Analytical Data
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Gene name
Carbonic Anhydrase 1
- Application
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Alternative Names
rHuCarbonic Anhydrase 1, His; Carbonic Anhydrase 1; Carbonate Dehydratase I; Carbonic Anhydrase B; CAB; Carbonic Anhydrase I; CA1
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Species
Human
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P00915
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Expression Region
A2-F261
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AA Sequence
ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASFHHHHHH
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Protein Length
Full Length of Mature Protein
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Molecular Weight
25-35 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
Carbonic Anhydrase 1 (CA1) is an enzyme that has garnered significant attention in biochemical and medical research due to its pivotal role in the regulation of pH and CO2 concentration in biological systems. This enzyme catalyzes the reversible hydration of carbon dioxide to bicarbonate and protons, which is crucial for various physiological processes, including respiration, acid-base balance, and photosynthesis in plants. Its dysfunction has been linked to numerous pathological conditions, including glaucoma, epilepsy, and certain types of cancer, making it a potential target for therapeutic intervention. The recombinant expression of CA1 provides a valuable tool for studying its structure-function relationships and developing inhibitors that could serve as drugs. Advances in molecular cloning and protein expression systems have enabled researchers to produce large quantities of highly purified CA1 for kinetic studies, structural analysis, and drug screening. Understanding the enzymatic mechanisms and regulation of CA1 at the molecular level can contribute to the development of novel pharmacological agents and enhance our comprehension of its biological significance in health and disease. Additionally, the study of CA1 is not only vital for its implications in human health but also offers insights into the evolutionary aspects of carbonic anhydrases across different organisms, illuminating their diverse functions and adaptations. Overall, research on recombinant CA1 is essential for both basic science and the potential development of clinical applications aimed at modulating its activity for therapeutic benefits.
