Analytical Data
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Gene name
xsc
- Application
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Alternative Names
/
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Species
Rhizobium meliloti
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92UW6
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Expression Region
1-341aa
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Molecular Weight
44.2 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
The research on XSC recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including biotechnology and medicine. XSC, or Xenopus laevis Swimming Crab, represents a unique source of proteins that can be utilized for the development of novel therapeutic agents and diagnostic tools. Recombinant protein technology enables the production of these proteins in host organisms, allowing for large-scale generation and efficient purification. The understanding of XSC's molecular structure and functions is crucial for elucidating its biological roles and exploring its utility in enzyme engineering, vaccine development, and drug delivery systems. Moreover, studying XSC recombinant proteins can contribute to insights into evolutionary biology, as they may exhibit specific adaptations that could inform the development of biotechnological applications. The ongoing research aims to overcome challenges associated with expression systems and optimize the functional properties of XSC-derived proteins, thereby expanding their commercial viability and enhancing their effectiveness in clinical and research contexts. Overall, the exploration of XSC recombinant proteins holds promise for advancing scientific knowledge and addressing practical challenges in various disciplines.
