Recombinant Human IL-32 beta Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human IL-32 beta 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 10-50 ng/mL.
Source
E. coli-derived human IL-32 beta protein
MNHKVHHHHHH Human IL-32 beta
(Met1-Lys188)
Accession # NP_001012649
N-terminus C-terminus
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
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

Theoretical MW
23.1 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.
Publications
Read Publications using
6769-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, -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °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 beta Protein, CF

  • IL32 beta
  • IL-32 beta
  • 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 vascular endothelial cells as well as in activated T cells (1‑6). It cooperates with inflammatory 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 (5‑9). The longest of several IL‑32 splicing variants is the 234 amino acid gamma isoform which is also known as natural killer cell transcript 4 (NK4) (9). The 25 kDa beta isoform (IL‑32 beta ) lacks aa 19‑64 including a portion of the putative signal peptide. Neutrophil‑derived Proteinase 3 (PR3) cleaves IL‑32 alpha between Thr57 and Val58, a cleavage site that is retained in other IL‑32 isoforms (10). The alpha, beta, gamma, delta, epsilon, and zeta isoforms show different degrees of antiviral activity against influenza virus replication with IL‑32 gamma being the most potent (11). 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 (6, 12‑14). IL‑32 inhibits HIV‑1 replication in vitro, and it is elevated in the serum of HIV‑1 patients (15, 16).
  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. Goda, C. et al. (2006) Int. Immunol. 18:233.
  5. Choi, J.-D. et al. (2009) Immunology 126:535.
  6. Shoda, H. et al. (2006) Arthritis Res. Ther. 8:R166.
  7. Netea, M.G. et al. (2005) Proc. Natl. Acad. Sci. 102:16309.
  8. Hong, J. et al. (2010) Cytokine 49:171.
  9. Kim, S.-H. et al. (2005) Immunity 22:131.
  10. Novick, D. et al. (2006) Proc. Natl. Acad. Sci. 103:3316.
  11. Li, W. et al. (2010) J. Immunol. 185:5056.
  12. Shioya, M. et al. (2007) Clin. Exp. Immunol. 149:480.
  13. Joosten, L.A.B. et al. (2006) Proc. Natl. Acad. Sci. 103:3298.
  14. Nishida, A. et al. (2009) J. Biol. Chem. 284:17868.
  15. Rasool, S.T. et al. (2008) Immunol. Lett. 117:161.
  16. Nold, M.F. et al. (2008) J. Immunol. 181:557.

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