Analytical Data
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Gene name
GSC
- Application
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Alternative Names
Goosecoid; goosecoid homeobox; GSC; GSC_HUMAN; Homeobox protein goosecoid
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P56915
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Expression Region
1-257aa
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AA Sequence
MPASMFSIDNILAARPRCKDSVLPVAHSAAAPVVFPALHGDSLYGASGGASSDYGAFYPRPVAPGGAGLPAAVSGSRLGYNNYFYGQLHVQAAPVGPACCGAVPPLGAQQCSCVPTPPGYEGPGSVLVSPVPHQMLPYMNVGTLSRTELQLLNQLHCRRKRRHRTIFTDEQLEALENLFQETKYPDVGTREQLARKVHLREEKVEVWFKNRRAKWRRQKRSSSEESENAEKWNKTSSSKASPEKREEEGKSDLDSDS
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Molecular Weight
54.5 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
Glycoprotein hormones, such as gonadotropin, play a critical role in the regulation of reproductive processes and are essential for maintaining normal physiological functions in both males and females. Among these, glycosylation is a key post-translational modification that significantly influences protein stability, bioactivity, and receptor interaction. Recent advances in recombinant DNA technology have enabled the production of glycoconjugates with specific glycosylation patterns through the use of mammalian cell expression systems. This has sparked a growing interest in the restructuring of glycoproteins, including the development of recombinant versions that can mimic their natural counterparts. Research in this field aims to better understand the structure-function relationship of glycoproteins and to engineer them for therapeutic purposes, such as in fertility treatments or biological assays. Furthermore, the ability to produce homogeneous glycoproteins with controlled glycosylation has important implications for the pharmaceutical industry, where consistency and efficacy are paramount. By exploring the molecular biology and genetics behind glycoprotein synthesis, researchers hope to unlock new avenues for innovation in drug design and development, ultimately leading to enhanced treatment options for reproductive and endocrine disorders. As investigations continue into the complexities of glycoprotein structure and function, the potential for engineered versions of these hormones offers a promising frontier in biomedicine.
