
Recombinant humaan COMMD1-eiwit
Kwaliteit
ISO Gecertificeerd
Levering
24-48 uur
Technische Specificaties
COMMD1, also known as copper metabolism MuRR1 domain-containing protein 1, is a 190 amino acid protein responsible for inhibition of TNF-induced NFkB p50 and has a suggested role in facilitation of biliary copper excretion within hepatocytes. High expression is found in liver tissue, with lower expressions in lung, heart, kidney and brain tissue. This protein interacts directly with COMMD6 and ATP7B, and indirectly with IkB-beta and COMMD7. Recombinant human COMMD1 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.
COMM domain-containing protein 1, C2orf5, MuRR1, COMM domain-containing protein 1, COMMD-1, COMMD 1, COMM, MuRR 1, MuRR-1
E.coli
Human
His-Tag
SDS-PAGE
0.5 mg/mL (determined by Bradford assay)
> 90% by SDS-PAGE
23.3 kDa (210aa) confirmed by MALDI-TOF
COMMD1, COMM domain-containing protein 1, C2orf5, MuRR1, COMM domain-containing protein 1, COMMD-1, COMMD 1, COMM, MuRR 1, MuRR-1, ATGP0630-10 µg, ATGP0630-20 µg, ATGP0630-50 µg, ATGP0630-100 µg, ATGP0630-250 µg, ATGP0630-500 µg, ATGP0630-1 mg, ATGP0630-10, ATGP0630-20, ATGP0630-50, ATGP0630-100, ATGP0630-250, ATGP0630-500, ATGP0630-1
Van De Sluis B, et al. (2002) Hum Mol Genet. 11 (2) :165-73.; ; Muller T, et al. (2003) J Hepatol. 38 (2) :164-8.;
Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol 0.1M NaCl
Signal Transduction
NP_689729
Q8N668
Human
MAAGELEGGK PLSGLLNALA QDTFHGYPGI TEELLRSQLY PEVPPEEFRP FLAKMRGILK SIASADMDFN QLEAFLTAQT KKQGGITSDQ AAVISKFWKS HKTKIRESLM NQSRWNSGLR GLSWRVDGKS QSRHSAQIHT PVAIIELELG KYGQESEFLC LEFDEVKVNQ ILKTLSEVEE SISTLISQPN
Beschrijving
COMMD1, also known as copper metabolism MuRR1 domain-containing protein 1, is a 190 amino acid protein responsible for inhibition of TNF-induced NFkB p50 and ha
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