Analytical Data
-
Gene name
FSH
- Application
-
Alternative Names
FSH-B; Follitropin Subunit Beta
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01225
-
Expression Region
Asn19~Glu129
-
Molecular Weight
16kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Recombinant follicle-stimulating hormone (FSH) is a key hormone in the regulation of reproductive processes, primarily influencing ovarian follicle development and spermatogenesis. Traditionally, FSH was extracted from the urine of postmenopausal women, which posed limitations in terms of availability, purity, and consistency. The advent of recombinant DNA technology has revolutionized FSH production, allowing for the generation of highly purified, biologically active FSH proteins that mirror the human form. This innovation not only enhances the quality and safety of FSH in clinical settings but also enables precise dosing and standardization for fertility treatments, such as in vitro fertilization (IVF) and ovulation induction. Current research focuses on optimizing the structural and functional properties of recombinant FSH, exploring its role in various treatment protocols, and investigating the potential for improved therapeutic outcomes. Additionally, studies are examining the impact of different glycosylation patterns on FSH's biological activity, as well as the development of long-acting formulations to reduce the frequency of injections. The understanding of FSH’s mechanisms of action at the molecular level is also a pivotal area of investigation, aiming to unravel its intricate signaling pathways and interactions with other hormones. Overall, the development and research surrounding recombinant FSH represent a significant advancement in reproductive medicine, providing hope for individuals facing fertility challenges while pushing the boundaries of hormonal therapies.
