H3K79me1 polyclonal antibody
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Specification
Product Description
Rabbit polyclonal antibody raised against synthetic peptide of H3K79me1.
Immunogen
A synthetic peptide (conjugated with KLH) corresponding to region of histone H3 containing the monomethylated lysine 79 (H3K79me1).
Host
Rabbit
Reactivity
Human
Form
Liquid
Recommend Usage
ELISA (1:500-1:1000)
Dot Blot (1:100000)
Western Blot (1:1000)
ChIP (5-10 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 H3K79me1 polyclonal antibody (Cat # PAB14056) in antigen coated wells.
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 : 30,000.Dot Blot
To determine the cross reactivity of H3K79me1 polyclonal antibody (Cat # PAB14056) with other histone H3 modifications, a Dot Blot analysis was performed.
Tested histone H3 modifications include di- and trimethylation of the same lysine and mono-, di- and trimethylation of lysine 9, 27 and 36. One hundred to 0.2 pmol of peptide containing the respective histone modification were spotted on a membrane and detected with the crude serum diluted 1 : 100,000.
Figure shows a high specificity for the modification of interest. -
Publication Reference
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Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling.
Kachirskaia I, Shi X, Yamaguchi H, Tanoue K, Wen H, Wang EW, Appella E, Gozani O.
The Journal of Biological Chemistry 2008 Oct; 283(50):34660.
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High-resolution profiling of histone methylations in the human genome.
Barski A, Cuddapah S, Cui K, Roh TY, Schones DE, Wang Z, Wei G, Chepelev I, Zhao K.
Cell 2007 May; 129(4):823.
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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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Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling.
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