Human IL-32 Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF3040
Product Details
Citations (4)
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Human IL-32 Biotinylated Antibody Summary

Species Reactivity
Human
Specificity
Detects human IL-32 in Western blots.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
E. coli-derived recombinant human IL‑32 alpha
Cys2-Lys131
Accession # NP_001012651
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human IL‑32

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: IL-32

Interleukin 32 (IL-32) is an N-glycosylated cytokine that is upregulated 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).

References
  1. Netea, M.G. et al. (2006) PloS Med. 3:e277.
  2. Nold-Petry, C.A. et al. (2009) Proc. Natl. Acad. Sci. USA 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. USA 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. USA 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. USA 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.
Long Name
Interleukin 32
Entrez Gene IDs
9235 (Human)
Alternate Names
IL32; IL-32; IL-32alpha; IL-32beta; interleukin 32; interleukin-32 theta; interleukin-32; natural killer cell transcript 4; Natural killer cells protein 4; NK4; NK4IL-32delta; TAIF; TAIFa; TAIFb; TAIFc; TAIFd; TAIFIL-32gamma; Tumor necrosis factor alpha-inducing factor

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Citations for Human IL-32 Biotinylated Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

4 Citations: Showing 1 - 4
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  1. Genetic variant in IL-32 is associated with the ex vivo cytokine production of anti-TNF treated PBMCs from rheumatoid arthritis patients
    Authors: MSMA Damen, K Schraa, L Tweehuysen, AA den Broede, MG Netea, CD Popa, LAB Joosten
    Sci Rep, 2018-09-19;8(1):14050.
    Species: Human
    Sample Types: Cell Culture Supernates
  2. Inflammation-dependent secretion and splicing of IL-32{gamma} in rheumatoid arthritis.
    Authors: Heinhuis B, Koenders MI, van de Loo FA, Netea MG, van den Berg WB, Joosten LA
    Proc. Natl. Acad. Sci. U.S.A., 2011-03-07;108(12):4962-7.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: ELISA Development
  3. Protection from RNA and DNA viruses by IL-32.
    Authors: Zepp JA, Nold-Petry CA, Dinarello CA, Nold MF
    J. Immunol., 2011-02-23;186(7):4110-8.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Electrochemiluminescent Assay
  4. Interleukin-32 expression in the pancreas.
    Authors: Nishida A, Andoh A, Inatomi O, Fujiyama Y
    J. Biol. Chem., 2009-04-21;284(26):17868-76.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Western Blot

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