Analytical Data
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Gene name
Gphb5
- Application
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Alternative Names
Gphb5；GPB5；ZLUT1；GlycoProtein hormone beta-5
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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
Q86YW7
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Expression Region
25-130aa
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AA Sequence
ASSGNL RTFVGCAVRE FTFLAKKPGC RGLRITTDAC WGRCETWEKP ILEPPYIEAH HRVCTYNETK QVTVKLPNCA PGVDPFYTYP VAIRCDCGAC STATTECETI
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Molecular Weight
14.2 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
GPHB5 (Glycoprotein Hormone Beta Subunit 5) is a crucial protein involved in the regulation of various physiological processes, particularly in the reproductive system and endocrine functions. As a beta subunit of glycoprotein hormones, GPHB5 contributes to the formation of biologically active hormone complexes, such as those that regulate gonadal function. The study of recombinant GPHB5 has gained significant attention due to its potential applications in reproductive medicine, endocrinology, and biotechnology. By producing recombinant forms of GPHB5 through techniques such as molecular cloning and expression in heterologous systems, researchers aim to elucidate its role in hormone signaling pathways, assess its biological activity, and explore its therapeutic implications. Additionally, understanding the structure-function relationship of GPHB5 can facilitate the design of novel drugs or diagnostic tools for fertility disorders. This research also offers insights into the evolutionary biology of glycoprotein hormones, as GPHB5 is conserved across various species. Overall, the investigation of recombinant GPHB5 presents an opportunity to enhance our understanding of hormone biology and improve clinical practices related to reproductive health.
