SRP0107
HDAC-5 full length human
recombinant, expressed in baculovirus infected insect cells, ≥10% (SDS-PAGE)
Synonym(s):
HD5, Histone deacetylase 5, NY-CO-9
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
Recommended Products
biological source
human
recombinant
expressed in baculovirus infected insect cells
Assay
≥10% (SDS-PAGE)
form
aqueous solution
potency
≥1 units/mg
mol wt
150 kDa
packaging
pkg of 5 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
>0.02 mg/mL
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... HDAC5(10014)
General description
Histone deacetylase 5 (HDAC5) belongs to the Hda1-like proteins class IIa HDAC family. It contains 17 phospho-acceptor residues and a classical deacetylase domain. The HDAC5 gene is mapped to human chromosome 17q21.
Application
HDAC-5 full-length human has been used in the adenosine diphosphate (ADP)-Glo assay and Γ-p32-adenosine triphosphate (ATP) radioisotope assay with focal adhesion kinase (FAK) kinase.
Biochem/physiol Actions
Histone deacetylase 5 (HDAC5) mediates synoviocyte activation, neural repair and regeneration. It regulates the assembly of the pericentric heterochromatin. Elevated expression of HDAC5 is implicated in high-risk medulloblastoma and breast cancer in very young women (BCVY).
Unit Definition
One unit is defined as the amount of enzyme required to deacetylate 1 pmol of substrate/min at 37°C.
Physical form
Formulated in 25 mM Tris-HCl, pH 8.0, 138 mM NaCl, 0.05% Tween-20 and 10% glycerol.
Preparation Note
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Regulatory Information
新产品
Choose from one of the most recent versions:
Certificates of Analysis (COA)
Lot/Batch Number
Don't see the Right Version?
If you require a particular version, you can look up a specific certificate by the Lot or Batch number.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Edward Seto et al.
Cold Spring Harbor perspectives in biology, 6(4), a018713-a018713 (2014-04-03)
Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl functional groups from the lysine residues of both histone and nonhistone proteins. In humans, there are 18 HDAC enzymes that use either zinc- or NAD(+)-dependent mechanisms to deacetylate acetyl
P Peixoto et al.
Cell death and differentiation, 19(7), 1239-1252 (2012-02-04)
Histone deacetylases (HDACs) form a family of enzymes, which have fundamental roles in the epigenetic regulation of gene expression and contribute to the growth, differentiation, and apoptosis of cancer cells. In this study, we further investigated the biological function of
beta-Adrenergic Stimulation Induces Histone Deacetylase 5 (HDAC 5) Nuclear Accumulation in Cardiomyocytes by B55alpha-PP 2A-Mediated Dephosphorylation
Weeks KL, et al.
Journal of the American Heart Association null
Sara S Oltra et al.
Cancers, 12(2) (2020-02-14)
Breast cancer in very young women (BCVY) defined as <35 years old, presents with different molecular biology than in older patients. High HDAC5 expression has been associated with poor prognosis in breast cancer (BC) tissue. We aimed to analyze HDAC5
Tadatoshi Sato et al.
Nature communications, 11(1), 3282-3282 (2020-07-03)
Osteocytes, cells ensconced within mineralized bone matrix, are the primary skeletal mechanosensors. Osteocytes sense mechanical cues by changes in fluid flow shear stress (FFSS) across their dendritic projections. Loading-induced reductions of osteocytic Sclerostin (encoded by Sost) expression stimulates new bone
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service