Analytical Data
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Gene name
A35R
- Application
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Species
Virus
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Source
HEK293
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Tag
C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
QJQ40286
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Expression Region
R58-T181
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Protein Length
Partial
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Molecular Weight
15-20 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 XII (CA12) is a member of the carbonic anhydrase enzyme family, which plays a crucial role in maintaining acid-base balance in biological systems by catalyzing the reversible hydration of carbon dioxide to bicarbonate and protons. The study of CA12 has garnered significant attention due to its unique expression profile, predominantly found in certain tissues such as the kidney and brain, as well as its upregulation in various cancer types. This elevation in expression is associated with tumor progression and metastasis, making CA12 an attractive target for cancer therapeutics and diagnostics. Moreover, its role in pH regulation in the tumor microenvironment suggests that inhibiting CA12 could enhance the efficacy of conventional cancer treatments. The recombinant production of CA12 protein is essential for studying its enzymatic properties, structural biology, and potential inhibitors. Understanding the function and regulation of CA12 through recombinant techniques provides insights into its mechanism in oncogenic processes and opens avenues for developing novel therapeutic strategies aimed at modulating its activity. This research holds promise not only for cancer treatment but also for understanding fundamental biological processes related to acid-base homeostasis and cellular signaling.
