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SRP0486

Sigma-Aldrich

Bromodomain Non-Acetylated Ligand 1

≥95% (HPLC)

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0.5 ML
CN¥7,062.48

CN¥7,062.48


Estimated to ship onNovember 11, 2025Details


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0.5 ML
CN¥7,062.48

About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

CN¥7,062.48


Estimated to ship onNovember 11, 2025Details


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Assay

≥95% (HPLC)

form

aqueous solution

mol wt

2602.1 kDa

packaging

pkg of 5 mL

shipped in

dry ice

storage temp.

−20°C

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This Item
SRP0485SRP0484SRP0402
assay

≥95% (HPLC)

assay

≥95% (HPLC)

assay

≥95% (HPLC)

assay

≥90% (HPLC)

form

aqueous solution

form

aqueous solution

form

aqueous solution

form

aqueous solution

packaging

pkg of 5 mL

packaging

pkg of 5 mL

packaging

pkg of 5 mL

packaging

pkg of 80 nmol

mol wt

2602.1 kDa

mol wt

2765.3 kDa

mol wt

2728.2 kDa

mol wt

-

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−70°C

General description

The Bromodomain Non-acetylated Ligand 1 is peptide histone H4 (1-21). It contains an C-terminal GG linker, followed by a biotinylated Lys. Bromodomains function as acetyl-lysine binding domains, and bromodomain/acetyl-lysine recognition can regulate histone modification, DNA replications, chromatin remodeling, and gene transcription. This peptide is suitable for use as a ligand for several bromodomains including members of the BET bromodomain family: BRD2, BRD3, BRD4, and BRDT. It contains an C-terminal GG linker, followed by a biotinylated Lys. Bromodomains function as acetyl-lysine binding domains, and bromodomain/acetyl-lysine recognition can regulate histone modification, DNA replications, chromatin remodeling, and gene transcription. This peptide is suitable for use as a negative control for several bromodomains including ATAD2 and BAZ2B.

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Pil-Hoon Park et al.
American journal of physiology. Gastrointestinal and liver physiology, 289(6), G1124-G1136 (2005-08-06)
Ethanol treatment increases gene expression in the liver through mechanisms that are not clearly understood. Histone acetylation has been shown to induce transcriptional activation. We have investigated the characteristics and mechanisms of ethanol-induced histone H3 acetylation in rat hepatocytes. Immunocytochemical

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