Anti-XIAP (MIHA/ILP-a) (Human) mAb

WB - 1 ug/mL (chemiluminescence detection system)

Caspase, related to ICE and to CED- 3, play central roles as effectors of apoptosis. Ablation of caspase activity is attained by p35 from baculovirus and CrmA from cowpox, which appear to be suicide inactivators, strongly inhibiting caspase activity. Overexpression of there caspase inhibitors in insect, nematoda and mammalian cells results in resistance to apoptotic stimuli, demonstrating that components of the apoptotic pathway are highly conserved throughout evolution, and leading to the speculation that mammalian functional equivalents of these protease inhibitors may exist. The inhibitor of apoptosis proteins (IAPs) are a family of anti-apoptotic proteins that are conserved across species. Four IAPs have been identified in mammal; NAIP, cIAP1/HIAP2/hMIHB, cIAP2/HIAP1/hMIHC, XIAP/hILP. A prototype of the human IAPs is the XIAP, with a 1.5 kb coding region corresponding to a 55 kDa protein. XIAP can directly inhibit two members of the cell death protease family, caspase-3 and -7.

1 mg/mL

1.0 mg/mL in PBS/50% glycerol, pH 7.2

Human: 331 Mouse: 11798

Full-length recombinant human XIAP protein

This antibody reacts with XIAP on Western blotting. 2F1 recognizes C-terminal region of XIAP (352-449 aa) and detects 55 kDa of XIAP on Western Blot using total cell lysate from human or mouse cell line, for example, Jurkat, Raji, NIH/3T3, etc.

1 year

This antibody was purified from hybridoma (clone 2F1) supernatant using protein A agarose. This hybridoma was established by fusion of mouse myeloma cell P3U1 with Balb/c mouse splenocyte immunized with the full length recombinant XIAP protein (1-497 aa).

XIAP