Analytical Data
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Gene name
SSR1
- Application
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Alternative Names
SSTR1;Somatostatin receptor type 1
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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
P43307
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Expression Region
22-207aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSRGGPRGL LAVAQDLTED EETVEDSIIE DEDDEAEVEE DEPTDLVEDK EEEDVSGEPE ASPSADTTIL FVKGEDFPAN NIVKFLVGFT NKGTEDFIVE SLDASFRYPQ DYQFYIQNFT ALPLNTVVPP QRQATFEYSF IPAEPMGGRP FGLVINLNYK DLNGNVFQDA VFNQTVTVIE REDGLDGET
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Molecular Weight
23 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
SSR1, a key protein associated with the endoplasmic reticulum (ER), plays a crucial role in the regulation of protein synthesis and folding. Its significance arises from its involvement in the biogenesis of essential membrane proteins and secretory proteins, thereby influencing various cellular processes. Research has highlighted the importance of SSR1 in maintaining ER homeostasis and its potential implications in disease states, particularly in neurodegenerative disorders, where protein misfolding and aggregation are prominent. By studying SSR1 recombinant protein, scientists aim to elucidate its structure-function relationships, enabling insights into its mechanisms of action and interactions with other cellular components. Furthermore, SSR1 serves as a valuable tool for biotechnological applications, including the development of recombinant proteins. Understanding SSR1's functional roles could pave the way for therapeutic strategies that target ER-related pathologies and enhance protein production in industrial settings. Thus, the exploration of SSR1 and its recombinant forms is vital for advancing both fundamental biological knowledge and practical applications in medicine and biotechnology.
