Analytical Data
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Gene name
CA2/Carbonic anhydrase II
- Application
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Alternative Names
CA-II; CAII; Car2; CAC; Carbonate dehydratase II; Carbonic anhydrase C
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Species
Chicken
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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
P07630
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Expression Region
Met1~Gln260
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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
Carbonic anhydrase II (CA2) is an enzyme that plays a crucial role in various physiological processes, including respiration, acid-base balance, and ion transport. It catalyzes the reversible hydration of carbon dioxide to bicarbonate and protons, a reaction essential for maintaining pH homeostasis in biological systems. CA2 is found in high concentrations in red blood cells, kidneys, and other tissues, reflecting its importance in facilitating gas exchange and metabolic functions. Due to its pivotal role in these processes, CA2 has garnered significant attention in biomedical research, particularly in relation to conditions like glaucoma, osteoporosis, and certain cancers, where its activity can be dysregulated. Recombinant CA2 protein is increasingly utilized in structural biology and biochemistry studies to elucidate its mechanism of action, protein dynamics, and interactions with other biomolecules. Moreover, understanding CA2's structure-function relationships is essential for developing therapeutic inhibitors that can selectively target this enzyme to treat various diseases. Recent advances in recombinant DNA technology enable the production of high-purity CA2 for in-depth studies, fostering exploration into its functional roles and potential applications in medicine and biotechnology. Overall, the study of CA2 and its recombinantly produced protein forms is critical for advancing our understanding of fundamental biochemical pathways and developing novel therapeutic strategies.
