Analytical Data
-
Gene name
CSH2
- Application
-
Alternative Names
Choriomammotropin;Lactogen;Placental lactogen;PL
-
Species
Human
-
Source
E. coli
-
Tag
N- His-GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0DML3
-
Expression Region
27-217aa
-
Molecular Weight
53.8 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
CSH2, or carbohydrate sulfotransferase 2, is an enzyme that plays a critical role in the biosynthesis of sulfated carbohydrates, particularly glycosaminoglycans, which are essential components of the extracellular matrix and involved in numerous biological processes, including cell signaling, adhesion, and tissue repair. The study of CSH2 recombinant proteins has gained significant interest due to their potential implications in understanding various pathological conditions, including cancer, inflammation, and genetic disorders. Recent advancements in molecular biology techniques have facilitated the expression and purification of CSH2 in heterologous systems, allowing researchers to investigate its structure-function relationships, enzymatic mechanisms, and interactions with other biomolecules. Furthermore, elucidating the function of CSH2 may contribute to the development of therapeutic strategies aimed at modulating sulfation patterns, thereby influencing cellular behavior and disease progression. As the demand for biopharmaceuticals increases, the optimization of CSH2 recombinant protein production becomes vital, highlighting the importance of ongoing research in this area to unlock the full potential of this enzyme in both basic research and clinical applications.
