Analytical Data
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Gene name
CRISP-1
- Application
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Alternative Names
AEGL1; ARP; CRISP-1; HSCRISP1D; HSCRISP1G; HUMARP; Acidic Epididymal Glycoprotein-like 1; Acidic epididymal glycoprotein homolog; AEG-like protein
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P12020
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Expression Region
Gln20~His246
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Molecular Weight
30kDa
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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
CRISP-1 (Cysteine-Rich Secretory Protein 1) is a member of the CRISP protein family, which plays crucial roles in various biological processes, including immune response, reproduction, and cell signaling. The study of CRISP-1 is particularly significant in the context of its potential therapeutic applications and its involvement in parasitic infections, particularly with the Schistosoma genus. Research has shown that CRISP-1 can interact with host immune cells, modulating immune responses and promoting parasite survival within the host. As such, understanding the structure and function of CRISP-1 is essential for developing new strategies for disease prevention and treatment. Furthermore, its unique cysteine-rich domains and ability to form disulfide bonds highlight its potential as a model for protein engineering and drug design. Investigating the recombinant expression of CRISP-1 provides insights into its functional mechanisms and paves the way for potential applications in biotechnology and medicine. Recent advances in recombinant DNA technology have enabled the production of CRISP-1 in various expression systems, facilitating its purification and characterization. This growing body of research aims not only to elucidate the role of CRISP-1 in host-parasite interactions but also to explore its potential as a biomarker or therapeutic target in infectious diseases and other pathological conditions.
