CREB Binding Protein bromodomain (1081-1197 aa) (GST-tagged), Human recombinant

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SKU:
7659-20
€185
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Description

CREB Binding Protein bromodomain (1081-1197 aa) (GST-tagged), Human recombinant is available at Gentaur for Next week delivery.

A bromodomain modulating the stability and function of tumor suppressor protein p53

Biomolecule/Target: CREBBP

Alternates names: cAMP-responsive element-binding protein 1 CREB-1; CBP; CREBBP

Synonyms: cAMP-responsive element-binding protein 1 CREB-1; CBP; CREBBP

Background Information: The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. A bromodomain is a protein domain that recognizes acetylated lysine residues such as those on the N-terminal tails of histones. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. These domains function in the linking of protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. Thus, bromodomains serve as “readers” of histone acetylation marks regulating the transcription of target promoters. The cAMP response element-binding protein (CREB) binding protein (CREBBP) bromodomain has been shown to modulate the stability and function of the tumor suppressor protein p53. CREBBP bromodomain recognizes the acetylated lysine residue 382 on p53. This product contains the bromodomain region of CREBBP.

Reconstitution Instructions: N/A

NCBI Gene Symbol: CREBBP

Gene ID: 1387

NCBI Accession: Q92793

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Additional Information

Size:
20 μg
Country of Manufacturing Origin:
USA
Country of Animal Origin:
USA
Gene Source:
Human
Recombinant:
Yes
Source:
E. coli
Purity by SDS-PAGE:
≥95%
Assay:
SDS-PAGE
Purity:
N/A
Assay 2:
HPLC
Endotoxin Level:
N/A
Activity (Specifications/test method):
N/A
Biological activity:
N/A
Results:
N/A
Molecular Weight:
40.8 kDa (1081-1197 aa + NT GST Tag)
Storage Temperature:
-80°C
Shelf Life:
12 months
Concentration:
N/A
Appearance:
Liquid
Handling:
Centrifuge the vial prior to opening.
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