Rabbit STUB1 Polyclonal Antibody | anti-STUB1 antibody

Anti-STUB1 Antibody

Cat. Num. AAA416683

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

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Affinity purified
• Form/Format: Liquid
• Concentration: 100ug/100ul (varies by lot)
• Sequence Length: 1646

• Applicable Applications for anti-STUB1 antibody: Peptide ELISA (EIA), Western Blot (WB)
• Application Notes: Peptide ELISA titer: 1:4,000-1:80,000; Western blot analysis: 1:200-500; Optimal dilutions/concentrations should be determined by the end user.
• Storage Buffer: PBS, pH 7.4 with 0.02% Sodium Azide
• Immunogen: Synthetic peptide conjugated to KLH
• Preparation and Storage: This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use. For extended storage, aliquot contents and freeze at -20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.

Western Blot (WB)

Related Product Information for anti-STUB1 antibody

STUB1, or CHIP, is a ubiquitin ligase/cochaperone that participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation (Min et al., 2008 [PubMed 18411298]).[supplied by OMIM, Jul 2009]

References

(1) Peng,X., Guo,X., Borkan,S.C.,,et,al Heat shock protein 90 stabilization of ErbB2 expression is disrupted by ATP depletion in myocytes, J. Biol. Chem. 2005;280 (13):13148-13152.

NCBI and Uniprot Product Information

• NCBI GI #: 56181386
• NCBI GeneID: 10273
• NCBI Accession #: NP_005852.2
• NCBI GenBank Nucleotide #: NM_005861
• Molecular Weight: 27,067 Da
• NCBI Official Full Name: Homo sapiens STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase (STUB1), mRNA
• 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; 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
• 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; Ligase; Ubiquitin conjugating system; EC 6.3.2.-; Ubiquitin ligase; Adaptor/scaffold

Chromosomal Location of Human Ortholog: 16p13.3

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

Molecular Function: protein binding, bridging; protein homodimerization activity; ubiquitin-protein ligase activity; Hsp90 protein binding; Hsp70 protein binding; misfolded 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 protein binding; negative regulation of transforming growth factor beta receptor signaling pathway

Disease: Spinocerebellar Ataxia, Autosomal Recessive 16