RNase A / Ribonuclease A / RNASE1 Protein (His Tag)

Ribonuclease, RNase A family, 1 (pancreatic) Protein Datasheet

RNase A / Ribonuclease A / RNASE1 Protein Product Information

• 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

RNase A / Ribonuclease A / RNASE1 Protein QC Testing

• Purity: (81.9+12.3+4.7) % as determined by SDS-PAGE
• 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.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: RNase A / Ribonuclease A / RNASE1 protein

RNase A / Ribonuclease A / RNASE1 Protein Usage Guide

• 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 / Ribonuclease A / RNASE1 Protein Description

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.

References

1. Tubert P. et al., 2011, Biophys J. 101 (2): 459-67.
2. Vinayagam A. et al., 2011, Sci Signal. 4 (189): 8.
3. Fischer S. et al., 2011, Thromb Haemost. 105 (2): 345-55.