Human/Rat IL-32 Antibody Summary
Accession # NP_001012649
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.
Detection of Human and Rat IL‑32 by Western Blot. Western blot shows lysates of Nb2-11 rat lymphoma cell line and U937 human histiocytic lymphoma cell line. PVDF membrane was probed with 1 µg/mL of Rabbit Anti-Human/Rat IL-32 Monoclonal Antibody (Catalog # MAB6769) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). Specific bands were detected for IL-32 at approximately 25 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
IL-32 in Human PBMCs. IL-32 was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) treated or untreated with calcium ionomycin and PMA using Rabbit Anti-Human/Rat IL-32 Monoclonal Antibody (Catalog # MAB6769) at 3 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Rabbit IgG Secondary Antibody (red; Catalog # NL004) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Preparation and Storage
- 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.
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).
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