CARP2, SUMO-His-tags Recombinant

Catalog #
81050
$465 *
Size: 25 µg
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*US Pricing only. For international pricing, please contact your local distributor.
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Description

Human CARP2 recombinant protein (Genbank Accession No. NP_476519), full length with N-terminal SUMO- and His-tags, expressed in E. coli.

Synonyms
RFFL, ring finger and FYVE-like domain containing 1
Product Info
Storage and Usage
Citations
Species
Human
Host Species/Expression System
E. coli
Purity
≥95% by SDS-PAGE
Format
Aqueous buffer solution
Formulation
50 mM Tris Buffer, pH 7.6, 150 mM NaCl, 10% glycerol
MW
41 kDa
Amino Acids
full length
Biological Activity
Typical enzyme concentration of 100 nM - 5 mM is used for in vitro conjugation, depending on conditions.
Genbank #
NP_476519
UniProt #
O75493
Tag(s)
N-terminal SUMO-His-tags
Background
CARP2 (caspase 8/10 associated RING protein 2) is a RING-domain E3 (ubiquitin protein ligase) that is involved in the conjugation of ubiquitin to target substrates, along with E1 and E2 enzymes. CARPs (CARP1 and CARP2, 77% identity) also belong to the IAP family (inhibitors of apoptosis proteins) inhibiting activation of DED (death effector domain) containing caspase proteins (8 and 10). In addition to targeting caspases 8 and 10, CARPs have been shown to target phosphorylated p53 for degradation in an Hdm2 independent manner. Furthermore, CARP2 has been shown to be a negative regulator of TNF induced NF-kappaB activation by targeting RIP for degradation.
References
1. Yang, W., et al., CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation. J Biol Chem, 2007. 282:3273-81.
2. Yang, W. and W.S. El-Deiry, CARPs are E3 ligases that target apical caspases and p53. Cancer Biol Ther, 2007. 6:1676-83.
3. McDonald, E.R., 3rd and W.S. El-Deiry, Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth. Proc Natl Acad Sci USA, 2004. 101:6170-5.
4. Liao, W., et al., CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation. Curr Biol, 2008. 18:641-9.