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
27.2 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
GH1, or Growth Hormone 1, is a crucial peptide hormone that plays a significant role in growth, metabolism, and overall physiological regulation in various species, including humans. Research on GH1 recombinant protein has gained considerable attention due to its potential applications in both medicine and biotechnology. The recombinant production of GH1 allows for the development of therapeutic interventions for growth hormone deficiencies, which can lead to various health issues, including stunted growth and metabolic disorders. Moreover, GH1 is also utilized in agricultural biotechnology to enhance livestock growth rates and improve feed efficiency. The challenges associated with conventional extraction methods from pituitaries, including ethical concerns and low yield, have prompted researchers to explore recombinant DNA technology as a more efficient and sustainable alternative. Through various expression systems such as bacteria, yeast, and mammalian cells, scientists have successfully produced GH1 with bioactivity comparable to its natural counterpart. This advancement not only facilitates large-scale production but also ensures the safety and consistency of the hormone for therapeutic use. Furthermore, ongoing studies are examining the nuanced molecular mechanisms of GH1 action, its receptor interactions, and the implications of GH1 in various metabolic pathways. Overall, the research on GH1 recombinant protein not only holds promise for clinical applications in treating hormonal deficiencies but also contributes to enhanced agricultural practices.
