Analytical Data
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基因名
GH
- Application
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别名
GH1;Somatotropin
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种属
HCMVM
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q6SW67
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表达区间
1-742aa
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氨基酸序列
MRPGLPSYLIILAVCLFSHLLSSRYGAEAVSEPLDKAFHLLLNTYGRPIRFLRENTTQCTYNSSLRNSTVVRENAISFNFFQSYNQYYVFHMPRCLFAGPLAEQFLNQVDLTETLERYQQRLNTYALVSKDLASYRSFSQQLKAQDSLGEQPTTVPPPIDLSIPHVWMPPQTTPHGWTESHTTSGLHRPHFNQTCILFDGHDLLFSTVTPCLHQGFYLIDELRYVKITLTEDFFVVTVSIDDDTPMLLIFGHLPRVLFKAPYQRDNFILRQTEKHELLVLVKKDQLNRHSYLKDPDFLDAALDFNYLDLSALLRNSFHRYAVDVLKSGRCQMLDRRTVEMAFAYALALFAAARQEEAGAQVSVPRALDRQAALLQIQEFMITCLSQTPPRTTLLLYPTAVDLAKRALWTPNQITDITSLVRLVYILSKQNQQHLIPQWALRQIADFALKLHKTHLASFLSAFARQELYLMGSLVHSMLVHTTERREIFIVETGLCSLAELSHFTQLLAHPHHEYLSDLYTPCSSSGRRDHSLERLTRLFPDATVPATVPAALSILSTMQPSTLETFPDLFCLPLGESFSALTVSEHVSYIVTNQYLIKGISYPVSTTVVGQSLIITQTDSQTKCELTRNMHTTHSITVALNISLENCAFCQSALLEYDDTQGVINIMYMHDSDDVLFALDPYNEVVVSSPRTHYLMLLKNGTVLEVTDVVVDATDSRLLMMSVYALSAIIGIYLLYRMLKTC
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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.
Quality inspection process
Related Products
Protein Description
Recombinant human growth hormone (rhGH) has garnered significant attention in biomedical research and clinical applications due to its essential role in growth regulation, metabolism, and overall physiological function. Human growth hormone, produced by the pituitary gland, is critical for growth and development during childhood and plays a vital role in modulating various metabolic processes in adults. However, its natural production can be insufficient due to genetic disorders, tumors, or other health conditions, leading to growth deficiencies and metabolic disorders. With advancements in molecular biology techniques, researchers have successfully utilized recombinant DNA technology to produce rhGH in host systems such as bacteria, yeast, and mammalian cells. This innovation not only allows for the large-scale production of biologically active hormone but also enables the exploration of its therapeutic potential in conditions such as dwarfism, adult growth hormone deficiency, and certain muscle-wasting diseases. Moreover, rhGH has gained attention within the fields of sports medicine and anti-aging research, albeit with ethical and regulatory implications. The ongoing investigation into the pharmacodynamics, pharmacokinetics, and safety profiles of rhGH continue to generate insights that enhance its medical applications and contribute to a deeper understanding of its mechanisms of action in human physiology. The expansion of rhGH research stands at the intersection of genetics, endocrinology, and biotechnology, paving the way for innovative treatments and improved healthcare outcomes.
