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Validated All-in-One™ qPCR Primer for HDAC7(NM_015401.4) Search again
Product ID:
HQP104155
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HD7, HD7A, HDAC7A
Gene Description:
histone deacetylase 7
Target Gene Accession:
NM_015401.4(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
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events.
Gene References into function
- Characterization of the mouse HDAC7 ortholog.
- Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor
- Interaction of HDAC7 with MEF2D is essential for repression of Nur77.
- HDAC7 phosphorylation is mediated by calcium/calmodulin-dependent kinase I, which also promotes the association of HDAC7 with 14-3-3 and stabilizes HDAC7
- HDAC7 increased transcriptional activity of HIF-1alpha through the formation of a complex with HIF-1alpha, HDAC7, and p300
- HDAC7 is sequestered to the cytoplasm from mitochondrial and nuclear compartments upon initiation of apoptosis
- Data indicate that protein kinase D1 regulates the expression of Nur77 during thymocyte activation at least in part by phosphorylating HDAC7.
- a mutant of HDAC7 specifically deficient in phosphorylation by protein kinase D, inhibits T cell receptor-mediated apoptosis of T cell hybridomas
- These results identify HDAC7 as a novel Androgen receptor corepressor whose subcellular and subnuclear compartmentalization can be regulated in an androgen-selective manner.
- Class IIa histone deacetylases (HDACs) are subjected to signal-independent nuclear export that relies on their constitutive phosphorylation. EMK and C-TAK1, are identified as regulators of this process.
- HDAC7 is a key modulator of endothelial cell migration and angiogenesis, at least in part, by regulating platelet-derived growth factor-B (PDGF-B) and its receptor PDGFR-beta gene expression.
- Histone deacetylase 7 associates with Runx2 and represses its activity during osteoblast maturation in a deacetylation-independent manner
- HDAC7 has a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity
- PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions.
- Caspase-8 cleaves histone deacetylase 7 and abolishes its transcription repressor function.
- PML sequesters HDAC7 to relieve repression and up-regulate gene expression
- The data showed alteration of HDACs gene expression in pancreatic cancer. Increased expression of HDAC7 discriminates PA from other pancreatic tumors.
- These results demonstrate that phosphorylation of HDAC7 serves as a molecular switch to mediate VEGF signaling and endothelial function.
- VEGF stimulates HDAC7 phosphorylation and cytoplasmic accumulation modulating MT-MMP1/MMP10 expression and angiogenesis.
- These results demonstrate a novel function of HDAC7 and provide a regulatory mechanism of PML sumoylation.