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Sino Biological Inc. liefert RNase A / Ribonuclease A / RNASE1 Protein (His Tag) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.
Weitere Informationen über RNase A / Ribonuclease A / RNASE1 Protein (His Tag) lesen Sie bitte: http://www.sinobiological.com/RNase A-Ribonuclease A-RNASE1-Protein-g-10171.html
| Synonym | RNASE1, RIB1, RNS1 |
| Protein Construction | A DNA sequence encoding the human RNASE1 (P07998)(Met1-Thr156) was expressed with a polyhistidine tag at the C-terminus. |
| Source | Human |
| Expression Host | Human Cells |
| Purity | > (81.9+12.3+4.7) % as determined by SDS-PAGE | SDS-PAGE:![]() RNase A 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 | Lys 29 | |
| Molecular Mass | The recombinant human RNASE1 comprises 139 amino acids and has a predicted molecular mass of 16 kDa. The apparent molecular mass of the protein is approximately 29 ,26 and 22 kDa in SDS-PAGE under reducing conditions | |
| Formulation | Lyophilized from sterile PBS, pH7.4.
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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. |
RNase A, also known as ribonuclease A and RNASE1, is a member of the ribonuclease A superfamily. RNase A cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. This Cleavage takes place in two steps: first, the 3’,5’-phosphodiester bond is cleaved to generate a 2’,3’-cyclic phosphodiester intermediate; second, the cyclic phosphodiester is hydrolyzed to a 3’-monophosphate. RNase A has four disulfide bonds in its native state: Cys26-Cys84, Cys58-110, Cys40-95 and Cys65-72. The first two are essential for conformational folding. The latter two disulfide bonds are less essential for folding; either one can be reduced (but not both) without affecting the native structure under physiological conditions.