RevMab

anti-Trimethyl-Histone H3 (Lys79), Rabbit Monoclonal (RM157)

CHF 251.00
In stock
REV-31-1053-00-C02525 µgCHF 251.00
REV-31-1053-00-C100100 µgCHF 559.00
More Information
Product Details
Synonyms H3 K79me3
Product Type Recombinant Antibody
Properties
Clone RM157
Isotype Rabbit IgG
Source/Host Rabbit
Immunogen/Antigen A trimethyl-peptide corresponding to Trimethyl-Histone H3 (Lys79).
Application

Western Blot: 0.2 µg/ml-1 µg/ml
ELISA: 0.1 µg/ml-0.5 µg/ml
Multiplex: 0.1 µg/ml-0.5 µg/ml

Crossreactivity All Vertebrates
Specificity

This antibody reacts to Histone H3 trimethylated at Lysine 79 (K79me3). No cross reactivity with monomethylated Lysine 79 (K79me1) or dimethylated Lysine 79 (K79me2), or other methylations in histone H3.

Purity Protein A purified.
Purity Detail Protein A affinity purified from an animal origin-free culture supernatant.
Concentration 1 mg/ml
Formulation Liquid. 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide.
Isotype Negative Control

Rabbit IgG

Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Accession Number P84243
Declaration Manufactured by RevMab Biosciences.
Shipping and Handling
Shipping BLUE ICE
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS Inquire
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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