Recombinant Human CA5A Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0495

Recombinant Human CA5A Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0495
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Product Overview

Tag His
Host Species Human
Accession NP_001730.1
Synonym CA5, CA5AD, CA5D, Carbonic Anhydrase VA, CAV, CAVA, GS1-21A4.1
Background Carbonic anhydrase 5A, mitochondrial, also known as Carbonate dehydratase VA, Carbonic anhydrase VA, CA-VA and CA5A, is a member of thealpha-carbonic anhydrase family. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA5A / CA-VA is activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. It is inhibited by coumarins, sulfonamide derivatives such as acetazolamide and Foscarnet (phosphonoformate trisodium salt).
Description A DNA sequence encoding the mature form of human CA5A (NP_001730.1) (Ala 40-Ser 305) was fused with an Met at N-terminus and a His tag at the C-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Ala 40-Ser 305
Molecular Weight The recombinant human CA5A consisting of 277 a.a. and has a calculated molecular mass of 31.6 kDa. It migrates as an approximately 33 kDa band in SDS-PAGE under reducing conditions.
Purity >96% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Measured by its esterase activity. The specific activity is >500 pmoles/min/ug.
Formulation Lyophilized from sterile 50mM NaAc, 50mM NaCl, 0.05% Brij 35, pH 5.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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