Recombinant Human IL-32α Protein(Trx Tag)

IL-32α

TAIFa;IL-32alpha;IL-32beta;IL-32delta;IL-32gamma;TAIFb;TAIFc;TAIFd;IL32;NK4;TAIF;IL 32alpha;IL 32beta;IL 32delta;IL 32gamma;IL-32;Interleukin 32;Interleukin 32 small;Interleukin 32 theta;Interleukin-32;interleukin-32 eta;Natural killer cell transcript 4;Natural killer cells protein 4;NK 4;OTTHUMP00000236040;OTTHUMP00000236041;OTTHUMP00000236042;OTTHUMP00000236043;OTTHUMP00000236044;OTTHUMP00000236045;OTTHUMP00000236046;OTTHUMP00000236047;OTTHUMP00000236048;OTTHUMP00000236049;OTTHUMP00000236050;OTTHUMP00000236051;OTTHUMP00000236052;OTTHUMP00000236053;OTTHUMP00000236054;OTTHUMP00000241545;OTTHUMP00000241602;OTTHUMP00000241603;OTTHUMP00000241604;OTTHUMP00000241605;OTTHUMP00000241606;OTTHUMP00000241607;OTTHUMP00000241608;OTTHUMP00000241609;OTTHUMP00000241610;OTTHUMP00000241611;OTTHUMP00000241612;Tumor necrosis factor alpha-inducing factor

36.4 kDa

35 kDa

P24001

IL-32 is a recently discovered cytokine that induces various proinflammatory cytokines (TNF-alpha, IL-1beta, IL-6) and chemokines in both human and mouse cells through the NF-kappaB and p38 MAPK inflammatory signal pathways. It is regulated robustly by other major proinflammatory cytokines and is crucial to inflammation and immune responses. Four of the IL-32 isoforms (alpha, beta, gamma, and delta) are the most representative IL-32 transcripts, and the gamma isoform of IL-32 is the most active, although all isoforms are biologically active. IL-32, a cytokine produced mainly by T, natural killer, and epithelial cells induces significant amounts of TNFalpha and MIP-2 and increases the production of both cytokines in a dose-dependent manner. IL-32 has been implicated in inflammatory disorders, Mycobacterium tuberculosis infections, inflammatory bowel disease, and influenza A virus infection, as well as in some autoimmune diseases, such as rheumatoid arthritis, ulcerative colitis, and in the human stomach cancer, human lung cancer, and breast cancer tissues. Thus, IL-32 expression might be valuable as a biomarker for cancer.

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.