Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Subsequently, 146 base pairs of DNA are wrapped around the octamer, forming a nucleosome, the basic subunit of chromatin. Histone modifications regulate DNA transcription, repair, recombination, and replication. The most commonly studied modifications are acetylation, phosphorylation, methylation, and ubiquitination. These modifications can alter local chromatin architecture, or recruit trans-acting factors that recognize specific histone modifications (the "histone code" hypothesis). Trimethylation of histone H3 on Lys9 (H3K9me3) is one of the most highly studied epigenetic marks. H3K9me3 functions in the repression of euchromatic genes, and in epigenetic control of heterochromatin assembly, most likely via acting as a recognition motif for the binding of chromatin-associated proteins, such as Swi6 or HP1Alpha/Beta. The enzymes responsible for H3K9me3 formation are SUV39H1 and SUV39H2.

Centromeric histone H3-like protein-1; centromere-specific H3 variant protein; A4PIF0_BRAJU;

Brassica juncea

WB,IHC,IF,ICC,ELISA

WB 1:500-2000
IHC 1:50-1:200
IF 1:100-1:400
ICC 1:100-1:400
ELISA 1:5000-10000

13.6kD

A4PIF0

https://www.uniprot.org/uniprotkb/A4PIF0

KLH conjugated synthetic peptide derived from Brassica juncea Centromeric histone H3-like protein-1

Rabbit

Polyclonal

IgG

affinity purified by Protein A

Liquid

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.