Analytical Data
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Gene name
hormone
- Application
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Alternative Names
; Prothoracicotropic hormone; PTTH) [Cleaved into: P2K; P6K; Prothoracicotropic hormone]
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Species
Bombyx mori
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17219
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Expression Region
116-224aa
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Molecular Weight
16.7 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
Hormone recombinant proteins represent a significant advancement in biotechnology and medicine, primarily aimed at addressing hormone deficiencies and metabolic disorders. In the late 20th century, the advancement in recombinant DNA technology enabled scientists to clone genes responsible for hormone production, leading to the synthesis of hormones such as insulin, human growth hormone, and erythropoietin in bacterial or yeast systems. This innovation not only allowed for the mass production of these crucial proteins but also ensured a safer and more controlled source compared to extraction from human or animal tissues, which posed risks of contamination and variability. Researchers have since focused on optimizing expression systems, refining purification techniques, and enhancing the biological activity of these recombinant proteins to mimic natural hormones more closely. Furthermore, the development of engineered variants and fusion proteins has enhanced the pharmacokinetics and therapeutic efficacy, improving patient outcomes in clinical settings. As a result, hormone recombinant proteins are now integral in treating conditions like diabetes, growth disorders, and anemia, highlighting their pivotal role in modern therapeutic strategies and ongoing research into novel hormone therapies.
