Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.1 EU per 1 μg of the protein by the LAL method.
Activity
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 ED 50 for this effect is 10-50 ng/mL.
Source
E. coli-derived
MNHKVHHHHHH Human IL-32 beta
(Met1-Lys188)
Accession # NP_001012649N-terminus C-terminus Accession #
N-terminal Sequence
AnalysisMet
Predicted Molecular Mass
23.1 kDa
SDS-PAGE
28 kDa & some aggregates, reducing conditions
6769-IL |
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Formulation Supplied as a 0.2 μm filtered solution in HEPES, NaCl, DTT and CHAPS. | ||
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: IL-32 beta
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).
References:
Netea, M.G. et al. (2006) PloS Med. 3:e277.
Nold-Petry, C.A. et al. (2009) Proc. Natl. Acad. Sci. 106:3883.
Li, W. et al. (2009) Eur. J. Immunol. 39:1019.
Goda, C. et al. (2006) Int. Immunol. 18:233.
Choi, J.-D. et al. (2009) Immunology 126:535.
Shoda, H. et al. (2006) Arthritis Res. Ther. 8:R166.
Netea, M.G. et al. (2005) Proc. Natl. Acad. Sci. 102:16309.
Hong, J. et al. (2010) Cytokine 49:171.
Kim, S.-H. et al. (2005) Immunity 22:131.
Novick, D. et al. (2006) Proc. Natl. Acad. Sci. 103:3316.
Li, W. et al. (2010) J. Immunol. 185:5056.
Shioya, M. et al. (2007) Clin. Exp. Immunol. 149:480.
Joosten, L.A.B. et al. (2006) Proc. Natl. Acad. Sci. 103:3298.
Nishida, A. et al. (2009) J. Biol. Chem. 284:17868.
Rasool, S.T. et al. (2008) Immunol. Lett. 117:161.
Nold, M.F. et al. (2008) J. Immunol. 181:557.
Long Name:
Interleukin 32 beta
Alternate Names:
IL32 beta; IL-32 beta
