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Sino Biological Inc. liefert CTRL-1 / CTRL / Chymotrypsin-like protease Protein (His Tag) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.
Weitere Informationen über CTRL-1 / CTRL / Chymotrypsin-like protease Protein (His Tag) lesen Sie bitte:http://www.sinobiological.com/CTRL-1-chymotrypsin-like-protease-Protein-Antibody-a-6236.html
| Synonym | CTRL, CTRL1 |
| Protein Construction | A DNA sequence encoding the human CTRL (P40313) (Met1-Asn264) was expressed with a polyhistidine tag at the C-terminus. |
| Source | Human |
| Expression Host | Human Cells |
| Purity | (36.0+62.4)% as determined by SDS-PAGE | SDS-PAGE:![]() CTRL-1 protein |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method | |
| Stability | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal | Cys 19 | |
| Molecular Mass | The recombinant human CTRL consists of 257 amino acids and predicts a molecular mass of 27.6 KDa. It migrates as an approximately 35 and 32KDa band in SDS-PAGE under reducing conditions. | |
| Formulation | Lyophilized from sterile PBS, pH 7.4.
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| Storage | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
CTRL-1, also known as chymotrypsin-like protease, belongs to the peptidase S1 family. CTRL-1 contains 1 peptidase S1 domain. Its expression is increased in preeclampsia (PE). Placental-derived chymotrypsin-like protease is responsible for inducing endothelial inflammatory phenotypic changes possibly by upregulation of cell adhesion molecule expressions, activation of cellular protease, and induction of extracellular regulated kinase phosphorylation. Activated microglia have been observed in various neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, and multiple sclerosis. Five structurally distinct inhibitors that are known to inhibit chymotrypsin-like proteases were partially protective. They might represent a novel class of drugs with benefit in diseases where overactivity of microglia contributes to the pathogenesis.