Rabbit anti-Human, Mouse STUB1 Polyclonal Antibody | anti-STUB1 antibody

Anti-STUB1 Antibody, Rabbit Polyclonal

Cat. Num. AAA8100962

• Gene Names: STUB1; CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• Reactivity: Human, Mouse
• Applications: Immunohistochemistry
• Purity: Protein A & Antigen Affinity
• Synonyms: STUB1; Polyclonal Antibody; Anti-STUB1 Antibody; Rabbit Polyclonal; STUB1 Antibody; Rabbit PAb; Antigen Affinity Purified; STIP1 homology and U-box containing protein 1; Anti-CHIP Antibody; Anti-HSPABP2 Antibody; Anti-NY-CO-7 Antibody; Anti-SCAR16 Antibody; Anti-SDCCAG7 Antibody; Anti-UBOX1 Antibody; anti-STUB1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: Human STUB1
• Purity/Purification: Protein A & Antigen Affinity
• Form/Format: Liquid; 0.2um filtered solution in PBS

• Applicable Applications for anti-STUB1 antibody: Immunohistochemistry-Paraffin (IHC-P)
• Application Notes: IHC-P: 1:500-1:2000
• Immunogen: A synthetic peptide corresponding to the C-terminus of the Human STUB1
• Conjugation: Unconjugated
• Preparation: Produced in rabbits immunized with a synthetic peptide corresponding to the C-terminus of the Human STUB1, and purified by antigen affinity chromatography.
• Preparation and Storage: This antibody can be stored at 2-8 degree C for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20 degree C to -80 degree C. Preservative-Free. Avoid repeated freeze-thaw cycles.

Immunohistochemistry (IHC)

(Immunochemical staining STUB1 in human skeletal muscle with rabbit polyclonal antibody (1:1000, formalin-fixed paraffin embedded sections).)

Immunohistochemistry (IHC)

(Immunochemical staining STUB1 in mouse skeletal muscle with rabbit polyclonal antibody (1:2000, formalin-fixed paraffin embedded sections).)

Related Product Information for anti-STUB1 antibody

CHIP, the protein encoded by STUB1, is a central component of cellular protein homeostasis and interacts with several key proteins involved in the pathogenesis of manifold neurodegenerative diseases. Missense and truncating mutations in STUB1 lead to SCAR16. CHIP/STUB1 ubiquitin ligase is a negative co-chaperone for HSP90/HSC70, and its expression is reduced or lost in several cancers, including breast cancer. Pathogenic variants in STUB1 were initially described in autosomal recessive spinocerebellar ataxia type 16 and dominant cerebellar ataxia with cerebellar cognitive dysfunction (SCA48). Data indicated that STUB1 deficiency leads both to the intracellular accumulation of protein aggregates and to an increase in the secretion of small extracellular vesicles (sEVs), including exosomes. Secreted sEVs are enriched in ubiquitinated and/or undegraded proteins and protein oligomers.

Product Categories/Family for anti-STUB1 antibody

Adaptor Proteins

References

Roux T, et al. (2020) Clinical, neuropathological, and genetic characterization of stub1 variants in cerebellar ataxias: A frequent cause of predominant cognitive impairment. Genet Med 22 (11): 1851-1862.Luan H, et al. (2018) Loss of the nuclear pool of ubiquitin ligase chip/stub1 in breast cancer unleashes the mzf1-cathepsin pro-oncogenic program. Cancer Res 78 (10): 2524-2535.Hayer SN, et al. (2017) Stub1/chip mutations cause gordon holmes syndrome as part of a widespread multisystemic neurodegeneration: Evidence from four novel mutations. Orphanet J Rare Dis 12 (1): 31.Ferreira JV, et al. (2019) Exosomes and stub1/chip cooperate to maintain intracellular proteostasis. PLoS One 14 (10): e0223790.

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