Analytical Data
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Gene name
Carbonic Anhydrase 8
- Application
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Alternative Names
Carbonic Anhydrase-Related Protein; CARP; Carbonic Anhydrase VIII; CA-VIII; CA8; CALS
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Species
Human
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Source
E. coli
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Tag
C- His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P35219
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Expression Region
2-290aa
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Molecular Weight
34.04 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
Related Products
Protein Description
Carbonic Anhydrase 8 (CA8) is a member of the carbonic anhydrase enzyme family, which plays a crucial role in regulating pH and CO2 levels in biological systems. This enzyme is predominantly expressed in the brain and testis, where it is implicated in several physiological processes, including neurotransmission and ion transport. Recent studies have highlighted CA8's involvement in conditions such as neurological disorders and cancer, making it a target of interest for therapeutic interventions. However, the lack of detailed structural and functional information has hindered a comprehensive understanding of CA8's mechanisms of action. To address this knowledge gap, researchers have turned to recombinant protein technology to produce CA8 in a controlled laboratory setting. This approach allows for the generation of large quantities of the enzyme, enabling various biochemical and biophysical analyses. Recombinant CA8 can be utilized to investigate its catalytic properties, interaction with potential inhibitors, and role in cellular pathways. Additionally, characterizing the enzyme's structure through techniques such as crystallography or nuclear magnetic resonance can provide insights into its active site and substrate specificity. Ultimately, the study of recombinant CA8 holds promise for unveiling its biological functions and establishing its potential as a therapeutic target, which could lead to the development of novel treatments for diseases associated with its dysregulation.
