RNASE1 Human
HEK293 Cells.
RNASE1, ribonuclease A family member 1, pancreatic, RAC1, RIB1, RNS1, ribonuclease pancreatic, HP-RNase, RIB-1, RNase UpI-1, RNase 1, Ribonuclease A, RNase A, Ribonuclease 1.
Greater than 90.0% as determined by SDS-PAGE.
Description
RNASE1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (29-156 a.a) containing a total of 134 amino acids, having a molecular mass of 15.3kDa.
RNASE1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Product Specs
Ribonuclease 1R (NASE1), a member of the pancreatic ribonuclease enzyme family, is a small protein. It possesses four disulfide bonds in its natural state and exhibits specific cleavage activity after pyrimidine nucleotides. The cleavage process unfolds in two steps: initially, the 3',5'-phosphodiester bond undergoes cleavage, yielding a 2',3'-cyclic phosphodiester intermediate; subsequently, this cyclic phosphodiester is hydrolyzed to generate a 3'-monophosphate. NASE1 exhibits heightened activation with single-stranded RNA. Its activity is inhibited by alkylation of His12 and His119 residues, while potassium and sodium salts enhance its activity. NASE1 is utilized to hydrolyze RNA present in protein samples.
Recombinant human RNASE1, produced in HEK cells, is a single, glycosylated polypeptide chain encompassing amino acids 29-156. With a total of 134 amino acids, it has a molecular weight of 15.3 kDa. A 6-amino acid His-tag is fused to the C-terminus of RNASE1, and it undergoes purification using proprietary chromatographic methods.
The RNASE1 solution is provided at a concentration of 1 mg/ml. It is formulated in a buffer containing 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
For short-term storage (2-4 weeks), the RNASE1 vial can be stored at 4°C. For extended storage, it is recommended to store the protein in frozen aliquots at -20°C. To further enhance long-term stability during freezing, the addition of a carrier protein (0.1% HSA or BSA) is advised. Repeated freeze-thaw cycles should be minimized.
The purity of RNASE1 is determined to be greater than 90.0% using SDS-PAGE analysis.
The specific activity of RNASE1 is determined to be greater than 3 x 10^6 units/mg. This value represents the quantity of enzyme required to hydrolyze 1 nanomole of RNA per minute at a temperature of 25°C.
RNASE1, ribonuclease A family member 1, pancreatic, RAC1, RIB1, RNS1, ribonuclease pancreatic, HP-RNase, RIB-1, RNase UpI-1, RNase 1, Ribonuclease A, RNase A, Ribonuclease 1.
HEK293 Cells.
KESRAKKFQR QHMDSDSSPS SSSTYCNQMM RRRNMTQGRC KPVNTFVHEP LVDVQNVCFQ EKVTCKNGQG NCYKSNSSMH ITDCRLTNGS RYPNCAYRTS PKERHIIVAC EGSPYVPVHF DASVEDSTHH HHHH
Product Science Overview
Ribonuclease 1 (RNase 1), also known as human pancreatic ribonuclease, is an extracellular enzyme that belongs to the ribonuclease A (RNase A) superfamily. This superfamily consists of eight members in humans, all of which are encoded on chromosome 14 . RNase 1 is a basic protein composed of 128 amino acid residues and is characterized by its high catalytic activity towards both single-stranded and double-stranded RNA .
RNase 1 is found in various organs, including the exocrine pancreas, blood, milk, saliva, urine, and seminal plasma . It plays a crucial role in the digestion of dietary RNA and has been implicated in antiviral host defense . The enzyme’s relevance to host defense is supported by reports of its antiviral activity against human immunodeficiency virus (HIV)-1 .
RNase 1 shares 70% sequence identity with the well-known bovine pancreatic RNase A . Despite this high degree of sequence identity, RNase 1 differentiates from the bovine enzyme by exhibiting a very high activity towards double-stranded RNA (dsRNA) . The enzyme cleaves RNA specifically on the 3′ side of pyrimidine bases . Under physiological-like conditions, RNase 1’s hybridase activity is maximal at neutral pH, increases with lowering ionic strength, and is fully inhibited by the cytosolic RNase inhibitor .
