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SRP0479

Sigma-Aldrich

GCN5 (727-837) human

recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥90% (SDS-PAGE)

form

aqueous solution

mol wt

14.1 kDa

packaging

pkg of 100 μg

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... KAT2A(2648)

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SRP0449SRP0448SRP0455
GCN5 (727-837) human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

Sigma-Aldrich

SRP0479

GCN5 (727-837) human

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

≥88% (SDS-PAGE)

form

aqueous solution

form

aqueous solution

form

aqueous solution

form

aqueous solution

mol wt

14.1 kDa

mol wt

40 kDa

mol wt

13.7 kDa

mol wt

14.9 kDa

packaging

pkg of 100 μg

packaging

pkg of 100 μg

packaging

pkg of 100 μg

packaging

pkg of 100 μg

General description

Human GCN5 or KAT2A containing bromodomain (GenBank Accession No. NM_021078) amino-acids 727 – 837 (end) with N-terminal HIS-tag, MW = 14.1 kDa, expressed in an E. coli expression system.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Shanshan Li et al.
The Journal of biological chemistry, 284(14), 9411-9417 (2009-02-17)
Bromodomains are acetyl lysine binding modules found in many complexes that regulate gene transcription. In budding yeast, the coactivator complex SAGA (Spt-Ada-Gcn5-acetyl-transferase) predominantly facilitates transcription of stress-activated genes and requires the bromodomain of the Gcn5 subunit for full activation of
Donna A Santillan et al.
Cancer research, 66(20), 10032-10039 (2006-10-19)
A critical unanswered question about mixed lineage leukemia (MLL) is how specific MLL fusion partners control leukemia phenotype. The MLL-cyclic AMP-responsive element binding protein-binding protein (CBP) fusion requires both the CBP bromodomain and histone acetyltransferase (HAT) domain for transformation and

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