G9a-like protein (human recombinant)

G9a-like protein (human recombinant)
Item number Size Datasheet Manual SDS Delivery time Quantity Price
Cay10755-50 50 µg - -

6 - 10 business days*

530.00€
 
Post-translational modification of histones by methylation of lysine residues can promote... more
Product information "G9a-like protein (human recombinant)"
Post-translational modification of histones by methylation of lysine residues can promote transcriptional activation or repression. G9a-like protein (GLP) and G9a are SET domain-containing methyltransferases that specifically mono- and di-methylate histone H3 at lysine 9 (H3K9). Methylation of H3K9 by a GLP/G9a heteromeric complex regulates gene expression by silencing euchromatin. GLP and G9a share 80% sequence identity in their SET domains. Structure-activity relationship (SAR) studies have been employed to design potent and selective inhibitors of these proteins, including BIX-01294 and UNC0638, with IC50 values in the nanomolar range.Synonyms: EHMT1, Euchromatic Histone-Lysine N-Methyltransferase 1, Eu HMTase 1, GLP, KMT1D. Purity: >95% estimated by SDS-PAGE. Source: active recombinant N-terminal GST-tagged protein expressed in E. coli. MW: 60.3 kDa. UniProt Accession #: Q9H9B1.
Keywords: GLP, GLP, GLP1, GLP1, EHMT1, EUHMTASE1, Eu-HMTase1, Eu-HMTase1, H3-K9-HMTase 5, H3-K9-HMTase 5, G9a-like protein 1, G9a-like protein 1, Lysine N-methyltransferase 1D, Lysine N-methyltransferase 1D, Histone H3-K9 methyltransferase 5, Histone H3-K9 methyltr
Supplier: Cayman Chemical
Supplier-Nr: 10755

Properties

Application: Enzyme activity
Conjugate: No
Host: E.coli
MW: 60,3 kD
Purity: >95% estimated by SDS-PAGE

Handling & Safety

Storage: -80°C
Shipping: -80°C (International: -80°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
You will get a certificate here
or to request a certificate of analysis.
Read, write and discuss reviews... more
Customer review for "G9a-like protein (human recombinant)"
Write a review
or to review a product.
Viewed