DATASHEET
Host:
Rabbit
Target Protein:
H3K4me1
Clonality:
Polyclonal
Isotype:
Not Determined
Entrez Gene:
8350
Swiss Prot:
P68431
Source:
Polyclonal antibody raised in rabbit against histone H3 containing the monomethylated lysine 4 (H3K4me1), using a KLH-conjugated synthetic peptide
Purification:
Whole antiserum from rabbit containing 0.05% azide
Storage Buffer:
0.01M TBS(pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Storage:
Store at -20°C for 12 months.
Background:
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
VALIDATION IMAGES
To determine the titer, an ELISA was performed using a serial dilution of the antibody directed against H3K4me1 (bs-53037R). The antigen used was a peptide containing the histone modification of interest. By plotting the absorbance against the antibody dilution, the titer of the antibody was estimated to be 1:3,800.
Histone extracts of HeLa cells (15 μg) were analyzed by Western blot using H3K4me1 Polyclonal Antibody (bs-53037R) diluted 1:750 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.
A Dot Blot analysis was performed to test the cross-reactivity of the antibody against H3K4me1 (bs-53037R) with peptides containing other modifications or unmodified sequences of histone H3. Other histone modifications include di- and trimethylation of the same lysine and mono-, di- and trimethylation of lysine 9, 27 and 36 and 79. One hundred to 0.2 pmol of the peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. The figure shows a high specificity of the antibody for the modification of interest.