Name :
Recombinant Human Ribonuclease A Protein (His Tag), HPLC-verified
Biological Activity :
Background :
RNase A, also known as ribonuclease A and RNASE1, belongs to ribonuclease A superfamily. It is a pancreatic-type of secretory ribonuclease. RNase A is a basic protein and its many positive charges are consistent with its binding to RNA (a poly-anion). More generally, RNase A is unusually polar or, rather, unusually lacking in hydrophobic groups, especially aliphatic ones. As an endonuclease, RNase A cleaves internal phosphodiester RNA bonds on the 3′-side of pyrimidine bases. It prefers poly(C) as a substrate and hydrolyzes 2′,3′-cyclic nucleotides, with a pH optimum near 8.0. RNase A is monomeric and more commonly acts to degrade ds-RNA over ss-RNA. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified.
Biological Activity :
Measured by its ability to hydrolyze yeast RNA(Sigma,Catalog # R9001). One unit of the enzyme causes an increase in absorbance of 1.0 at 260 nm in 15 min when yeast RNA is hydrolyzed at 37°C and pH 7.0. The specific activity is >2.5×106 unit/mg.
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
P07998
NCBI Gene ID :
Synonyms :
Synonyms :
ribonuclease, RNase A family, 1 (pancreatic)
Amino Acid Sequence :
Molecular Weight :
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
Purity :
≥ 95 % as determined by SDS-PAGE. ≥ 95 % as determined by SEC-HPLC.
State of Matter :
Product Concentration :
Storage and Stability :
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.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the human RNASE1 (P07998) (Met1-Thr156) was expressed with a polyhistidine tag at the C-terminus.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
RAC1 Protein, Human; RIB1 Protein, Human; RNS1 Protein, Human Ribonuclease A 背景信息 RNase A, also known as ribonuclease A and RNASE1, belongs to ribonuclease A superfamily. It is a pancreatic-type of secretory ribonuclease. RNase A is a basic protein and its many positive charges are consistent with its binding to RNA (a poly-anion). More generally, RNase A is unusually polar or, rather, unusually lacking in hydrophobic groups, especially aliphatic ones. As an endonuclease, RNase A cleaves internal phosphodiester RNA bonds on the 3′-side of pyrimidine bases. It prefers poly(C) as a substrate and hydrolyzes 2′,3′-cyclic nucleotides, with a pH optimum near 8.0. RNase A is monomeric and more commonly acts to degrade ds-RNA over ss-RNA. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified.
References & Citations :
Tubert P, et al. (2011) Interactions crucial for three-dimensional domain swapping in the HP-RNase variant PM8. Biophys J. 101(2):459-67.Vinayagam A, et al. (2011) A directed protein interaction network for investigating intracellular signal transduction. Sci Signal. 4(189):rs8.Fischer S, et al. (2011) Expression and localisation of vascular ribonucleases in endothelial cells. Thromb Haemost. 105(2):345-55.
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