H3K79me2 polyclonal antibody
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Specification
Product Description
Rabbit polyclonal antibody raised against synthetic peptide of H3K79me2.
Immunogen
A synthetic peptide (conjugated with KLH) corresponding to region of histone H3 containing the dimethylated lysine 79 (H3K79me2).
Host
Rabbit
Reactivity
Human
Form
Liquid
Recommend Usage
ELISA (1:200)
Dot Blot (1:50000)
Western Blot (1:250)
ChIP (7 ul/ChIP )
The optimal working dilution should be determined by the end user.Storage Buffer
In serum (0.05% sodium azide)
Storage Instruction
Store at -20°C. For long term storage store at -80°C.
Aliquot to avoid repeated freezing and thawing.Note
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Applications
ChIP
Western Blot
Enzyme-linked Immunoabsorbent Assay
ELISA was performed using a serial dilution of H3K79me2 polyclonal antibody (Cat # PAB14047).
The antigen used was a peptide containing the histone modification of interest.
By plotting the absorbance against the antibody dilution, the titer of the crude serum was estimated to be 1 : 4,500.Dot Blot
A Dot Blot analysis was performed to test the cross reactivity of H3K79me2 polyclonal antibody (Cat # PAB14047) with other modifications of histone H3.
Other H3 modifications include mono- and trimethylation of the same lysine and mono-, di- and trimethylation of lysine 9, 27 and 36.
One hundred to 0.2 pmol of the peptide containing the respective histone modification were spotted on a membrane.
The antibody was used at a dilution of 1 : 50,000.
Figure shows a high specificity of the crude serum for the modification of interest. -
Publication Reference
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Specific histone modification responds to arsenic-induced oxidative stress.
Ma L, Li J, Zhang Z, Chen L, Li D, Bai Q, Gao C, Li J, Zeng X, He Z, Wang S, Xiao Y, Zhang A, Chen W.
Toxicology and Applied Pharmacology 2016 Jul; 302:52.
Application:S-ELISA, Human, Peripheral blood lymphocytes.
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Dynamic regulation of histone lysine methylation by demethylases.
Shi Y, Whetstine JR.
Molecular Cell 2007 Jan; 25(1):1.
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Intra- and inter-nucleosomal protein-DNA interactions of the core histone tail domains in a model system.
Zheng C, Hayes JJ.
The Journal of Biological Chemistry 2003 Apr; 278(26):24217.
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Translating the histone code.
Jenuwein T, Allis CD.
Science 2001 Aug; 293(5532):1074.
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Specific histone modification responds to arsenic-induced oxidative stress.
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