Recombinant Human IL-32 beta Protein, CF

Catalog # Availability Size / Price Qty
6769-IL-025
Product Details
Citations (3)
FAQs
Reviews (1)

Recombinant Human IL-32 beta Protein, CF Summary

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.0 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 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
Analysis
Met
Predicted Molecular Mass
23.1 kDa

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

6769-IL

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.
  • 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.
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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
  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.
Long Name
Interleukin 32 beta
Alternate Names
IL32 beta; IL-32 beta; IL32; IL-32alpha; IL-32beta; IL-32delta; IL-32gamma; interleukin 32; NK4; TAIF; TAIFa; TAIFb; TAIFc; TAIFd

Citations for Recombinant Human IL-32 beta Protein, CF

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.

3 Citations: Showing 1 - 3
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  1. M-CSF inhibits anti-HIV-1 activity of IL-32, but they enhance M2-like phenotypes of macrophages.
    Authors: Osman A, Bhuyan F, Hashimoto M, Nasser H, Maekawa T, Suzu S
    J Immunol, 2014;192(11):5083-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Role of interleukin-32 in Helicobacter pylori-induced gastric inflammation.
    Authors: Sakitani K, Hirata Y, Hayakawa Y, Serizawa T, Nakata W, Takahashi R, Kinoshita H, Sakamoto K, Nakagawa H, Akanuma M, Yoshida H, Maeda S, Koike K
    Infect Immun, 2012;80(11):3795-803.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Dendritic Cell-Derived IL-32alpha: A Novel Inhibitory Cytokine of NK Cell Function.
    Authors: Gorvel L, Korenfeld D, Tung T, Klechevsky E
    J Immunol, 0;199(4):1290-1300.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

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Recombinant Human IL-32 beta Protein, CF
By Anonymous on 06/19/2019
Application: Binding assay/Protein-protein interaction