STUB1 sirna

STUB1 siRNA (Human)

Cat. Num. AAA8218676

• Gene Names: STUB1; CHIP; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7
• Reactivity: Human
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: STUB1; STUB1 siRNA (Human); CHIP; E3 ubiquitin-protein ligase CHIP; Antigen NY-CO-7; CLL-associated antigen KW-8; Carboxy terminus of Hsp70-interacting protein; STIP1 homology and U box-containing protein 1; STUB1 sirna

• Host: Synthetic
• Reactivity: Human
• Specificity: STUB1 siRNA (Human) is a target-specific 19-23 nt siRNA oligo duplexes designed to knock down gene expression.
• Purity/Purification: > 97%
• Form/Format: Lyophilized powder
• Sequence Length: 231

• Applicable Applications for STUB1 sirna: RNA Interference (RNAi)
• Quality Control: Oligonucleotide synthesis is monitored base by base through trityl analysis to ensure appropriate coupling efficiency. The oligo is subsequently purified by affinity-solid phase extraction. The annealed RNA duplex is further analyzed by mass spectrometry to verify the exact composition of the duplex. Each lot is compared to the previous lot by mass spectrometry to ensure maximum lot-to-lot consistency.
• Directions for Use: We recommends transfection with 100 nM siRNA 48 to 72 hours prior to cell lysis. Before resuspending, briefly centrifuge the tube to ensure the lyophilized siRNA is at the bottom of the tube. Resuspend the siRNA oligos to an appropriate concentration with DEPC water. For each vial, suitable for 250 transfections in 24 well plate (20 pmol for each well).
• Components: We offer pre-designed sets of 3 different target-specific siRNA oligo duplexes of human STUB1 gene. Each vial contains 5 nmol of lyophilized siRNA. The duplexes can be transfected individually or pooled together to achieve knockdown of the target gene, which is most commonly assessed by qPCR or western blot. Our siRNA oligos are also chemically modified (2'-OMe) at no extra charge for increased stability and enhanced knockdown in vitro and in vivo.
• Preparation and Storage: Shipped at 4 degree C. Store at -20 degree C for one year.

Related Product Information for STUB1 sirna

siRNA to inhibit STUB1 expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 645912990
• NCBI GeneID: 10273
• NCBI Accession #: NP_001280126.1
• NCBI GenBank Nucleotide #: NM_001293197.1
• UniProt Accession #: Q9UNE7; O60526; Q969U2; Q9HBT1; A2IDB9
• 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: 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 conjugating system; Ubiquitin ligase; EC 6.3.2.-; 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 binding; enzyme binding; protein homodimerization activity; G-protein-coupled receptor binding; TPR domain binding; ubiquitin protein ligase binding; ubiquitin-protein ligase activity; misfolded protein binding; Hsp90 protein binding; Hsp70 protein 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; ubiquitin-dependent SMAD protein catabolic process; DNA repair; positive regulation of protein ubiquitination; transforming growth factor beta receptor signaling pathway; positive regulation of ubiquitin-protein ligase activity; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; 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