Analytical Data
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Gene name
SRR
- Application
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Alternative Names
SRR;Serine racemase
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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
Q9GZT4
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Expression Region
1-340aa
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AA Sequence
MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
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Molecular Weight
68.1 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
The study of SRR (serum response regulator) recombinant proteins has gained significant attention due to their critical role in various biological processes, including cellular differentiation, proliferation, and response to extracellular signals. SRR proteins are transcription factors that interact with serum response element (SRE) in gene promoters, thereby regulating the expression of immediate early genes involved in muscle development, tissue repair, and stress responses. The increasing interest in understanding the molecular mechanisms of gene regulation has propelled researchers to explore SRR proteins not just in the context of development and physiology, but also in disease models, particularly in cancers and cardiovascular diseases where altered SRR activity has been implicated. Additionally, the ability to produce recombinant SRR proteins allows for the detailed study of their functions and interactions in vitro, paving the way for potential therapeutic applications. Recent advances in genetic engineering techniques, such as CRISPR and recombinant DNA technology, have facilitated the cloning and expression of SRR proteins, enabling researchers to investigate their structural properties and functional dynamics. Moreover, the development of SRR-based biosensors and therapeutic agents is on the rise, making it imperative to continue exploring their potential in both basic and applied biological research. This promising field combines molecular biology, bioengineering, and pharmacology, aiming to unlock new avenues for therapeutic intervention and enhance our understanding of cellular signaling networks.
