Analytical Data
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Gene name
Saa3
- Application
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Alternative Names
Saa3；LSF；SEF；Alpha-globin transcription factor CP2
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Species
Mouse
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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
P04918
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Expression Region
20-122aa
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AA Sequence
RWVQFMKEAGQGSRDMWRAYSDMKKANWKNSDKYFHARGNYDAARRGPGGAWAAKVISDAREAVQKFTGHGAEDSRADQFANEWGRSGKDPNHFRPAGLPKRY
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Molecular Weight
11.8 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
Saa3, also known as Secreted Acidic cysteine-rich protein 3, is a member of the SA (Secreted Acidic) protein family, which plays crucial roles in various biological processes, including cell adhesion, migration, and tissue remodeling. The research surrounding Saa3 has gained attention due to its potential implications in developmental biology and pathologies such as cancer and tissue repair. Studies have revealed that Saa3 is expressed in various tissues, indicating its importance in physiological and pathological conditions. The protein's structure, characterized by its acidic and cysteine-rich nature, suggests a unique functionality in extracellular environments. Recent advancements in recombinant protein technology have enabled the production of Saa3 in significant quantities, facilitating in-depth studies of its biochemical properties and interactions. Understanding the molecular mechanisms underlying Saa3's function may shed light on its role in extracellular matrix composition and cellular signaling pathways. Furthermore, the potential applications of Saa3 in biomaterial development and regenerative medicine are being explored, making it a promising target for therapeutic intervention. Overall, research on Saa3 not only enhances our understanding of its biological significance but also opens avenues for novel applications in biotechnology and medical research.
