Anti-phospho-Histone H1 Antibody

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Format: Purified

Immunoaffinity Purified immunoglobulin in 0.02M Phosphate Buffer, 0.25 M NaCl, pH 7.6 with 15 mg/mL BSA containing no preservatives.

Protein A purified

Maintain for 2 years at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Control
Positive Antigen Control: Catalog #12-309, Hela cell nuclear extract. Add an equal volume of Laemmli reducing sample buffer to 10 μL of extract and boil for 5 minutes to reduce the preparation. Load 20 μg of reduced extract per lane for minigels.

Immunoblot Analysis: 0.5-2 μg/mL detected phosphorylated Histone H1 from acid extracts of colcemid treated HeLa cells but not untreated HeLa cells (Catalog # 17-306).

Immunocytochemistry: 5-10 μg/mL showed positive immunostaining for Histone H1 in mitotic HeLa cells fixed with 95% ethanol/5% glacial acetic acid (v/v).

Anti-phospho-Histone H1 Antibody is a high quality Rabbit Polyclonal Antibody for the detection of phospho-Histone H1 & has been validated in ICC & WB.

Research Category
Epigenetics & Nuclear Function

Research Sub Category
Histones

Recognizes phospho-Histone H1, Mr 32 kDa. Additional proteins were also detected, Mr 66 and 100 kDa.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

32 kDa

Histone H1 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H1 is involved with the structure of the nucleosomes of the ′beads on a string′ structure.

The N-terminal tail of histone H1 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.

Hyper-phosphorylated isoform of tetrahymena Histone H1 purified by cation-exchange HPLC