关键信息
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基因名
Follistatin/FST
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简介
Follistatin (FST) is a regulator of TGFβ family signaling and acts by selectively binding to TGFβ family ligands and preventing ligand binding to the receptor complex. Follistatin has the ability to suppress the follicle stimulating hormone (FSH)[1][2]. Follistatin/FST Protein, Human (HEK293, His) is produced in HEK293 cells with six C-Terminal His-tags. It consists of 288 amino acids (G30-N317).
- 应用
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别名
follistatin isoform FS288; FS-288; Follistatin; FS; FSActivin-binding protein; FST
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种属
Human
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表达系统
HEK293
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标签
C-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P19883-2
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表达区间
G30-N317
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氨基酸序列
GNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCN
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蛋白长度
Partial
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分子量
33-42 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
质检流程
相关产品
背景信息
Follistatin (FST) is a powerful glycoprotein that functions primarily as an antagonist of members of the transforming growth factor-beta (TGF-β) superfamily, particularly activins and myostatin. The research on FST has gained significant momentum due to its implications in various biological processes, including muscle growth, reproductive functions, and tissue repair. Follistatin's ability to inhibit myostatin—a negative regulator of muscle mass—has attracted attention in the field of muscle physiology and regenerative medicine, as potential therapies targeting FST may enhance muscle growth in conditions such as muscular dystrophy and age-related muscle wasting. Additionally, FST plays a vital role in regulating fibrosis and inflammation, making it a promising candidate for therapeutic interventions in fibrotic diseases and metabolic disorders. Advances in recombinant DNA technology have enabled the production of recombinant FST proteins, facilitating the exploration of their therapeutic potential through preclinical and clinical studies. As a result, ongoing research aims to elucidate the precise mechanisms of FST action, optimize its therapeutic applications, and investigate its role in various diseases, paving the way for innovative strategies to manipulate muscle and tissue health.
