Recombinant Human IL-32 alpha Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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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) and Polymyxin B. 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 #
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

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
Publications
Read Publications using
3040-IL in the following applications:

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

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.

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Publications for IL-32 alpha (3040-IL)(8)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 2 applications: Bioassay, ELISA Standard.


Filter By Application
Bioassay
(7)
ELISA Standard
(1)
All Applications
Filter By Species
Human
(7)
N/A
(1)
All Species
Showing Publications 1 - 8 of 8.
Publications using 3040-IL Applications Species
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;4(2):e1701729. 2018 [PMID: 29507875] (Bioassay, Human) Bioassay Human
Gorvel L, Korenfeld D, Tung T, Klechevsky E Dendritic Cell-Derived IL-32alpha: A Novel Inhibitory Cytokine of NK Cell Function. J Immunol, 0;199(4):1290-1300. 0 [PMID: 28701509] (Bioassay, Human) Bioassay Human
Victoria Catalán Increased Interleukin-32 Levels in Obesity Promote Adipose Tissue Inflammation and Extracellular Matrix Remodeling: Effect of Weight Loss Diabetes, 2016;65(12):3636-3648. 2016 [PMID: 27630206] (Bioassay, Human) 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;21(17):3969-76. 2015 [PMID: 25944800] (Bioassay, Human) 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;192(11):5083-9. 2014 [PMID: 24748497] (Bioassay, Human) 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, 2014;95(4):631-42. 2014 [PMID: 24295830] (Bioassay, Human) 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;487(7408):505-9. 2012 [PMID: 22763448] (Bioassay, Human) 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;108(12):4962-7. 2011 [PMID: 21383200] (ELISA Standard, N/A) ELISA Standard N/A

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Bioinformatics

Gene Symbol IL32
Entrez
Uniprot