Analytical Data
-
Gene name
Cystathionine gamma-lyase/CTH
- Application
-
Alternative Names
CSE; Cystathionase; Cysteine-protein sulfhydrase; Gamma-cystathionase
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P32929
-
Expression Region
Thr163~Asp382
-
Molecular Weight
26kDa
-
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
Cystathionine gamma-lyase (CTH) is an important enzyme involved in the transsulfuration pathway, playing a crucial role in cysteine and hydrogen sulfide (H2S) production from cystathionine. This pathway is essential for maintaining cellular redox balance and protecting against oxidative stress. Dysregulation of CTH expression and activity has been implicated in various pathological conditions, including cardiovascular diseases, neurodegenerative disorders, and cancers. Recent research highlights the therapeutic potential of modulating H2S production, given its signaling properties and cytoprotective effects. Consequently, the recombinant expression of CTH has emerged as a valuable strategy to study its biochemical properties, characterize its catalytic mechanisms, and explore its therapeutic applications. In particular, the generation of recombinant CTH allows for detailed kinetic studies, structure-function analyses, and the evaluation of its role in cellular and physiological processes. Moreover, understanding the structure of CTH can facilitate the design of small molecule inhibitors or activators that may have significant implications in treating diseases associated with H2S dysregulation. Overall, the investigation of CTH recombinant protein is integral to advancing our understanding of sulfur metabolism and its implications in health and disease.
