Human/Rat IL-32 beta 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 beta 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 beta Monoclonal Antibody (Catalog # MAB6769) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). Specific bands were detected for IL‑32 beta at approximately 25 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
IL-32 beta in Human PBMCs. IL‑32 beta 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 beta 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.
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).
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