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SRP2144

Sigma-Aldrich

SRC1, receptor interaction domain (627-786), GST tagged human

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

Sinónimos:

F-SRC-1, KAT13A, MGC129719, MGC129720, RIP160, SRC1, bHLHe42, bHLHe74

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.77

biological source

human

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

frozen liquid

mol wt

~44 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

500 μg/mL

color

clear colorless

NCBI accession no.

NM_003743

UniProt accession no.

Q15788

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... NCOA1(8648)

Biochem/physiol Actions

Steroid receptor coactivator 1 (SRC1) is a transcriptional coactivator that mediates the activating functions of many of the nuclear hormone receptors. It is also known as NCoA1 and is a member of the SRC/p160 coactivator family. SRC1 is a 160 kDa protein that contains several LXXLL motifs, which are involved in nuclear receptor interaction. The region 627-786 contains 3 LXXLL motifs that are involved in interaction with nuclear hormone receptors and has been previously used in assays detecting ligand-dependent receptor-cofactor interactions.

Physical form

Clear and colorless frozen liquid solution

Preparation Note

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

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Jianming Xu et al.
Molecular endocrinology (Baltimore, Md.), 17(9), 1681-1692 (2003-06-14)
The p160 steroid receptor coactivator (SRC) gene family contains three homologous members, which serve as transcriptional coactivators for nuclear receptors and certain other transcription factors. These coactivators interact with ligand-bound nuclear receptors to recruit histone acetyltransferases and methyltransferases to specific
S A Oñate et al.
Science (New York, N.Y.), 270(5240), 1354-1357 (1995-11-24)
A yeast two-hybrid system was used to identify a protein that interacts with and enhances the human progesterone receptor (hPR) transcriptional activity without altering the basal activity of the promoter. Because the protein stimulated transactivation of all the steroid receptors
D M Heery et al.
Nature, 387(6634), 733-736 (1997-06-12)
The binding of lipophilic hormones, retinoids and vitamins to members of the nuclear-receptor superfamily modifies the DNA-binding and transcriptional properties of these receptors, resulting in the activation or repression of target genes. Ligand binding induces conformational changes in nuclear receptors

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