Analytical Data
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Gene name
CROP
- Application
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Alternative Names
LUC7L3; LUC7A; CREAP-1; CRA; CRE-Associated Protein; Luc7-like protein 3; Okadaic acid-inducible phosphoprotein OA48-18; cAMP regulatory element-associated protein 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95232
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Expression Region
Met1~Leu247
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Molecular Weight
32kDa
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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
CROP (Cysteine-Rich Oligopeptide) recombinant proteins have garnered significant attention in recent years due to their potential applications in various fields such as medicine, agriculture, and biotechnology. The initial interest in these proteins stems from their unique structural features, which often include high cysteine content that contributes to their stability and functionality. Research has shown that CROP proteins can serve as effective tools for protein engineering, enabling the design of molecules with enhanced properties for therapeutic use, including targeted drug delivery and improved immune response. In agriculture, CROP proteins have been explored for their roles in plant defense mechanisms, making them valuable candidates for developing disease-resistant crops. Advances in recombinant DNA technology have facilitated the production of these proteins in various host systems, enhancing their availability for research and commercial use. Furthermore, the ability to modify their sequences allows scientists to tailor CROP proteins for specific applications, driving innovation in areas such as vaccine development and biopesticides. Overall, the study of CROP recombinant proteins represents a promising frontier in the effort to harness biological molecules for human benefit, leading to breakthroughs in health and sustainability.
