Analytical Data
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Gene name
CELA2A
- Application
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Alternative Names
Elastase-2A
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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
P08217
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Expression Region
29-269aa
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Molecular Weight
29.9 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
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Protein Description
The CELA2A protein, classified as a serine protease, has gained significant attention in the fields of biochemistry and molecular biology due to its potential implications in physiological processes and disease states. CELA2A is primarily expressed in the pancreas and plays a pivotal role in the digestion of dietary proteins, making it a crucial component of the digestive enzyme repertoire. Research has revealed its significance in various pathological conditions, such as pancreatic disorders and inflammation. The study of CELA2A's structure, function, and regulatory mechanisms is essential for understanding its role in health and disease.
Recent advances in recombinant DNA technology have enabled the expression and purification of CELA2A for in-depth functional analyses and structural characterization. These studies aim to elucidate the substrate specificity of CELA2A, its interaction with other biomolecules, and its enzymatic activities. Furthermore, the exploration of CELA2A's role in cellular signaling pathways could lead to potential therapeutic applications, particularly in conditions associated with protease dysregulation. Overall, the ongoing research on CELA2A not only enhances our understanding of digestive physiology but also holds promise for developing novel strategies for treating related disorders.
