protein

CHIP, 1-303aa, Human, Recombinant, E Coli

MBS203190

0.1 mg

255 USD

Recombinant Protein

CHIP, 1-303aa, Human, Recombinant, E Coli

CHIP

STuB1; HSPABP2; NY-CO-7; SDCCAG7; uBOX1; Carboxy terminus of HSP70 interacting protein Antigen NY CO 7; CLL associated antigen KW 8; Carboxy terminus of Hsp70p interacting protein; CHIP; E3 ubiquitin protein ligase CHIP; STuB 1; uBOX 1; Heat shock protein A binding protein 2 (c terminal); NY CO 7; Serologically defined colon cancer antigen 7; STIP1 homology and u Box containing protein 1.

E3 ubiquitin-protein ligase CHIP isoform a; E3 ubiquitin-protein ligase CHIP; E3 ubiquitin-protein ligase CHIP; CLL-associated antigen KW-8; antigen NY-CO-7; carboxy terminus of Hsp70-interacting protein; heat shock protein A binding protein 2 (c-terminal); serologically defined colon cancer antigen 7; STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; Antigen NY-CO-7; CLL-associated antigen KW-8; Carboxy terminus of Hsp70-interacting protein; STIP1 homology and U box-containing protein 1

CHIP

STUB1; STUB1; CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7

CHIP_HUMAN

303

MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG RAITRNPLVA VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL GQCQLEMESY DEAIANLQRA YSLAKEQRLN FGDDIPSALR IAKKKRWNSI EERRIHQESE LHSYLSRLIA AERERELEEC QRNHEGDEDD SHVRAQQACI EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM REPCITPSGI TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV EDY

> 90% by SDS-PAGE

Liquid. In 20 mM Tris-HCl buffer (pH 7.5) containing 5 mM DTT, 10% glycerol

1 mg/ml (determined by Bradford assay)

Can be stored at 4 degree C short term (1-2 weeks). For long term storage, aliquot and store at -20 degree C or -70 degree C. Avoid repeated freezing and thawing cycles.

SDS-PAGE

Antigen Species: Human

Expression System: E Coli. Endotoxin: < 1.0 Eu per 1 microgram of protein (determined by LAL method)

Heat Shock Proteins

CHIP, also known as STuB1, is a cytoplasmic protein whose amino acid sequence is highly conserved across species. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain, whereas its u-box domain contains its E3 ubiquitin ligase activity. Its interaction with these molecular chaperones results in client substrate ubiquitylation and degradation by the proteasome. Thus, CHIP acts to tilt the folding-refolding machinery toward the degradative pathway, and it serves as a link between the two. Recombinant human CHIP protein was expressed in E.coli and purified by using conventional chromatography techniques.

Kajiro M., et al. (2009) Nat Cell Biol. 11(3):312-9. Ko HS., et al. (2009) Proc Natl Acad Sci. 106(8):2897-902.

56181387

NP_005852

NM_005861.3

34.8 kDa (303 aa), confirmed by MALDI-TOF.

Adaptive Immune System Pathway 366160!!Alpha-synuclein Signaling Pathway 137913!!Androgen Receptor Signaling Pathway 198806!!Antigen Processing: Ubiquitination Proteasome Degradation Pathway 366162!!Class I MHC Mediated Antigen Processing Presentation Pathway 366161!!Disease Pathway 530764!!Downregulation Of TGF-beta Receptor Signaling Pathway 645293!!Immune System Pathway 106386!!Loss Of Function Of SMAD2/3 In Cancer Pathway 906019!!Loss Of Function Of SMAD4 In Cancer Pathway 906017

This gene encodes a protein containing tetratricopeptide repeat and a U-box that functions as a ubiquitin ligase/cochaperone. The encoded protein binds to and ubiquitinates shock cognate 71 kDa protein (Hspa8) and DNA polymerase beta (Polb), among other targets. Mutations in this gene cause spinocerebellar ataxia, autosomal recessive 16. Alternative splicing results in multiple transcript variants. There is a pseudogene for this gene on chromosome 2. [provided by RefSeq, Jun 2014]

0.1 mg

255 USD