CHIP recombinant protein

CHIP, 1-303aa, Human, E Coli

Cat. Num. AAA203190

• Gene Names: STUB1; CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• Applications: SDS-Page
• Purity: > 90% by SDS-PAGE
• Synonyms: CHIP; 1-303aa; Human; E Coli; Carboxy terminus of HSP70 interacting protein; 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; 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.; CHIP recombinant protein

• Host: E Coli
• Purity/Purification: > 90% by SDS-PAGE
• Form/Format: Liquid. In 20 mM Tris-HCl Buffer (pH 7.5) containing 5 mM DTT, 10% glycerol
• Concentration: 1 mg/ml (determined by Bradford assay) (varies by lot)
• Sequence: 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
• Sequence Length: 303

• Applicable Applications for CHIP recombinant protein: SDS-PAGE
• Antigen Species: Human
• Endotoxin Level: < 1.0 EU per 1 microgram of protein (determined by LAL method)
• Preparation and Storage: 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

Related Product Information for CHIP recombinant protein

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.

Product Categories/Family for CHIP recombinant protein

Heat Shock Proteins

References

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.;

NCBI and Uniprot Product Information

• NCBI GI #: 56181387
• NCBI GeneID: 10273
• NCBI Accession #: NP_005852
• NCBI GenBank Nucleotide #: NM_005861.3
• UniProt Accession #: Q9UNE7; O60526; Q969U2; Q9HBT1; A2IDB9
• Molecular Weight: 34.8 kDa (303 aa), confirmed by MALDI-TOF.
• NCBI Official Full Name: E3 ubiquitin-protein ligase CHIP isoform a
• NCBI Official Synonym Full Names: STIP1 homology and U-box containing protein 1
• NCBI Official Symbol: STUB1
• NCBI Official Synonym Symbols: CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• NCBI Protein Information: E3 ubiquitin-protein ligase CHIP
• UniProt Protein Name: E3 ubiquitin-protein ligase CHIP
• Protein Family: Chitoporin
• UniProt Gene Name: STUB1

NCBI Description

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]

Uniprot Description

E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed:27708256). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed:24613385).