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Recombinant Human cIAP1/HIAP2 Protein (AVI Tag) (PKSH031263)

All Size Price Qty
100μg $ 680.00
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For research use only.

Synonyms API1, HIAP2, Hiap-2, MIHB, RNF48, c-IAP1, cIAP1
Species Human
Expression Host E.coli
Sequence Glu 144-Leu 356
Accession NP_001157.1
Calculated Molecular Weight 26.5 kDa
Observed Molecular Weight 26.5 kDa
Tag C-Avi
Bio-activity Measured by its ability to inhibit DEVD-AFC cleavage activity in cell extracts activated by addition of cytochrome c and dATP. The IC50 for this effect is typically 25-750 nM.
Purity > 92 % as determined by reducing SDS-PAGE.
Endotoxin Please contact us for more information.
Storage 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.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from sterile 10mM Tris, 5% glycerol, 0.5mM EDTA, 5mM DTT, pH 7.5
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution Please refer to the printed manual for detailed information.
Background The cellular inhibitor of apoptosis protein-1 (cIAP1) is a member of the Inhibitor of Apoptosis family proteinsare (IAP) whose members are characterized by a novel domain of about 70 amino acids termed baculoviral IAP repeats (BIRs). The BIR domains of cIAP1 and cIAP2 bind to caspases, the key effector proteases of apoptosis. The IAP protein family which can enhance cell survival are crucial regulators of programmed cell death. Both cIAP1 and cIAP2 are the E3 ubiquitin protein isopeptide ligases for Smac, taking part in promoting cancer survival through functioning as E3 ubiqitin ligases. Removal of cIAP1 by genetic deletion may result in NF-&kappa;B signaling activation that induces TNF&alpha; production and in killing sensitive tumor cells through enhanced TNF-R1 death-receptor signaling and caspase 8 activation. The substrate-dependent E3 activity of cIAPs is mediated by their RING domains and is dependent on the specific interactions between cIAPs and Smac. cIAP1 and cIAP2 are also reported to be regulators of NF-kB activation upon TNF&alpha;treatment.
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