Bertin Bioreagent

anti-Histone H3 Dimethyl (K)-Phospho (S), mAb (2H12)

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BRT-G01056-R100100 µlCHF 777.00
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Product Details
Synonyms H3K9me2 S10p; H3K27me2 S28p
Product Type Monoclonal Antibody
Properties
Clone 2H12
Isotype Mouse IgG1κ
Source/Host Mouse
Immunogen/Antigen Ovalbumin conjugated synthetic peptide ASGSSRSKS[dimethyl K]DRKYTL(C) corresponding to aa 180-195 of human TAF10.
Application ELISA, Western Blot, Immunofluorescence, Immunoprecipitation. Recommended dilutions: 1/500-1/5000.
Specificity Recognizes dimethylated (K9)-phosphorylated (S10) histone H3 or dimethylated (K27)-phosphorylated (S28) histone H3. The generated 51TA2H12 clone recognizes S10- or S28-phosphorylated histone H3, but only when doubly modified with H3K9me2 or H3K27me2.
Formulation Liquid. Does not contain any preservative.
Other Product Data

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Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by Bertin Bioreagent
Shipping and Handling
Shipping BLUE ICE
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability Stable for at least 3 years after receipt when stored at -20°C.
Documents
Product Specification Sheet
Datasheet Download PDF
Description
Histone H3 is one of the DNA-binding proteins found in the chromatin of all eukaryotic cells. H3 along with four core histone proteins binds to DNA forming the structure of the nucleosome. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Histone H3 has three main variants, H3.1 and H3.2, which are deposited in chromatin only during DNA replication and H3.3, which is replication independent and is found primarily in the regions of active transcription and heterochromatin. Post translationally, histones are modified in a variety of ways to either directly change the chromatin structure or allow for the binding of specific transcription factors. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.
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