Recombinant Human IL-32 gamma Protein, CF

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

Recombinant Human IL-32 gamma Protein, CF Summary

• Details of Functionality: Measured by its ability to induce TNF-alpha secretion by RAW 264.7 mouse monocyte/macrophage cells under serum free conditions in the presence of 10 µg/mL of Polymyxin B. Kim, S.H. et al. (2005) Immunity 22:131. The ED₅₀ for this effect is 30-180 ng/mL.
• Source: E. coli-derived human IL-32 gamma protein
  

  MNHKVHHHHHH	Human IL-32 gamma (Met1 - Lys234) Accession # P24001
  N-terminus	C-terminus

• Accession #: P24001
• N-terminal Sequence: Met
• Protein/Peptide Type: Recombinant Proteins
• Gene: IL32
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 28.1 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.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 2 weeks, 2 to 8 °C under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in HEPES, NaCl, DTT and CHAPS.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain

Notes

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

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

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

Background

Interleukin-32 gamma (IL-32 gamma ), a proinflammatory cytokine previously termed natural killer cells transcript 4 (NK4) (also tumor necrosis factor alpha (TNF alpha ) -inducing factor), is a 27 kDa, secreted glycoprotein that belongs to no known cytokine family (1). Little is known about it. However, because it has the ability to induce proinflammatory cytokines such as TNF alpha and IL-8 in THP-1 cells, and activates typical cytokine signaling pathways involving NF-kappa B and p38, IL-32 is considered to be a cytokine (2). Human IL-32 gamma is 234 amino acids (aa) in length (1). It contains a 30 aa signal sequence, plus a 204 aa mature region that possesses three potential myristoylation sites and one potential N-linked glycosylation site (1, 2). IL-32 gamma represents the standard protein, and is the first isoform. In addition, there are five potential alternate splice forms (3). IL-32 alpha lacks two of the splicing variant regions found in IL-32 gamma (aa 19 - 64 and aa 154 - 210). IL-32 beta is missing aa 19 - 64, and IL-32δ is missing aa 1 - 10 and aa 19 - 64. IL-32 epsilon and IL-32 zeta are novel isoforms that have not yet been characterized. Human IL-32 gamma is active in mouse cells (2). No rodent orthologs have been reported. No putative IL-32 receptor has been found, but using the isoform IL-32 alpha , the protein proved to bind to proteinase 3 (PR3) (4, 5). IL-32 is involved in activation-induced cell death in T cells (3) and is highly expressed in tissues in a number of disease states including the synovial tissue in rheumatoid arthritis (5, 6) and human colon epithelial tissue in Crohn’s disease (5). Using siRNA to endogenous IL-32 in primary human blood monocytes, there were significant decreases (greater than 50%) in IFN-gamma, TNF, and IL-6, suggesting that endogenous IL-32 is upstream in the cytokine cascade in monocytes (7). Increased levels of IL-32 during human immunodeficiency virus (HIV) infection may play a protective role by suppressing HIV replication (8). In addition, mycobacteria species are potent stimuli for the production of IL-32 from human monocytes and macrophages (9).

1. Dahl, C. et al. (1992) J. Immunol. 148:597.
2. Kim, S-H. et al. (2005) Immunity 22:131.
3. Goda, C. et al. (2006) Int. Immunol. 18:233.
4. Novick, D. et al. (2006) Proc. Natl. Acad. Sci. USA 103:3316.
5. Dinarello C. and S-H. Kim (2006) Ann. Rheum. Dis. 65(Suppl III):iii61.
6. Joosten, L. et al. (2006) Proc. Natl. Acad. Sci. USA 103:3298.
7. Nold M. F. et al. (2008) J. Immuno. 180: 557.
8. Rasool, S. T. et al. (2008) Immunol Lett. 117:161.
9. Netea, M. et al. (2006) PloS Med. 3:1310.

Publications for IL-32 gamma (4690-IL/CF)(4)

Publications using 4690-IL/CF

• Soussi, S;Maione, AS;Lefèvre, L;Pizzinat, N;Iacovoni, J;Gonzalez-Fuentes, I;Cussac, D;Iengo, L;Santin, Y;Tundo, F;Tondo, C;Pompilio, G;Parini, A;Douin-Echinard, V;Sommariva, E; Analysis of effector/memory regulatory T cells from arrhythmogenic cardiomyopathy patients identified IL-32 as a novel player in ACM pathogenesis Cell death & disease 2025-02-11 [PMID: 39934117] (Bioassay, Human)
• GE Vezeau, LR Gadila, HM Salis Automated design of protein-binding riboswitches for sensing human biomarkers in a cell-free expression system Nature Communications, 2023-04-27;14(1):2416. 2023-04-27 [PMID: 37105971] (Bioassay, 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 2017-12-26 [PMID: 29296919] (Bioassay, Human)
• Nold-Petry C, Rudloff I, Baumer Y, Ruvo M, Marasco D, Botti P, Farkas L, Cho S, Zepp J, Azam T, Dinkel H, Palmer B, Boisvert W, Cool C, Taraseviciene-Stewart L, Heinhuis B, Joosten L, Dinarello C, Voelkel N, Nold M IL-32 promotes angiogenesis. J Immunol, 2013-12-11;192(2):589-602. 2013-12-11 [PMID: 24337385] (In Vivo, Mouse)

Bioinformatics

• Gene Symbol: IL32
• Uniprot:
  • P24001()