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Anti-Histone H4 Rabbit Antibody [L22H17]

Catalog No.: F4020

Application: Reactivity: Mouse, Rat, Human, Drosophila melanogaster

Usage Information

Dilution
WB1:1000 IHC1:2000 IF1:100

Application
WB, IHC, IF, ChIP

Reactivity
Mouse, Rat, Human, Drosophila melanogaster

Source
Rabbit

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
11 kDa 11 kDa, 15 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Datasheet & SDS

Biological Description

Specificity
Anti-Histone H4 Rabbit Antibody [L22H17] recognizes total endogenous levels of Histone H4 protein.

Clone
L22H17

Synonym(s)
H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, HIST1H4H, H4C9, H4/M, H4FM, HIST1H4I, H4C11, H4/E, H4FE

Background
Histones are highly conserved DNA-binding proteins that form the structural backbone of chromatin in all eukaryotic cells. They are classified into five main groups: H1/H5, H2A, H2B, H3, and H4. The nucleosome, the fundamental repeating unit of chromatin, consists of two copies each of H2A, H2B, H3, and H4, which assemble into a histone octamer. While once thought to provide only a static scaffold for DNA packaging, the nucleosome is now recognized as a dynamic structure subject to diverse post-translational modifications (PTMs) such as acetylation, phosphorylation, methylation, and ubiquitination. Histone acetylation occurs mainly on lysine residues within the amino-terminal tails of histones—H2A (Lys5), H2B (Lys5, 12, 15, 20), H3 (Lys9, 14, 18, 23, 27, 36, 56), and H4 (Lys5, 8, 12, 16). These modifications regulate key processes including histone deposition, transcriptional activation, DNA replication, recombination, and DNA repair. Importantly, acetylation of specific lysines generates docking sites for bromodomain-containing proteins, enabling them to selectively recognize and bind acetylated histones.

Background

Histones are highly conserved DNA-binding proteins that form the structural backbone of chromatin in all eukaryotic cells. They are classified into five main groups: H1/H5, H2A, H2B, H3, and H4. The nucleosome, the fundamental repeating unit of chromatin, consists of two copies each of H2A, H2B, H3, and H4, which assemble into a histone octamer. While once thought to provide only a static scaffold for DNA packaging, the nucleosome is now recognized as a dynamic structure subject to diverse post-translational modifications (PTMs) such as acetylation, phosphorylation, methylation, and ubiquitination. Histone acetylation occurs mainly on lysine residues within the amino-terminal tails of histones—H2A (Lys5), H2B (Lys5, 12, 15, 20), H3 (Lys9, 14, 18, 23, 27, 36, 56), and H4 (Lys5, 8, 12, 16). These modifications regulate key processes including histone deposition, transcriptional activation, DNA replication, recombination, and DNA repair. Importantly, acetylation of specific lysines generates docking sites for bromodomain-containing proteins, enabling them to selectively recognize and bind acetylated histones.

References
https://pubmed.ncbi.nlm.nih.gov/15268870/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%