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Validated All-in-One™ qPCR Primer for STUB1(NM_005861.3) Search again
Product ID:
HQP000334
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CHIP, HSPABP2, NY-CO-7, SCA48, SCAR16, SDCCAG7, UBOX1
Gene Description:
STIP1 homology and U-box containing protein 1
Target Gene Accession:
NM_005861.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Gene References into function
- Ubiquitin ligases (u box) determine protein stability in a highly regulated manner by coordinating the addition of polyubiquitin chains to proteins that are then targeted to the proteasome for degradation.
- Chip overexpression reduced the rate of AR degradation, consistent with an effect on AR folding,Chip affected AR folding was further supported by the finding that the effects of exogenous Chip were reproduced by a mutant lacking the U box
- CHIP E3 controls both the association of Hsp70/Hsp90 chaperones with ErbB2 and the down-regulation of ErbB2 induced by inhibitors of Hsp90
- tau binds to Hsc70, and its phosphorylation is a recognition requirement for the addition of ubiquitin by the E3 Ub ligase CHIP
- CHIP can interact with the Smad1/Smad4 proteins and block BMP signal transduction through the ubiquitin-mediated degradation of Smad proteins.
- Hsp70/CHIP may play an important role in the pathogenesis of tauopathies
- In cells treated with dexamethasone and geldanamycin, the GFP-GR becomes concentrated in fluorescent globules located periodically along the neurites. CHIP protein concentrates in the same loci in a steroid-dependent and geldanamycin-dependent manner.
- CHIP functions as a negative regulator of AR transcriptional activity by promoting AR degradation
- HspBP1 interferes with the CHIP-induced degradation of immature forms of the cystic fibrosis transmembrane conductance regulator (CFTR) and stimulates CFTR maturation.
- Results suggest that co-chaperone CHIP, possibly with another E3 ligase(s), modulates the ubiquitylation of mutant Cu/Zn-superoxide dismutase and renders them more susceptible for proteasomal degradation.
- CHIP is an E3 ligase for nNOS whose action is facilitated by (and possibly requires) its interaction with nNOS-bound hsp70
- CHIP is an E3 ligase that mediates alternative effects of the ubiquitin-proteasome pathway on glucocorticoid receptor down-regulation and transactivation
- findings suggest that CHIP can modulate the sensitivity of the TGF-beta signaling by controlling the basal level of Smad3 through ubiquitin-mediated degradation
- CHIP-induced degradation was observed for mutant and wild-type p53, which transiently associate with molecular chaperones Hsc70 and Hsp90 and can be diverted onto a degradation pathway through this association
- CHIP promotes ERalpha degradation and attenuates receptor-mediated gene transcription.
- Increases in CHIP may protect against neurofibrillary tangles formation in the early stages of Alzheimer's disease.
- Hsc70 cochaperone BAG-2 as a main component of CHIP complexes. BAG-2 inhibits the ubiquitin ligase activity of CHIP.
- CHIP directly interacts with C-terminal deleted HSF1 but not with full-length HSF1 under non-stressed conditions, and with full-length HSF1 under heat shock treatment; interaction requires conformational change of HSF1 by heat stress.
- CHIP is identified as a functional partner of Ubc13-Uev1a in formation of Lys63-linked polyubiquitin chains, extending CHIP's roles into ubiquitin regulation as well as targeted destruction.
- Chip may be at least one ubiquitin E3 ligase responsible for eIF4E ubiquitination
- CHIP recognizes AR in a highly specific, phosphorylation- and sequence-dependent manner
- Results show that CHIP and ataxin-1 proteins directly interact and co-localize in nuclear inclusions both in cell culture and spinocerebellar ataxia type-1 postmortem neurons.
- Our findings suggest that the role of CHIP in aggregation of polyQ proteins greatly varies depending on the context of full-length polyQ proteins.
- Dorfin-CHIP(L) rescued neuronal cells from mutant SOD1-associated toxicity and reduced the aggresome formation induced by mutant SOD1 more effectively than did Dorfin(WT).
- A critical mediator of Hsp90 inhibition leading to p-tau degradation is CHIP.
- DAPK is found in two distinct immune complexes, one containing HSP90 and CHIP and a second complex containing only DIP1/Mib; strict modulation of DAPK activities by HSP90 heterocomplexes is critical for regulation of apoptosis and cellular homeostasis
- CHIP possesses an intrinsic chaperone activity that enables it to selectively recognize and bind nonnative proteins
- CHIP might be a direct chaperone of wild type p53 that helps p53 in maintaining wild type conformation under physiological condition as well as help resurrect p53 mutant phenotype into a folded native state under stress condition.
- Ubiquitin ligase activity of CHIP is dispensable for Tal1/SCL binding but essential for degradation.
- CHIP might preferentially regulate phosphorylated Smad1 and thus the BMP signaling
- These results indicate that the MKKS mutants have an abnormal conformation and that chaperone-dependent degradation mediated by CHIP is a key feature of McKusick-Kaufman syndrome/Bardet-Biedl syndrome diseases.
- Data show that CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins XRCC1, DNA polymerase beta, and DNA ligase III.
- CHIP preferentially recognizes and mediates degradation of toxic, oligomeric forms of alphaSyn
- Inhibition of tyrosine kinase activity of Her-2/neu by quercetin could indicate an lateration in the Her-2/neu structure which promotes CHIP recruitments and down-regulation of Her-2/neu
- This study reveals a critical role for CHIP in the aggresome pathway.
- both UBC7/gp78 and UbcH5a/CHIP may be involved in CYP3A4 ER-associated degradation, although their relative physiological contribution remains to be established
- Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.