Analytical Data
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Gene name
SRI
- Application
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Alternative Names
SRI;Sorcin
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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
P30626
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Expression Region
1-198aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGS MAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS V
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Molecular Weight
24 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
SRI (Serum Response Factor Interacting) proteins are an intriguing area of research due to their involvement in various cellular processes, including growth, differentiation, and response to mechanical stress. The discovery of SRI proteins, which interact with serum response factor (SRF), highlights their potential role in gene regulation and cellular signaling pathways. As key regulators in muscle development and smooth muscle cell function, these proteins have garnered attention in studies related to cardiovascular diseases and muscle disorders. Researchers have been exploring the biochemical properties of SRI proteins, their downstream effects on gene expression, and their potential as therapeutic targets. Furthermore, understanding the molecular mechanisms through which SRI proteins exert their influence can provide insights into tissue regeneration, developmental biology, and the pathology of diseases characterized by aberrant SRF signaling. With advancements in proteomics and molecular biology techniques, the characterization of SRI protein functions and their interactions continues to evolve, offering promising avenues for innovative treatment strategies in conditions where cellular responsiveness is compromised. This growing body of knowledge not only enriches our understanding of fundamental biological processes but also underscores the significance of SRI proteins in health and disease.
