Analytical Data
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Gene name
FSH
- Application
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Alternative Names
FSH；Follitropin subunit beta
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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
P23945
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Expression Region
18-366AA
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AA Sequence
CHHRICHCSNRVFLCQESKVTEIPSDLPRNAIELRFVLTKLRVIQKGAFSGFGDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQNLPNLQYLLISNTGIKHLPDVHKIHSLQKVLLDIQDNINIHTIERNSFVGLSFESVILWLNKNGIQEIHNCAFNGTQLDELNLSDNNNLEELPNDVFHGASGPVILDISRTRIHSLPSYGLENLKKLRARSTYNLKKLPTLEKLVALMEASLTYPSHCCAFANWRRQISELHPICNKSILRQEVDYMTQARGQRSSLAEDNESSYSRGFDMTYTEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILR
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Molecular Weight
44.0 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
Follicle-stimulating hormone (FSH) is a key glycoprotein hormone involved in the regulation of reproductive processes, primarily influencing ovarian follicle development in females and spermatogenesis in males. The significance of FSH in fertility treatments and its potential therapeutic applications have spurred extensive research into the production and characterization of recombinant FSH proteins. Traditional methods of obtaining FSH from human sources are limited by ethical considerations and availability, leading to increased interest in recombinant DNA technology as a sustainable alternative. Utilizing mammalian cell systems for the expression of recombinant FSH allows for proper folding, glycosylation, and bioactivity, which are essential for its physiological function. Research has focused on optimizing production methods, improving yields, and enhancing the pharmacokinetic properties of recombinant FSH. Moreover, understanding the molecular structure and dynamics of FSH has paved the way for the development of more efficient and less immunogenic forms of the hormone, which can potentially minimize side effects in clinical settings. As a result, recombinant FSH has become an integral component in assisted reproductive technologies such as in vitro fertilization (IVF), highlighting its pivotal role in modern reproductive medicine. This ongoing research not only contributes to fertility treatments but also provides insights into hormonal regulation and reproductive health, emphasizing the importance of FSH as a target for therapeutic innovation in reproductive endocrinology.
