Recombinant Human IL-32 alpha Protein, CF

Catalog # Availability Size / Price Qty
3040-IL-050
Product Details
Citations (8)
FAQs
Supplemental Products
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Recombinant Human IL-32 alpha Protein, CF Summary

Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 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 cellsunder serum free conditions in the presence of muramyl dipeptide (MDP). Netea, M.G. et al. (2005) Proc. Nat. Acad. Sci. 102:16309. The ED50 for this effect is 2‑12 μg/mL.
Source
E. coli-derived human IL-32 alpha protein
Cys2-Lys131
Accession #
N-terminal Sequence
Analysis
Cys2
Predicted Molecular Mass
14.9 kDa
SDS-PAGE
18.8 kDa, reducing conditions

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.

3040-IL

Formulation Lyophilized from a 0.2 μm filtered solution in PBS and DTT.
Reconstitution Reconstitute at 200 μg/mL in PBS.
Shipping The product is shipped with polar packs. 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: IL-32 alpha

Interleukin 32 (IL-32) is an N-glycosylated cytokine that is up‑regulated 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. 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. 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. 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. 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 alpha
Entrez Gene IDs
9235 (Human)
Alternate Names
IL32 alpha; IL-32 alpha; IL32; IL-32alpha; IL-32beta; IL-32delta; IL-32gamma; interleukin 32; NK4; TAIF; TAIFa; TAIFb; TAIFc; TAIFd

Citations for Recombinant Human IL-32 alpha 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.

8 Citations: Showing 1 - 8
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  1. Allele-specific long-distance regulation dictates IL-32 isoform switching and mediates susceptibility to HIV-1
    Authors: RJ Palstra, E de Crignis, MD Röling, T van Staver, TW Kan, W van Ijcken, YM Mueller, PD Katsikis, T Mahmoudi
    Sci Adv, 2018;4(2):e1701729.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Increased Interleukin-32 Levels in Obesity Promote Adipose Tissue Inflammation and Extracellular Matrix Remodeling: Effect of Weight Loss
    Authors: Victoria Catalán
    Diabetes, 2016;65(12):3636-3648.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Differential Expression of Immune-Regulatory Genes Associated with PD-L1 Display in Melanoma: Implications for PD-1 Pathway Blockade.
    Authors: Taube J, Young G, McMiller T, Chen S, Salas J, Pritchard T, Xu H, Meeker A, Fan J, Cheadle C, Berger A, Pardoll D, Topalian S
    Clin Cancer Res, 2015;21(17):3969-76.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Molecular mechanisms regulating the synergism between IL-32gamma and NOD for the activation of eosinophils.
    Authors: Wong C, Dong J, Lam C
    J Leukoc Biol, 2014;95(4):631-42.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. 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
  6. Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
    Authors: Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J
    Nature, 2012;487(7408):505-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. 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;108(12):4962-7.
    Species: N/A
    Sample Types: N/A
    Applications: ELISA (Standard)
  8. 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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