Passa al contenuto
Merck
Tutte le immagini(4)

Documenti fondamentali

H7162

Sigma-Aldrich

Anti-methyl-Histone H3 (Me-Lys9) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Anti-H3K9me1

Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali


About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

Reattività contro le specie

Drosophila, Caenorhabditis elegans, rat, bovine, human, mouse, frog, chicken

tecniche

microarray: suitable
western blot: 1:1,000 using whole cell extract of the human epitheloid carcinoma HeLa cell line

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

monomethylation (Lys9)

Descrizione generale

Histones are proteins that form the nucleosome along with DNA. A nucleosome consists of core histone octamers made of two heterodimers of H2A and H2B along with two heterodimers of H3 and H4. This octamer is bound by the DNA and H1 protein. The HIST3H3 gene is mapped on the human chromosome at 1q42.13.

Specificità

Anti-Methyl-Histone H3 [Me-Lys9] recognizes histone H3 methylated on Lys9.

Immunogeno

synthetic methylated peptide corresponding to amino acids 7-20 [Me-Lys9] of human histone H3. The sequence is identical in many species.

Applicazioni

Anti-methyl-Histone H3 (Me-Lys9) antibody produced in rabbit may be used in immunoblotting.

Azioni biochim/fisiol

Histones H3 and H4 are the predominant histones modified by methylation and are highly methylated in mammalian cells. Lysine residues can be mono-, di-, and tri-methylated, adding further complexity to the regulation of chromatin structure. Conserved lysine residues in the N-terminal tail domains of histone H3, Lys-4, Lys-9 and Lys-27 are the preferred sites of methylation. Methylation of H3 at Lys-9 is a modification intrinsically linked to epigenetic silencing and heterochromatin assembly. Histone H3 is methylated at Lys-9 by site-specific H3 methyltransferases (HMTases) and generates a binding site for heterochromatin protein 1 (HP1).

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

Stoccaggio e stabilità

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots at −20 °C. Repeated freezing and thawing is not recom-mended. Storage in frost-free freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

Esclusione di responsabilità

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.

Non trovi il prodotto giusto?  

Prova il nostro Motore di ricerca dei prodotti.

Prodotti correlati


Scegli una delle versioni più recenti:

Certificati d'analisi (COA)

Lot/Batch Number

Non trovi la versione di tuo interesse?

Se hai bisogno di una versione specifica, puoi cercare il certificato tramite il numero di lotto.

Possiedi già questo prodotto?

I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.

Visita l’Archivio dei documenti

B D Strahl et al.
Nature, 403(6765), 41-45 (2000-01-19)
Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of
J C Rice et al.
Current opinion in cell biology, 13(3), 263-273 (2001-05-10)
Post-translational addition of methyl groups to the amino-terminal tails of histone proteins was discovered more than three decades ago. Only now, however, is the biological significance of lysine and arginine methylation of histone tails being elucidated. Recent findings indicate that

Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..

Contatta l'Assistenza Tecnica.