Analytical Data
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Gene name
GH1
- Application
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Alternative Names
GH1；Somatotropin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01241
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Expression Region
27-217aa
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AA Sequence
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
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Molecular Weight
27.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
The GH1 (Growth Hormone 1) protein, a critical peptide hormone synthesized in the pituitary gland, plays a vital role in growth, metabolism, and overall physiological regulation in various species, including humans. Research on GH1 recombinant proteins emerged to address the medical need for growth hormone deficiencies and related disorders. The use of recombinant DNA technology has enabled scientists to produce GH1 in various expression systems, such as bacteria, yeast, and mammalian cells, facilitating the study of its structure, function, and therapeutic potential. Over the years, this research has expanded our understanding of GH1's mechanisms of action, the signaling pathways it influences, and its interactions with receptors. Furthermore, the development of recombinant GH1 has paved the way for the treatment of growth disorders in children and adults, significantly impacting clinical endocrinology. Current investigations focus on optimizing production methods, enhancing the biological activity of recombinant GH1, and exploring novel therapeutic applications. As our knowledge of GH1 continues to evolve, it holds promise for innovative treatments for growth hormone-related conditions and potential implications in wider areas such as metabolic disorders and aging research.
