Rabbit STUB1 Antibody | anti-STUB1 antibody

STUB1 Antibody

Cat. Num. AAA8504137

• Gene Names: STUB1; CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunohistochemistry
• Purity: Affinity purification
• Synonyms: STUB1; STUB1 Antibody; CHIP; HSPABP2; NY-CO-7; SDCCAG7; UBOX1; anti-STUB1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Isotype: IgG
• Purity/Purification: Affinity purification
• Sequence Length: 231

• Applicable Applications for anti-STUB1 antibody: Western Blot (WB), Immunohistochemistry (IHC)
• Application Notes: WB: 1:500-1:2000; IHC: 1:50-1:200
• Immunogen: Recombinant protein of human STUB1
• Storage Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
• Preparation and Storage: Store at-20 degree C or-80 degree C. Avoid freeze/thaw cycles.

Related Product Information for anti-STUB1 antibody

The carboxy terminus of Hsc70-interacting protein (CHIP, STUB1) is a co-chaperone protein and functional E3 ubiquitin ligase that links the polypeptide binding activity of Hsp70 to the ubiquitin proteasome system (1). Cytoplasmic CHIP protein contains three 34-amino acid TPR (tetratricopeptide repeat) domains at its amino terminus and a carboxy-terminal U-box domain. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain, while E3 ubiquitin ligase activity is confined to the U-box domain (2, 3). The binding of CHIP to Hsp70 can stall the folding of Hsp70 client proteins and concomitantly facilitate the U-box dependent ubiquitination of Hsp70-bound substrates (4-6). CHIP appears to play a central role in cell stress protection (7) and is responsible for the degradation of disease-related proteins that include cystic fibrosis transmembrane conductance regulator (4), p53 (8), huntingtin and Ataxin-3 (9), Tau protein (10), and alpha-synuclein (11).

Product Categories/Family for anti-STUB1 antibody

Autophagy antibody; Cancer; Cardiovascular; Cell Biology; Epigenetics & Nuclear Signaling; Developmental Biologys; Immunology; Drug Discovery Products; Metabolism; Neuroscience; Signal Transduction; Stem Cells

References

1. McDonough, H. and Patterson, C. (2003) Cell Stress Chaperones 8, 303-8. 2. Ballinger, C.A. et al. (1999) Mol Cell Biol 19, 4535-45. 3. Murata, S. et al. (2001) EMBO Rep 2, 1133-8. 4. Meacham, G.C. et al. (2001) Nat Cell Biol 3, 100-5. 5. Younger, J.M. et al. (2004) J Cell Biol 167, 1075-85. 6. Jiang, J. et al. (2001) J Biol Chem 276, 42938-44. 7. Dai, Q. et al. (2003) EMBO J 22, 5446-58. 8. Esser, C. et al. (2005) J Biol Chem 280, 27443-8. 9. Jana, N.R. et al. (2005) J Biol Chem 280, 11635-40. 10. Shimura, H. et al. (2004) J Biol Chem 279, 4869-76. 11. Shin, Y. et al. (2005) J Biol Chem 280, 23727-34.

NCBI and Uniprot Product Information

• NCBI GI #: 645912990
• NCBI GeneID: 10273
• NCBI Accession #: NP_001280126.1
• NCBI GenBank Nucleotide #: NM_001293197.1
• UniProt Accession #: Q9UNE7; O60526; Q969U2; Q9HBT1; A2IDB9
• Molecular Weight: 35kDa
• NCBI Official Full Name: E3 ubiquitin-protein ligase CHIP isoform b
• 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: STIP1 homology and U box-containing protein
• 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).