Recombinant Human IL-32 alpha Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-32 alpha Protein, CF Summary

• Details of Functionality: Measured by its ability to induce TNF-alpha secretion by RAW 264.7 mouse monocyte/macrophage cellsunder serum free conditions in the presence of muramyl dipeptide (MDP). Netea, M.G. et al. (2005) Proc. Nat. Acad. Sci. 102:16309. The ED₅₀ for this effect is 2‑12 μg/mL.
• Source: E. coli-derived human IL-32 alpha protein
  Cys2-Lys131
• Accession #: AAS80146
• N-terminal Sequence: Cys2
• Protein/Peptide Type: Recombinant Proteins
• Gene: IL32
• Purity: >85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 14.9 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 18.8 kDa, reducing conditions

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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS and DTT.
• Purity: >85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 200 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human IL-32 alpha Protein, CF

• IL32 alpha
• IL-32 alpha
• IL32
• IL-32alpha
• IL-32beta
• IL-32delta
• IL-32gamma
• interleukin 32
• NK4
• TAIF
• TAIFa
• TAIFb
• TAIFc
• TAIFd

Background

Interleukin 32 (IL-32) is an N-glycosylated cytokine that is up‑regulated 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. 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. 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. 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. 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.

Publications for IL-32 alpha (3040-IL)(12)

Publications using 3040-IL

• K Garofano, K Rashid, M Smith, C Brantner, S Suwunnakor, D Diemert, O Gordon, A Horvath, S Khan, A Popratilof, J Rhim, A Sidahmed, SB Maggirwar, TJ O'Brien, MA Perera, NH Lee Prostate cancer cell-platelet bidirectional signaling promotes calcium mobilization, invasion and apoptotic resistance via distinct receptor-ligand pairs Scientific Reports, 2023-02-17;13(1):2864. 2023-02-17 [PMID: 36806315] (Bioassay, Human)
• HJ Kim, SH Kim, YS Oh, SR Lee, HD Chae Dienogest May Reduce Estradiol- and Inflammatory Cytokine-Induced Cell Viability and Proliferation and Inhibit the Pathogenesis of Endometriosis: A Cell Culture- and Mouse Model-Based Study Biomedicines, 2022-11-21;10(11):. 2022-11-21 [PMID: 36428561] (Cell Culture, Human)
• A Conod, M Silvano, A Ruiz I Alt On the origin of metastases: Induction of pro-metastatic states after impending cell death via ER stress, reprogramming, and a cytokine storm Cell Reports, 2022-03-08;38(10):110490. 2022-03-08 [PMID: 35263600] (Bioassay, Human)
• J Zhang, X Sun, L Zhong, B Shen IL-32 exacerbates adenoid hypertrophy via activating NLRP3-mediated cell pyroptosis, which promotes inflammation Molecular Medicine Reports, 2021-01-26;23(3):. 2021-01-26 [PMID: 33495843] (Bioassay, Human)
• T Gruber, M Kremenovic, H Sadozai, N Rombini, L Baeriswyl, F Maibach, RL Modlin, M Gilliet, D von Werdt, RE Hunger, SM Seyed Jafa, G Parisi, G Abril-Rodr, A Ribas, M Schenk IL-32&amp;gamma potentiates tumor immunity in melanoma JCI Insight, 2020-09-17;5(18):. 2020-09-17 [PMID: 32841222] (Bioassay, Mouse)
• 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] (Bioassay, Human)
• Victoria Catalán Increased Interleukin-32 Levels in Obesity Promote Adipose Tissue Inflammation and Extracellular Matrix Remodeling: Effect of Weight Loss Diabetes, 2016-09-14;65(12):3636-3648. 2016-09-14 [PMID: 27630206] (Bioassay, Human)
• Taube J, Young G, McMiller T, Chen S, Salas J, Pritchard T, Xu H, Meeker A, Fan J, Cheadle C, Berger A, Pardoll D, Topalian S Differential Expression of Immune-Regulatory Genes Associated with PD-L1 Display in Melanoma: Implications for PD-1 Pathway Blockade. Clin Cancer Res, 2015-05-05;21(17):3969-76. 2015-05-05 [PMID: 25944800] (Bioassay, Human)
• Osman A, Bhuyan F, Hashimoto M, Nasser H, Maekawa T, Suzu S M-CSF inhibits anti-HIV-1 activity of IL-32, but they enhance M2-like phenotypes of macrophages. J Immunol, 2014-04-18;192(11):5083-9. 2014-04-18 [PMID: 24748497] (Bioassay, Human)
• Wong C, Dong J, Lam C Molecular mechanisms regulating the synergism between IL-32gamma and NOD for the activation of eosinophils. J Leukoc Biol, 2013-12-02;95(4):631-42. 2013-12-02 [PMID: 24295830] (Bioassay, Human)
• Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012-07-26;487(7408):505-9. 2012-07-26 [PMID: 22763448] (Bioassay, 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 (Standard))

Bioinformatics

• Gene Symbol: IL32
• Uniprot:
  • AAS80146()