Rabbit STUB1 Polyclonal Antibody | anti-STUB1 antibody

STUB1 Conjugated Antibody

Cat. Num. AAA9443346

• Gene Names: STUB1; CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• Reactivity: Human, Mouse, Rat
• Applications: Most Applications
• Synonyms: STUB1; Polyclonal Antibody; STUB1 Conjugated Antibody; CHIP; HSPABP2; NY-CO-7; SDCCAG7; anti-STUB1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Specificity: The antibody detects endogenous level of total STUB1 protein.
• Form/Format: 0.01M Sodium Phosphate, 0.25M NaCl, pH 7.6, 5mg/ml Bovine Serum Albumin, 0.02% Sodium Azide

• Applicable Applications for anti-STUB1 antibody: Most Applications
• Application Notes: Suggested Dilution:; AF350 conjugated: most applications: 1:50-1:250; AF405 conjugated: most applications: 1:50-1:250; AF488 conjugated: most applications: 1:50-1:250; AF555 conjugated: most applications: 1:50-1:250; AF594 conjugated: most applications: 1:50-1:250; AF647 conjugated: most applications: 1:50-1:250; AF680 conjugated: most applications: 1:50-1:250; AF750 conjugated: most applications: 1:50-1:250; Biotin conjugated: working with enzyme-conjugated streptavidin, most applications: 1:50-1:1000
• Immunogen: Recombinant protein of human STUB1.
• Conjugation: Biotin AF350 AF405 AF488 AF555 AF594 AF647 AF680 AF750
• Excitation Emission: AF350: 346nm/442nm
• Preparation and Storage: Store at 4 degree C for 6 months.

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).

NCBI and Uniprot Product Information

• NCBI GI #: 78099173
• NCBI GeneID: 10273
• UniProt Accession #: Q9UNE7; O60526; Q969U2; Q9HBT1; A2IDB9
• Molecular Weight: 303
• NCBI Official Full Name: E3 ubiquitin-protein ligase CHIP
• NCBI Official Synonym Full Names: STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase
• NCBI Official Symbol: STUB1
• NCBI Official Synonym Symbols: CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• NCBI Protein Information: E3 ubiquitin-protein ligase CHIP; antigen NY-CO-7; CLL-associated antigen KW-8; serologically defined colon cancer antigen 7; carboxy terminus of Hsp70-interacting protein; heat shock protein A binding protein 2 (c-terminal)
• UniProt Protein Name: E3 ubiquitin-protein ligase CHIP
• Protein Family: STIP1 homology and U box-containing protein
• UniProt Gene Name: STUB1
• UniProt Entry Name: CHIP_HUMAN

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

CHIP: 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. Homodimer. Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Interacts with the C-terminal domains of HSPA8 and HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DYX1C1 and POLB. Interacts (via TPR repeats) with HSP90AA1. Interacts (when monoubiquitinated) with ATXN3. Interacts with UBE2W. Interacts (via the U-box domain) with the UBE2V2- UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with DNAJB6. Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 6.3.2.19; Ubiquitin ligase; EC 6.3.2.-; Ligase; Ubiquitin conjugating system; Adaptor/scaffold

Chromosomal Location of Human Ortholog: 16p13.3

Cellular Component: nucleoplasm; intermediate filament cytoskeleton; endoplasmic reticulum; ubiquitin conjugating enzyme complex; cytoplasm; plasma membrane; cytosol; ubiquitin ligase complex; nuclear inclusion body

Molecular Function: protein binding, bridging; protein homodimerization activity; ubiquitin-protein ligase activity; misfolded protein binding; Hsp90 protein binding; Hsp70 protein binding; protein binding; enzyme binding; G-protein-coupled receptor binding; TPR domain binding; ubiquitin protein ligase binding; SMAD binding; kinase binding; ligase activity

Biological Process: ubiquitin-dependent protein catabolic process; proteasomal ubiquitin-dependent protein catabolic process; protein autoubiquitination; protein polyubiquitination; unfolded protein response; protein maturation; misfolded or incompletely synthesized protein catabolic process; DNA repair; ubiquitin-dependent SMAD protein catabolic process; positive regulation of protein ubiquitination; transforming growth factor beta receptor signaling pathway; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of ubiquitin-protein ligase activity; regulation of glucocorticoid metabolic process; negative regulation of transforming growth factor beta receptor signaling pathway; negative regulation of protein binding

Disease: Spinocerebellar Ataxia, Autosomal Recessive 16