protein

Recombinant Human Estrogen receptor

MBS1265365

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Estrogen receptor

Estrogen receptor

ER-alpha; Estradiol receptor; Nuclear receptor subfamily 3 group A member 1

estrogen receptor isoform 1; Estrogen receptor; estrogen receptor; estrogen receptor 1; ER-alpha; Estradiol receptor; Nuclear receptor subfamily 3 group A member 1

ESR1

ESR1; ESR1; ER; ESR; Era; ESRA; ESTRR; NR3A1; ESR; NR3A1; ER

ESR1_HUMAN

E Coli

9-591

595

ASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSS
KPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEA
AAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHG
QQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRER
LASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCE
GCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRL
RKCYEVGMMKGGIRKDRRGGR

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Transcription

Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform 1

Human oestrogen receptor cDNA sequence, expression and homology to v-erb-A.Green S., Walter P., Kumar V., Krust A., Bornert J.-M., Argos P., Chambon P.Nature 320:134-139(1986) Sequence and expression of human estrogen receptor complementary DNA.Greene G.L., Gilna P., Waterfield M., Baker A., Hort Y., Shine J.Science 231:1150-1154(1986) A novel 80 kDa human estrogen receptor containing a duplication of exons 6 and 7.Pink J.J., Wu S.Q., Wolf D.M., Bilimoria M.M., Jordan V.C.Nucleic Acids Res. 24:962-969(1996) NIEHS SNPs programThe full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Identification, cloning, and expression of human estrogen receptor-alpha36, a novel variant of human estrogen receptor-alpha66.Wang Z., Zhang X., Shen P., Loggie B.W., Chang Y., Deuel T.F.Biochem. Biophys. Res. Commun. 336:1023-1027(2005) The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003)

62821794

NP_000116.2

NP_000116.2

P03372

69kD

Endocrine And Other Factor-regulated Calcium Reabsorption Pathway (213307); Endocrine And Other Factor-regulated Calcium Reabsorption Pathway (213276); Estrogen Signaling Pathway (799177); Estrogen Signaling Pathway (198863); Estrogen Signaling Pathway (799197); FOXA1 Transcription Factor Network Pathway (137979); FOXM1 Transcription Factor Network Pathway (137935); Gene Expression Pathway (1269649); Generic Transcription Pathway (1269650); Integrated Breast Cancer Pathway (219801)

This gene encodes an estrogen receptor, a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding, and activation of transcription. The protein localizes to the nucleus where it may form a homodimer or a heterodimer with estrogen receptor 2. Estrogen and its receptors are essential for sexual development and reproductive function, but also play a role in other tissues such as bone. Estrogen receptors are also involved in pathological processes including breast cancer, endometrial cancer, and osteoporosis. Alternative promoter usage and alternative splicing result in dozens of transcript variants, but the full-length nature of many of these variants has not been determined. [provided by RefSeq, Mar 2014]

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180