Analytical Data
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Gene name
Carbonic Anhydrase 7
- Application
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Alternative Names
CA-VII; CAVII; Carbonate dehydratase VII
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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
B2RZ61
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Expression Region
Arg29~Asp173
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Molecular Weight
17kDa
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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 7 (CA7) is a member of the carbonic anhydrase family of enzymes, which are crucial for regulating bicarbonate and pH levels in biological systems. This enzyme facilitates the reversible hydration of carbon dioxide to bicarbonate, playing a vital role in various physiological processes, including respiration, acid-base balance, and ion transport. CA7 is particularly interesting due to its exclusive expression in the kidney and testis, indicating its potential involvement in renal function and reproductive processes. Research has suggested that CA7 might contribute to the pathology of various diseases, including renal disorders and certain cancers, making it a target for therapeutic interventions. Despite its importance, the structural and functional characterization of CA7 remains limited, with few studies exploring its enzymatic activity and interactions with other biomolecules. Recombinant expression of CA7 in heterologous systems, such as E. coli or yeast, allows for the production of the protein in sufficient quantities for biochemical studies, structure-function analysis, and potential drug design. By elucidating the properties and mechanisms of CA7, researchers aim to deepen the understanding of its biological roles and explore its potential as a biomarker or therapeutic target in disease states. Thus, the study of recombinant CA7 protein is not only essential for grasping its fundamental biological functions but also for paving the way towards novel clinical applications and interventions.
