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Validated All-in-One™ qPCR Primer for VCP(NM_007126.4) Search again
Product ID:
HQP018469
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CDC48, FTDALS6, TERA, p97
Gene Description:
valosin containing protein
Target Gene Accession:
NM_007126.4(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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Summary
The protein encoded by this gene is a member of a family that includes putative ATP-binding proteins involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. This protein, as a structural protein, is associated with clathrin, and heat-shock protein Hsc70, to form a complex. It has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation. [provided by RefSeq].
Gene References into function
- VCP regulates NFKappaB pathway, which is important for metastasis of osteosarcoma
- p97/VCP is essential for degrading membrane-associated ubiquitinated proteins and that profound deficits in its ATPase activity severely affect ER quality control, leading to abnormal ER expansion and cell death
- VCP expression level has prognostic significance for disease-free and overall survival of patients with HCC
- ataxin-3 associates with the ubiquitin- and proteasome-binding factors Rad23 and valosin-containing protein (VCP/p97)
- valosin-containing protein has a role in progression of colorectal carcinomas
- VCP expression analysis is a useful prognosticator for PENs (pancreatic endocrine neoplasms).
- Valosin-containing protein functionally regulates Dorfin through direct interaction
- A 55-year-old German patient with inclusion body myopathy and frontotemporal dementia who harbors a heterozygous R155C missense mutation residing in the N-terminal CDC48 domain of VCP, which is involved in ubiquitin binding.
- VCP/CDC48 is required for transport of T cell-specific adapter protein into the eukaryotic nucleus
- Functional characterizations indicate that VCP is not an Hsp90 substrate, but rather demonstrate the biochemical hallmarks of an Hsp90 co-chaperone
- p97 does not provide the primary driving force for extracting the cholera toxin A1 chain from the endoplasmic reticulum
- p97/valosin-containing protein ATPase activity is regulated by oxidative modification of the evolutionally conserved cysteine 522 residue in Walker A motif
- We identified a novel missense mutation in the VCP gene segregating with this disease in an Austrian family of four affected siblings, who exhibited progressive proximal myopathy and Paget disease of the bone.
- Results suggest that the D2 domain of valosin-containing protein is involved in aggresome formation.
- VCP-Atx-3 association is a potential target for therapeutic intervention and suggest that it might influence the progression of spinocerebellar ataxia type 3.
- VCP is an essential target of Akt signaling
- valosin-containing protein (VCP) is an integral component of the endoplasmic reticulum associated degradation and cellular stress pathways induced by the unfolded protein response, which destroys the CFTR to cause cystic fibrosis
- Our findings are consistent with the hypothesis that the pathology associated with VCP gene mutations is the result of impairment of ubiquitin-based degradation pathways.
- the PUB domain functions as a p97 binding module in human peptide N-glycanase
- These results indicate that VCP is required for maintenance of normal endoplasmic reticulum structure and function and mediates the degradation of some proteins via the ubiquitin (Ub)-proteasome system.
- VCP knockdown by small interfering RNA eventually deconstructed both the ER and Golgi and interdicted protein trafficking through the secretory pathway to the plasma membrane.
- PBX1 plays a crucial role in valosin-containing protein (VCP) expression and function and the PBX-VCP pathway might be important for cell survival under cytokine stress
- results support the hypothesis that components of the retrotranslocation machinery such as VCP do not interact with CFTR in epithelial cells that endogenously express wild-type CFTR since under normal conditions processing of WT protein is efficient
- p97 can exert unfoldase activity in vitro, provided that a single tyrosine residue is introduced into the D1 pore and that the N domain is deleted.
- These findings indicate that ELF2/NERF promotes VCP transcription and that ELF2/NERF-VCP pathway might be important for cell survival and proliferation under cytokine stress.
- Frontotemporal dementia with inclusion body myopathy and Paget's disease of bone (IBMPFD) is a rare, autosomal dominant disorder caused by mutations in the gene valosin-containing protein (VCP).
- VCP (valosin-containing protein; p97) has a role in the control of N-glycosylation of proteins in the endoplasmic reticulum
- There is no evidence, that common variants in VCP confer a strong risk to the development of sporadic FTD.
- We have found a novel rare variant within the VCP gene, but we did not find a variant that could explain the linkage signal for LOAD on chromosome 9.
- This study demonstrate that VCP is present in both myonuclei and endothelial cell nuclei in normal human muscle tissue.
- Our study demonstrates that VCP mutations are found in patients of Italian background and may lead to a variable clinical phenotype even within the same kinship.
- SVIP is an endogenous inhibitor of ERAD that acts through regulating the assembly of the gp78-p97/VCP-Derlin1 complex.
- A patient with Inclusion body myopathy with Paget disease of bone and frontotemporal dementia carried a novel heterozygous base pair change, 47832C>T, in the VCP gene that resulted in substitution of an arginine residue by cysteine at position 93 (R93C).
- Novel VCP mutations N387H and L198W in six individuals from two families who presented with proximal muscle weakness at a mean age of diagnosis of 40 years, most losing the ability to walk within a few years of onset.
- VCP-containing protein mediates the endoplasmic reticulum degradation of V2 vasopressin receptors.
- Mutations of the valosin-containing protein gene (VCP) at 9p13 cause inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia.
- The interaction of EerI with the p97 complex appears to negatively influence a deubiquitinating process that is mediated by p97-associated deubiquitinating enzymes
- The findings demonstrated that monocytic differentiation and G0/G1 growth arrest in human U937 leukemia cells was accompanied by an increase in VCP/p97 expression and a distinct subcellular distribution to be reverted during retrodifferentiation.
- describes the first Italian family with multiple individuals diagnosed as having IBMPFD and carrying the recurrent R155H mutation.
- ELF2 transactivates VCP promoter through binding to two motifs, with a predominant contribution of the upstream one.
- These results suggest a role for p97 phosphorylation in the degradation of misfolded glycoproteins.
- UBXD7 links p97 to the ubiquitin ligase CUL2/VHL and its substrate hypoxia-inducible factor 1alpha (HIF1alpha).