• Kristin Roseth Aass, Robin Mjelle, Martin H. Kastnes, Synne S. Tryggestad, Luca M. van den Brink, Ingrid Aass Roseth et al. Intracellular IL-32 regulates mitochondrial metabolism, proliferation, and differentiation of malignant plasma cells iScience 1/21/2022 [PMID: 35005550]
• JC Dos Santos, AM Barroso de, MV Teodoro Si, B Cirovic, LCJ de Bree, MSMA Damen, SJCFM Moorlag, RS Gomes, MM Helsen, M Oosting, ST Keating, A Schlitzer, MG Netea, F Ribeiro-Di, LAB Joosten β-Glucan-Induced Trained Immunity Protects against Leishmania braziliensis Infection: a Crucial Role for IL-32 Cell Rep, 2019-09-03;28(10):2659-2672.e6. 2019-09-03 [PMID: 31484076] (IHC-P, Transgenic Mouse)
• Yvette J. E. Sloot, Katrin Rabold, Thomas Ulas, Dennis M. De Graaf, Bas Heinhuis, Kristian Händler et al. Interplay between thyroid cancer cells and macrophages: effects on IL-32 mediated cell death and thyroid cancer cell migration Cell Oncol (Dordr) 10/1/2019 [PMID: 31201646]
• Yvette J. E. Sloot, Katrin Rabold, Thomas Ulas, Dennis M. De Graaf, Bas Heinhuis, Kristian Händler et al. Interplay between thyroid cancer cells and macrophages: effects on IL-32 mediated cell death and thyroid cancer cell migration Cell Oncol (Dordr) 2019-10-01 [PMID: 31201646] (Western Blot, Human)
• MSMA Damen, K Schraa, L Tweehuysen, AA den Broede, MG Netea, CD Popa, LAB Joosten Genetic variant in IL-32 is associated with the ex vivo cytokine production of anti-TNF treated PBMCs from rheumatoid arthritis patients Sci Rep, 2018-09-19;8(1):14050. 2018-09-19 [PMID: 30232372] (Human)
• RJ Palstra, E de Crignis, MD Röling, T van Staver, TW Kan, W van Ijcken, YM Mueller, PD Katsikis, T Mahmoudi Allele-specific long-distance regulation dictates IL-32 isoform switching and mediates susceptibility to HIV-1 Sci Adv, 2018-02-21;4(2):e1701729. 2018-02-21 [PMID: 29507875] (Western Blot, Human)
• Muhammad Zahoor, Marita Westhrin, Kristin Roseth Aass, Siv Helen Moen, Kristine Misund, Katarzyna Maria Psonka-Antonczyk et al. Hypoxia promotes IL-32 expression in myeloma cells, and high expression is associated with poor survival and bone loss Blood Advances 12/26/2017 [PMID: 29296919]
• Muhammad Zahoor, Marita Westhrin, Kristin Roseth Aass, Siv Helen Moen, Kristine Misund, Katarzyna Maria Psonka-Antonczyk et al. Hypoxia promotes IL-32 expression in myeloma cells, and high expression is associated with poor survival and bone loss Blood Advances 2017-12-26 [PMID: 29296919] (Western Blot, Human)
• Kang J, Park Y, Kim M, Lee D, Bak Y, Ham S, Park S, Hong J, Yoon D Interleukin (IL)-32beta-mediated CCAAT/enhancer-binding protein alpha (C/EBPalpha) phosphorylation by protein kinase Cdelta (PKCdelta) abrogates the inhibitory effect of C/EBPalpha on IL-10 production. J Biol Chem, 2013-06-30;288(33):23650-8. 2013-06-30 [PMID: 23814099] (Immunoprecipitation, Human)
• Sakitani K, Hirata Y, Hayakawa Y, Serizawa T, Nakata W, Takahashi R, Kinoshita H, Sakamoto K, Nakagawa H, Akanuma M, Yoshida H, Maeda S, Koike K Role of interleukin-32 in Helicobacter pylori-induced gastric inflammation. Infect Immun, 2012-08-13;80(11):3795-803. 2012-08-13 [PMID: 22890997] (Western Blot, Human)
• Marcondes AM, Li X, Tabellini L, Bartenstein M, Kabacka J, Sale GE, Hansen JA, Dinarello CA, Deeg HJ Inhibition of IL-32 activation by alpha-1 antitrypsin suppresses alloreactivity and increases survival in an allogeneic murine marrow transplantation model. Blood, 2011-09-06;118(18):5031-9. 2011-09-06 [PMID: 21900190] (Western Blot, Human)
• Heinhuis B, Koenders MI, van de Loo FA, Netea MG, van den Berg WB, Joosten LA Inflammation-dependent secretion and splicing of IL-32{gamma} in rheumatoid arthritis. Proc. Natl. Acad. Sci. U.S.A., 2011-03-07;108(12):4962-7. 2011-03-07 [PMID: 21383200] (ELISA Development, Human)
• Zepp JA, Nold-Petry CA, Dinarello CA, Nold MF Protection from RNA and DNA viruses by IL-32. J. Immunol., 2011-02-23;186(7):4110-8. 2011-02-23 [PMID: 21346229] (Electrochemiluminescent Assay, Human)
• Hasegawa H, Thomas HJ, Schooley K, Born TL Native IL-32 is released from intestinal epithelial cells via a non-classical secretory pathway as a membrane-associated protein. Cytokine, 2011-01-01;53(1):74-83. 2011-01-01 [PMID: 20926308] (Western Blot, Human)
• Nishida A, Andoh A, Inatomi O, Fujiyama Y Interleukin-32 expression in the pancreas. J. Biol. Chem., 2009-04-21;284(26):17868-76. 2009-04-21 [PMID: 19386602] (IHC, Human)
• Shioya M, Nishida A, Yagi Y, Ogawa A, Tsujikawa T, Kim-Mitsuyama S, Takayanagi A, Shimizu N, Fujiyama Y, Andoh A Epithelial overexpression of interleukin-32alpha in inflammatory bowel disease. Clin. Exp. Immunol., 2007-06-22;149(3):480-6. 2007-06-22 [PMID: 17590175] (IHC, Human)

Review for IL-32 Antibody (AF3040) (1)

Average Rating: 5

(Based on 1 review)

We have 1 review tested in 1 species: Human.

reviewed by: Verified Customer WB Human 01/07/2015

Summary

• Application: Western Blot
• Sample Tested: See PMID 22890997
• Species: Human

Bioinformatics

• Gene Symbol: IL32
• Uniprot:
  • NP_001012651()