目錄:愛必信(上海)生物科技有限公司>>細(xì)胞生物學(xué)>>重組蛋白>> abs04196Recombinant Human/Mouse Activin A
供貨周期 | 一周 | 規(guī)格 | 10ug |
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貨號 | abs04196 |
概述 | |
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描述 | Recombinant Human Activin A is produced by our Mammalian expression system and the target gene encoding Gly311-Ser426 is expressed. |
別名 | Inhibin beta A chain,INHBA,Activin A |
形態(tài) | Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. |
來源 | Human Cells |
氨基酸序列 | GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINH YRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS |
內(nèi)毒素水平 | Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test. |
Accession # | P08476 |
性能 | |
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背景 | Activin and inhibin are two closely related protein complexes that have almost directly opposite biological effects. Activins, members of the TGF-beta superfamily, are disulfide-linked dimeric proteins originally purified from gonadal fluids as proteins that stimulated pituitary follicle stimulating hormone (FSH) release. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Activins are homodimers or heterodimers of the various beta subunit isoforms, while inhibins are heterodimers of a unique alpha subunit and one of the various beta subunits. |
溶解方法 | Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 μg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
保存方法 | Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
純度 | Greater than 95% as determined by reducing SDS-PAGE. |
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