Analytical Data
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Gene name
Carbonic Anhydrase 4
- Application
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Alternative Names
CA-IV; CAIV; Car4; RP17; Retinitis Pigmentosa 17(Autosomal Dominant); Carbonate dehydratase IV
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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 95% as determined by SDS-PAGE.
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Uniprot
P22748
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Expression Region
Ala19~Lys283
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Molecular Weight
33kDa
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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 4 (CA4) is an enzyme that plays a critical role in maintaining acid-base balance in various tissues, particularly in the lungs and kidneys. It catalyzes the reversible reaction between carbon dioxide and water to form bicarbonate and protons, thereby facilitating gas exchange and ion transport. The importance of CA4 in physiological processes has made it a target for research in various fields, including respiratory diseases, kidney disorders, and cancer. Mutations or dysregulation of CA4 can lead to pathological conditions, making it imperative to understand its structure and function. Recent advances in recombinant DNA technology have enabled the production of recombinant CA4, allowing for detailed studies of its enzymatic activity and interaction with inhibitors or substrates. This research enhances our understanding of CA4's role in health and disease, paving the way for potential therapeutic interventions. The study of recombinant CA4 not only contributes to basic biochemical knowledge but also holds promise for developing new strategies in treating conditions linked to acid-base imbalances and abnormal carbon dioxide metabolism.
