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Purified anti-human IL-32α Antibody

Pricing & Availability
Clone
A15159A (See other available formats)
Regulatory Status
RUO
Other Names
IL-32 alpha, Natural killer cells protein 4 (NK4), Natural killer transcript 4 (NK4), Tumor necrosis factor alpha-inducing factor (TAIF)
Isotype
Mouse IgG2b, κ
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Product Citations
publications
A15159A_PURE_IL-32alpha_Antibody_WB_012017
Total cell lysates (15 µg protein) from NIH3T3, Jurkat, and HeLa (negative control) were resolved by 4-12% Bis-tris gel electrophoresis, transferred to nitrocellulose, and probed with 1 µg/mL purified anti-human IL-32α (clone A15159A) antibody. Proteins were visualized using an HRP goat anti-mouse-IgG secondary antibody (clone Poly4053) and chemiluminescence detection. Direct-Blot™ HRP anti-β-actin (clone 2F1-1) antibody was used as a loading control. M*: protein marker standards with longer exposure time.
  • A15159A_PURE_IL-32alpha_Antibody_WB_012017
    Total cell lysates (15 µg protein) from NIH3T3, Jurkat, and HeLa (negative control) were resolved by 4-12% Bis-tris gel electrophoresis, transferred to nitrocellulose, and probed with 1 µg/mL purified anti-human IL-32α (clone A15159A) antibody. Proteins were visualized using an HRP goat anti-mouse-IgG secondary antibody (clone Poly4053) and chemiluminescence detection. Direct-Blot™ HRP anti-β-actin (clone 2F1-1) antibody was used as a loading control. M*: protein marker standards with longer exposure time.
Cat # Size Price Save
694702 100 µg ¥58,300
Description

IL-32 is a proinflammatory cytokine with both extracellular and intracellular functions. IL-32 was originally identified as a natural killer transcript 4 (NK4). Several isoforms of IL-32 have been identified, and IL-32α is the most abundant. Overexpression of IL-32α in myeloid cell lines enhances natural killer cell-mediated killing, and IL-32 expression can be induced by IL-18 in NK cells. IL-32α can be released by some epithelial cell lines in response to INF-γ, TNF-α, and IL-1β. IL-32 can induce production of various cytokines including TNF-α, IL-1β, IL-8 and IL-6 through NF-κB and p38 MAPK activation. IL-32 works synergistically with IL-17 to induce osteoclast differentiation. Recombinant IL-32α can induce macrophage apoptosis in the presence of M. tuberculosis. Intracellular IL-32α increases IL-6 production by interacting with PKCε and STAT3, which not only increases STAT3 phosphorylation but also enhances STAT3 recruitment to the IL-6 promoter. IL-32 can synergize with NOD1 and NOD2 ligands to induce IL-1β and IL-6 through the caspase I-dependent pathway. IL-32 has been associated with pathogenesis of many chronic inflammatory diseases including rheumatoid arthritis and ulcerative colitis. IL-32 is highly expressed in various cancers including gastric and pancreatic cancer. Studies have suggested that IL-32 can function as an angiogenic factor. In addition, IL-32α expression in liver cells is increased following progression of many liver diseases. Also, IL-32 is involved in the immune response to many viruses including HIV, influenza A, hepatitis B, and papillomavirus.

Product Details
Technical data sheet

Product Details

Verified Reactivity
Human
Antibody Type
Monoclonal
Host Species
Mouse
Immunogen
Recombinant human IL-32α
Formulation
Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
Preparation
The antibody was purified by affinity chromatography.
Concentration
0.5 mg/ml
Storage & Handling
The antibody solution should be stored undiluted between 2°C and 8°C.
Application

WB - Quality tested
Recommended Usage

Each lot of this antibody is quality control tested by Western blotting. For Western blotting, the suggested use of this reagent is 0.5 - 2.0 µg per ml. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

Clone A15159A does not cross-react with mouse (in-house tested).

RRID
AB_2650733 (BioLegend Cat. No. 694702)

Antigen Details

Structure
131 amino acids with a predicted molecular weight of 15 kD.
Distribution
Secreted by T cells, natural killer cells, dendritic cells, and keratinocytes.
Function
IL-32α expression can be induced by IL-18, IL-1β, IFN-γ, IL-12 and IL-17. The activity of IL-32α can be significantly increased by limited cleavage of IL-32α by neutrophil proteinase 3.
Interaction
IL-32α has been reported to interact with neutrophil proteinase 3, PKC, STAT3, integrin and paxilin.
Cell Type
T cells, NK cells, Dendritic cells
Biology Area
Cell Biology, Immunology
Molecular Family
Cytokines/Chemokines
Antigen References

1. Joosten LA, et al. 2013. Cell. Mol. Life Sci. 70:3883.
2. Kang JW, et al. 2012. J. Biol. Chem. 287:35556.
3. Cheon S, et al. 2011. J. Biol. Chem. 286:12049.
4. Nishida A, et al. 2009. J. Biol. Chem. 284:17868.
5. Heinhuis B, et al. 2012. J. Biol. Chem. 287:5733.
6. Novick D, et al. 2006. Proc. Natl. Acad. Sci. USA 103:3316.
7. Shioya M, et al. 2007. Clin. Exp. Immunol. 149:480. 

Gene ID
9235 View all products for this Gene ID
UniProt
View information about IL-32alpha on UniProt.org

Related FAQs

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Go To Top Version: 1    Revision Date: 01/23/2017

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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This data display is provided for general comparisons between formats.
Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors.
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