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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
- 保质期:
Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
- 英文名:
Recombinant Human Estrogen receptor (ESR1), partial
- 库存:
200
- 供应商:
武汉华美生物工程有限公司
- 规格:
1mg/100μg/20μg
| 规格: | 1mg | 产品价格: | ¥12060.0 |
|---|---|---|---|
| 规格: | 100μg | 产品价格: | ¥2820.0 |
| 规格: | 20μg | 产品价格: | ¥1500.0 |
纯度:
Greater than 90% as determined by SDS-PAGE.基因名:
ESR1Uniprot No.:
P03372别名:
ER-alphaEstradiol receptor;Nuclear receptor subfamily 3 group A member 1种属:
Homo sapiens (Human)蛋白长度:
Partial来源:
Yeast分子量:
31.5 kDa表达区域:
315-551aa氨基酸序列:
MVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHA蛋白标签:
C-terminal 6xHis-Myc-tagged产品提供形式:
Liquid or Lyophilized powder缓冲液:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.货期:
25-35 business days注意事项:
Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.功能:
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 elent (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 elent 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 elents; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates mbrane-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内毒素:
Not test.SDS-PAGE:
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.LC-MS Image Description/Western Blot:
/Product types:
Developed ProteinBiological_Activity:
/Research Areas:
TranscriptionReconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.Reference:
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)Function:
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文献和实验Nature 深度剖析:管坤良与 Alj 组研究成果为何截然相反,Hippo 通路调控乳腺癌的两面性
maintains ER expression and ER+ breast cancer growth 的文章,提出了与上文结果截然相反的结论 —— 抑癌激酶 LATS1/2 反而促进 ESR1(ERα 编码基因)的表达,从而驱动 ER + 乳腺癌的发展。 图片来源:Nature本文作者首先通过 CRISPR 同时敲除了 MCF-7 细胞中的 LATS1/2,然而意外的是,细胞生长竟然停滞了,且 ESR1 mRNA 水平和 ERα 蛋白水平大幅下降。但 Alj 组文章中,LATS1/2 仅在蛋白水平上降解
Characterization of Nuclear Receptor Ligands by Multiplexed Peptide Interactions
., and McDonnell, D.P. 1999. Peptide antagonists of the human estrogen receptor. Science 285:744‐746. Northrop, J.P., Nguyen, D., Piplani, S., Olivan, S.E., Kwan, S.T., Go, N.F., Hart, C
Steroid hormones, such as estrogen, progesterone, androgens, glucocorticoids, and mineralocorticoids, are well-known regulators of the expression of specific gene networks in higher eukaryotes (1 –3 ). The hormonal action is mediated
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