Analytical Data
-
Gene name
CBS
- Application
-
Alternative Names
Beta-thionase;Serine sulfhydrase
-
Species
Human
-
Source
Yeast
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P35520
-
Expression Region
1-413aa
-
Molecular Weight
47.4 kDa
-
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
CBS (Cystathionine β-synthase) is an enzyme that plays a crucial role in the transsulfuration pathway, where it catalyzes the condensation of homocysteine and serine to form cystathionine, a precursor of cysteine. Mutations in the CBS gene are linked to homocystinuria, a metabolic disorder characterized by elevated levels of homocysteine, which can lead to serious health issues such as cardiovascular diseases, thrombosis, and developmental delays. Understanding the structure and function of CBS is vital for elucidating its role in cellular metabolism and disease. Recent studies have focused on the recombinant expression of CBS, allowing for the production of large quantities of the enzyme for biochemical and structural analysis. By using techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, researchers aim to uncover the enzyme's active site dynamics, substrate specificity, and the mechanisms by which mutations affect its function. These insights are essential for the development of targeted therapies for homocystinuria and related disorders, as well as for understanding the broader implications of sulfur amino acid metabolism in human health. Additionally, recombinant CBS is being explored for potential applications in biotechnology, where its enzymatic activities could be harnessed for the production of cysteine and other sulfur-containing compounds.
