Mouse anti-Human STUB1 Monoclonal Antibody | anti-STUB1 antibody

STUB1 (STIP1 Homology and U box-containing Protein 1, E3 Ubiquitin-protein Ligase CHIP, Antigen NY-CO-7, CLL-associated Antigen KW-8, Carboxy Terminus of Hsp70-interacting Protein, CHIP, PP1131, HSPABP2, NY-CO-7, SDCCAG7, UBOX1) (HRP)

Cat. Num. AAA6155260

• Gene Names: STUB1; CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• Reactivity: Human
• Applications: ELISA, Western Blot
• Purity: Purified by Protein A Affinity Chromatography.
• Synonyms: STUB1; Monoclonal Antibody; STUB1 (STIP1 Homology and U box-containing Protein 1; E3 Ubiquitin-protein Ligase CHIP; Antigen NY-CO-7; CLL-associated Antigen KW-8; Carboxy Terminus of Hsp70-interacting Protein; CHIP; PP1131; HSPABP2; NY-CO-7; SDCCAG7; UBOX1) (HRP); EC=6.3.2.-; anti-STUB1 antibody

• Host: Mouse
• Reactivity: Human
• Clonality: Monoclonal
• Isotype: IgG2a, lambda
• Clone Number: 2E12
• Specificity: Recognizes human STUB1.
• Purity/Purification: Purified by Protein A Affinity Chromatography.
• Form/Format: Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with horseradish peroxidase (HRP).

• Applicable Applications for anti-STUB1 antibody: ELISA (EIA), Western Blot (WB)
• Application Notes: Applications are based on unconjugated antibody.
• Immunogen: Partial recombinant protein corresponding to aa204-303 from STUB1 with GST tag. MW of the GST tag alone is 26kD.
• Immunogen Sequence: HDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY
• Conjugate: HRP
• Preparation and Storage: Store product at 4 degree C if to be used immediately within two weeks. For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20 degree C. Aliquots are stable at -20 degree C for 12 months after receipt. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Note: Sodium azide is a potent inhibitor of peroxidase and should not be added to HRP conjugates. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Western Blot (WB)

(Western Blot detection against Immunogen using 134020 (37.11kD).)

Product Categories/Family for anti-STUB1 antibody

Antibodies; Ubiquitin Ligases

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: 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