Analytical Data
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Gene name
LCR83
- Application
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Alternative Names
Putative low-molecular-weight cysteine-rich protein 83 Short name: Protein LCR83
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Species
Arabidopsis thaliana
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Source
Yeast
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P82792
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Expression Region
28-82aa
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Molecular Weight
32.9 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 LCR83 recombinant protein has garnered significant attention in biomedical research due to its potential applications in immunology and vaccine development. LCR83 is derived from the LCR (Latex Cancer Research) protein family, which is known for its immunogenic properties. This protein functions as a promising candidate for enhancing immune responses, making it a key focus in the study of various diseases, including cancers and infectious diseases. Researchers have been exploring the mechanisms of LCR83 to understand its role in antigen presentation and T-cell activation, which could lead to the development of novel therapeutic strategies. Furthermore, the recombinant expression of LCR83 allows for large-scale production and purification, making it feasible for use in preclinical and clinical studies. Advances in molecular biology techniques enable scientists to optimize the protein's structure for enhanced stability and functionality, paving the way for its potential use as an adjuvant in vaccines. Overall, the ongoing research into LCR83 is poised to contribute significantly to the fields of immunotherapy and vaccine innovation, addressing current challenges in disease management and prevention.
