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Key Documents

H2292

Sigma-Aldrich

Histone H3.1 human

Sinónimos:

Histone, Human

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About This Item

Número de CAS:
1523001-32-2
UNSPSC Code:
12352202
NACRES:
NA.25

biological source

human

Quality Level

200

recombinant

expressed in E. coli

form

liquid

concentration

1 mg/mL

technique(s)

MALDI-TOF: suitable

UniProt accession no.

P68431

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... H3C1(8350)

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General description

Histone H3.1 is a histone H3 variant. It differs from H3.2 with residue 96 being a cysteine instead of serine. H3.1 is a replication-dependent histone and is a component of nucleosomes during the S-phase.

Application

Histone H3.1 human has been used in in vitro Schizosaccharomyces pombe Set7 histone methyltransferase assay for matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF) studies.

Biochem/physiol Actions

Histone H3.1 human (H3.1) undergoes a majority of post-translational modification especially acetylation and demethylation in lysine 14 and 9 respectively. During differentiation, the levels of H3.1 transcripts decrease as cell division slows down. The incorporation of H3.1 into chromatin is mediated by a chaperone, chromatin assembly factor (CAF-1). A transversion mutation in the H3.1 may be implicated in glioma.

Physical form

Supplied as 1 mg/mL in 20 mM NaPO4, pH 7.0, 0.3 M NaCl, 1 mM EDTA, and 1 mM DTT.

pictograms

Exclamation mark
GHS07

signalword

Warning

hcodes

H319

Hazard Classifications

Eye Irrit. 2

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Sandra B Hake et al.
Proceedings of the National Academy of Sciences of the United States of America, 103(17), 6428-6435 (2006-03-31)
In the history of science, provocative but, at times, controversial ideas have been put forward to explain basic problems that confront and intrigue the scientific community. These hypotheses, although often not correct in every detail, lead to increased discussion that
Yunpeng Shen et al.
Structure (London, England : 1993), 27(4), 631-638 (2019-02-19)
Histone methylation by histone methyltransferases (HMTases) has a key role in transcriptional regulation. Discrepancies between the known HMTases and the histone lysine methylome suggest that HMTases remain to be identified. Here we report the discovery, characterization, and crystal structure of

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