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CREB binding protein (catalytic domain) (human), (recombinant)

 
BML-SE452-0100 100 µg 531.00 USD
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Product Details

Alternative Name:CBP
 
MW:45.4 kDa
 
Source:Produced in E. coli. Catalytic domain (aa 1319-1710) of human CBP.
 
UniProt ID:Q92793
 
Formulation:Liquid. In 50mM TRIS-HCl, pH 8.0, containing 0.1mM EDTA, 10% glycerol.
 
Purity Detail:Partially purified by single-step affinity chromatography and gel filtration.
 
Specific Activity:≥250 pmol/min/µg assayed as production of CoA-SH from AcCoA in the presence of a peptide comprising human p53 residues 368-386 (Prod. No. BML-P198). CoA-SH is determined colorimetrically by reaction with DTNB (5,5′-Dithiobis(2-nitrobenzoic acid)).
 
Application Notes:Can be used to study CBP kinetics and regulation, for screening for inhibitors or activators and for radiolabeling of proteins or peptides with, for example [3H]-Acetyl CoA.
 
Shipping:Dry Ice
 
Long Term Storage:-80°C
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
 
Scientific Background:Although originally termed histone acetyltransferases (HATs) for their lysine acetylation activity on histone N-terminal tails, CBP and its paralogue, p300, have been shown to acetylate a variety of non-histone proteins including p53, DNA polymerase β and nuclear import factors. p300/CBP acetylations play regulatory roles in transcription, DNA repair and replication, the cell cycle, p53 turnover, and nuclear import. In addition to functions which overlap with those of p300, CBP has a number of unique functions, including a role in p27Kip1 induction.
 
Regulatory Status:RUO - Research Use Only
 
CREB binding protein (catalytic domain) (human), (recombinant) SDS-PAGE
SDS-PAGE Analysis: Lane 1: MW Marker, Lane 2: 1 μg, Lane 3: 2 μg, Lane 4: 5 μg CBP.
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CREB binding protein (catalytic domain) (human), (recombinant) SDS-PAGE

Product Literature References

Regulation of inositol 1, 3, 4-trisphosphate 5/6-kinase (ITPK1) by reversible lysine acetylation: C. Zhang, et al.; Proc. Natl. Acad. Sci. U. S. A. 109, 2290 (2012), Abstract; Full Text

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