Purified anti-HDAC1 Phospho Ser406 Antibody, HDAC1, BT-15,BioLegend,611001

When tested for western blot, this clone produced a band that showed a ~1-3 kD mass shift compared to a pan HDAC1 antibody. This observation is consistent with a previous study of the HDAC1 Phospho (Ser406) site.This clone recognizes zebrafish HDAC1 phosphorylated at Ser4062.Clone BT-15 cross-reacts to Zebrafish2

Host

Mouse

Reactivity

Human, Zebrafish

Application

WB -Quality testedICFC -Verified

Platform ID

BAB961185520

BioLegend

Headquarters

8999 BioLegend Way San Diego, CA 92121 United States

Contact

Tel: 1-858-455-9588
Fax: +49 (4131) 7023913

Email:

Product Specifications
Scientific Background

Specifications

NamePurified anti-HDAC1 Phospho Ser406 Antibody, HDAC1, BT-15
Cat. No.611001
HostMouse
RRIDAB_2801111 (BioLegend Cat. No. 611001)AB_2801112 (BioLegend Cat. No. 611002)
IsotypeMouse IgG2b, κ
ReactivityHuman, Zebrafish
ApplicationWB -Quality testedICFC -Verified
ClonalityMonoclonal
Clone NumberBT-15
Concentration0.5 mg/ml
TargetHDAC1 Phospho Ser406
ImmunogenSynthetic peptide corresponding to human HDAC1 phosphorylated at Serine 406
PurityThe antibody was purified by affinity chromatography.
FormulationPhosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
StorageThe antibody solution should be stored undiluted between 2°C and 8°C.
Regulatory StatusResearch Use Only

Scientific Background

Histone Deacetylase 1 (HDAC1) plays a critical role in various cellular processes, including cell cycle progression, proliferation, and differentiation. The enzyme functions by removing acetyl moieties from histone targets, resulting in histone compaction and alterations in nucleosomal positioning.  Aurora kinases phosphorylate HDAC1 at Ser406 during prophase, immediately after cells begin mitosis, resulting in reduced deacetylase activity of HDAC1. This modification plays an essential role in regulating cell cycle progression, as well as controlling the expression of genes involved in central nervous system development.

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