Analytical Data
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Gene name
FSHb
- Application
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Alternative Names
FSHb；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
P01225
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Expression Region
1-129aa
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AA Sequence
MKTLQFFFLFCCWKAICCNSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE
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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
FSHb, or fetal sheep hemoglobin, is a fetal hemoglobin variant that has garnered significant interest in biomedical research due to its unique properties and potential therapeutic applications. Research into FSHb began in the context of understanding the oxygen transport mechanisms in fetal sheep, which possess a distinct form of hemoglobin during development. This variant exhibits higher oxygen affinity compared to adult hemoglobin, allowing fetuses to effectively extract oxygen from maternal blood in low-oxygen environments. The biochemical and genetic analysis of FSHb not only enhances our understanding of hemoglobin structure-function relationships but also sheds light on disorders like sickle cell anemia and thalassemia, where hemoglobin dysfunction is a critical factor. Moreover, the exploration of FSHb provides insights into potential treatments, such as gene therapy and protein engineering approaches to develop modified hemoglobin variants for therapeutic use, targeting conditions associated with inadequate oxygen transport. Consequently, FSHb research continues to be a focal point for innovations in medicine, particularly in the development of blood substitutes and improved therapies for hemoglobinopathies.
