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Bertin Bioreagent
anti-Histone H3 (Phospho-Ser10), mAb (4C8)
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664
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CHF 664.00
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BRT-G01053-R100100 µlCHF 664.00
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| Product Details | |
|---|---|
| Synonyms | H3 pSer10; H3 Ser10p |
| Product Type | Monoclonal Antibody |
| Properties | |
| Clone | 4C8 |
| Isotype | Mouse IgG2aκ |
| Source/Host | Mouse |
| Immunogen/Antigen | Ovalbumin conjugated synthetic peptide (ARK[phospho-S]TGGKAPRKQLC) corresponding to aa 7-20 of Histone H3 (17 kDa). This sequence is conserved in a wide range of species. |
| Application | ELISA, Western Blot, Immunofluorescence, Immunoprecipitation, Immunohistochemistry. Recommended dilutions: 1/500-1/5000. |
| Specificity | Recognizes phosphorylated (Ser10) histone H3. |
| Formulation | Liquid. Does not contain any preservative. |
| Other Product Data |
Click here for Original Manufacturer 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.