Mouse E3 ubiquitin-protein ligase CHIP ELISA Kit | STUB1 elisa kit

Mouse E3 ubiquitin-protein ligase CHIP ELISA Kit

Cat. Num. AAA760268

• Gene Names: STUB1; CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• Reactivity: Mouse
• Synonyms: E3 ubiquitin-protein ligase CHIP; Mouse E3 ubiquitin-protein ligase CHIP ELISA Kit; STUB1/HSPABP2/NY-CO-7/SDCCAG7/STUB1/UBOX1/Antigen NY-CO-7/Carboxy terminus of Hsp70-interacting protein/CHIPSTIP1 homology and U box-containing protein 1/CLL-associated antigen KW-8/E3 ubiquitin-protein ligase CHIP/EC 6.3.2.-/heat shock protein A binding protein 2 (c-terminal)/HSPABP2/NY-CO-7/SDCCAG7/serologically defined colon cancer antigen 7/STIP1 homology and U-box containing protein 1/STIP1 homology and U-box containing protein 1; E3 ubiquitin protein ligase/UBOX1; STUB1 elisa kit

• Reactivity: Mouse
• Sequence Length: 231

• Samples: Serum, plasma and other biological fluids.
• Assay Type: Sandwich ELISA, Double Antibody
• Detection Range: 0.156-10ng/ml
• Sensitivity: 0.094ng/ml
• Preparation and Storage: Store at 4 degree C if kit is to be used within 1 week. Stable for 6 months (if micro ELISA Plate, Lyophilized Standard and Concentrated Biotinylated Detection Protein stored at-20 degree C. Other components at 2-8 degree C). Stable for 12 months (if the entire kit is stored at-20 degree C).

Typical Testing Data

Typical Standard Curve

Related Product Information for STUB1 elisa kit

Principle of the Assay||This kit was based on sandwich enzyme-linked immune-sorbent assay technology. anti-Mouse STUB1 antibody was pre-coated onto 96-well plates. And the biotin conjugated anti-Mouse STUB1 antibody was used as detection antibodies. The standards, test samples and biotin conjugated detection antibody were added to the wells subsequently, and wash with wash buffer. HRP-Streptavidin was added and unbound conjugates were washed away with wash buffer. TMB substrates were used to visualize HRP enzymatic reaction. TMB was catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the Mouse STUB1 amount of sample captured in plate. Read the O.D. absorbance at 450nm in a microplate reader, and then the concentration of Mouse STUB1 can be calculated.

NCBI and Uniprot Product Information

• NCBI GI #: 645912990
• NCBI GeneID: 10273
• NCBI Accession #: NP_001280126.1
• NCBI GenBank Nucleotide #: NM_001293197.1
• Molecular Weight: 27,067 Da
• NCBI Official Full Name: E3 ubiquitin-protein ligase CHIP isoform b
• 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
• UniProt Protein Name: E3 ubiquitin-protein ligase CHIP
• Protein Family: E3 ubiquitin-protein ligase
• 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: Ubiquitin ligase; EC 6.3.2.19; Ligase; Adaptor/scaffold; EC 6.3.2.-; Ubiquitin conjugating system

Chromosomal Location of Human Ortholog: 16p13.3

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

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

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

Disease: Spinocerebellar Ataxia, Autosomal Recessive 16