Analytical Data
-
Gene name
CA5B
- Application
-
Alternative Names
CA-VB; CAVB; Carbonate dehydratase VB
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y2D0
-
Expression Region
Cys34~Pro317
-
Molecular Weight
36kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
CA5B (Carbonic Anhydrase 5B) is a member of the carbonic anhydrase enzyme family, which plays a crucial role in various physiological processes, including acid-base balance, respiration, and fluid secretion. Research on CA5B has garnered attention due to its involvement in metabolic disorders and its potential implications in cancer biology. Unlike other carbonic anhydrases, CA5B is primarily expressed in specific tissues, such as the kidney and brain, suggesting a specialized function that warrants investigation. Moreover, aberrant expression of CA5B has been observed in certain pathological states, raising questions about its role in disease mechanisms. The recombinant production of CA5B protein allows for detailed biochemical and structural studies, enabling researchers to elucidate its enzymatic properties and interactions with other biomolecules. Understanding the structure-function relationship of CA5B may pave the way for novel therapeutic strategies targeting related diseases. Additionally, the exploration of CA5B's regulatory mechanisms could provide insights into metabolic adaptation and cellular homeostasis, further emphasizing its significance in both health and disease. Thus, the study of CA5B recombinant protein is not just a pursuit of basic science; it holds potential for translational applications in medicine and biotechnology.
