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Key Documents

14-155

Sigma-Aldrich

Histone H1 Protein, 20 mg

Purified bovine Histone H1 protein for use as a substrate in histone modification assays (HAT, HDAC, DNMT) and chromatin assembly studies.

Synonym(s):

Linker Histone H1

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About This Item

UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.32

biological source

bovine

Quality Level

mol wt

Mw 32 kDa

manufacturer/tradename

Upstate®

technique(s)

activity assay: suitable (kinase)

NCBI accession no.

UniProt accession no.

shipped in

dry ice

General description

H1 and related linker histones are important both for maintenance of higher-order chromatin structure and for the regulation of gene expression. Nucleosomal stabilization is provided through the binding of histone H1 to the nucleosomal dyad and the linker DNA entering and exiting the core particle. Additional experimental evidence illustrates the influence of histone H1 on chromatin arrangement and compaction. The family of histone H1 proteins contains five somatic variants (H1.1, H1.2, H1.3, H1.4 and H1.5) which are expressed in nearly all cell types.
Product Source: Lysine rich fraction from calf thymus

Quality

Routinely evaluated by Kinase assay using cdk2/cyclin A, active (14-448) to phosphorylate Histone H1.

Physical form

Sterilized through a 0.2 micron membrane filter

Storage and Stability

1 year at -20°C

Other Notes

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
This product is derived from bovine source. Export of this product to certain countries may be restricted. Please contact Customer Service or your local distributor to inquire about product availability and export options.

Legal Information

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

Disclaimer

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Hyo Kyun Chung et al.
The Journal of biological chemistry, 278(30), 28079-28088 (2003-04-30)
The Gadd45 family of proteins includes Gadd45alpha, MyD118/Gadd45beta, and CR6/OIG37/Gadd45gamma. These proteins play important roles in maintaining genomic stability and in regulating the cell cycle. This study reports the cloning of a novel protein called CR6-interacting factor 1 (CRIF1) which
B Ouyang et al.
The Journal of biological chemistry, 272(45), 28646-28651 (1997-11-14)
Human prk encodes a novel protein serine/threonine kinase capable of strongly phosphorylating casein but not histone H1 in vitro. prk expression is tightly regulated at various levels during different stages of the cell cycle in lung fibroblasts. The Prk kinase
Rocío Montes de Oca et al.
The Journal of biological chemistry, 280(51), 42252-42262 (2005-10-06)
Barrier to autointegration factor (BAF) is an essential conserved double-stranded DNA-binding protein in metazoans. BAF binds directly to LEM domain nuclear proteins (e.g. LAP2, Emerin, and MAN1), lamin A, homeodomain transcription factors, and human immunodeficiency virus type 1-encoded proteins. BAF
J Pan et al.
Oncogene, 29(47), 6245-6256 (2010-08-31)
We report here a novel role for Jun dimerization protein-2 (JDP2) as a regulator of the progression of normal cells through the cell cycle. To determine the role of JDP2 in vivo, we generated Jdp2-knockout (Jdp2KO) mice by targeting exon-1
Rho-dependent Rho kinase activation increases CD44 surface expression and bone resorption in osteoclasts.
Chellaiah, MA; Biswas, RS; Rittling, SR; Denhardt, DT; Hruska, KA
The Journal of Biological Chemistry null

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