Analytical Data
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Gene name
Emb
- Application
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Alternative Names
Emb；Embigin
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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
Q6PCB8
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Expression Region
1-327aa
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AA Sequence
MRALPGLLEARARTPRLLLLQCLLAAARPSSADGSAPDSPFTSPPLREEIMANNFSLESHNISLTEHSSMPVEKNITLERPSNVNLTCQFTTSGDLNAVNVTWKKDGEQLENNYLVSATGSTLYTQYRFTIINSKQMGSYSCFFREEKEQRGTFNFKVPELHGKNKPLISYVGDSTVLTCKCQNCFPLNWTWYSSNGSVKVPVGVQMNKYVINGTYANETKLKITQLLEEDGESYWCRALFQLGESEEHIELVVLSYLVPLKPFLVIVAEVILLVATILLCEKYTQKKKKHSDEGKEFEQIEQLKSDDSNGIENNVPRHRKNESLGQ
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Molecular Weight
36.8 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
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Protein Description
Embryonic (Emb) proteins, particularly those associated with embryonic stem cells, have garnered significant attention in recent years due to their essential roles in development and potential therapeutic applications. These proteins are critical for maintaining pluripotency and self-renewal capabilities of stem cells, making them pivotal in early embryogenesis. The study of Emb proteins extends beyond basic developmental biology; it intersects with regenerative medicine, cancer research, and tissue engineering. Understanding the mechanisms governing their expression and function can unveil insights into cellular differentiation processes and the molecular underpinnings of various diseases. For example, abnormalities in Emb protein function may contribute to oncogenesis or developmental disorders. Advances in molecular biology and genetics have enabled researchers to manipulate these proteins in experimental settings, leading to innovative approaches for tissue regeneration and repair. As such, the ongoing investigation into Emb proteins not only enriches our knowledge of fundamental biological processes but also holds promise for developing novel therapies to address a range of medical challenges, including organ failure and degenerative diseases. These insights pave the way for potential applications in personalized medicine, where harnessing the unique properties of Emb proteins could lead to tailored treatments for individual patients. Thus, the study of Emb proteins represents a promising frontier in biomedical research, intertwining basic science with practical applications in human health.
