Nuclease

DNase I (EC 3.1.21.1) is an enzyme that degrade DNA, it plays a key role in the cleavage of extracellular DNA is crucial for limiting the inflammatory response and maintaining homeostasis. Exogenous deoxyribonuclease shows beneficial effects in inflammatory diseases and cancer.

RNase A (Bovine pancreatic RNase) is a widely used Endonuclease in DNA purification by specifically hydrolyzing cytosine or uracil residues of RNA. RNase A degrades the RNA in the RNA/DNA duplex. RNase A catalyses the breakdown of 3',5'-phosphodiester linkages of single stranded RNA. RNase A family members in organisms are tightly involved in various physiological and pathological processes including cell growth and development, proliferation, differentiation and migration. Dysregulation of RNase A activity or expression level is closely related to pancreatic, ovarian, bladder and thyroid cancer. RNase A has tumor cell-killing ability.

Recombinant DNase I (RNase-free) is a recombinant deoxyribonuclease that degrades DNA. Recombinant DNase I is essential for limiting inflammatory responses and maintaining homeostasis.

RNase A (10mg/mL, DNase free) is a ribonuclease used to catalyze RNA degradation without containing DNase. RNase A is often employed in cell cycle assay.

Serratia marcescens nuclease (EC 3.1.30.2) is a nonspecific nuclease. Serratia marcescens nuclease has broad utility due to its potent digestive activity toward both DNA and RNA.

RNase A (Bovine pancreatic RNase) is a widely used Endonuclease in DNA purification by specifically hydrolyzing cytosine or uracil residues of RNA. RNase A degrades the RNA in the RNA/DNA duplex. RNase A catalyses the breakdown of 3',5'-phosphodiester linkages of single stranded RNA. RNase A family members in organisms are tightly involved in various physiological and pathological processes including cell growth and development, proliferation, differentiation and migration. Dysregulation of RNase A activity or expression level is closely related to pancreatic, ovarian, bladder and thyroid cancer. RNase A has tumor cell-killing ability. RNase B, Bovine Pancreas (Ribonuclease B, Bovine Pancreas) is the N-glycosylated form of RNase A. RNase B, Bovine Pancreas can promote the folding of polypeptide chains and play a role similar to molecular chaperones.

Deoxyribonuclease II (DNase II) is an endonuclease that hydrolyzes the phosphodiester bonds of deoxyribonucleotides in native and denatured DNA, producing 3' phosphate and 5'-hydroxyl termini. Deoxyribonuclease II works best at acidic pH and is commonly used in biochemical research.

Micrococcal nuclease is an endonuclease derived from Staphylococcus aureus. Micrococcal nuclease is able to digest both single and double-stranded DNA (ssDNA and dsDNA) and RNA, and can cleave and hydrolyze the AT or AU-rich regions specifically. Micrococcal nuclease could be used as an indicator of Staphylococcus aureus contamination.

Nuclease P1 is a single-stranded specific endonuclease, it hydrolyzes nucleic acids into 5'-mononucleotides and cleaves the single-stranded region of a double-stranded nucleic acid. Nuclease P1 is one of the most well-known single stranded specific nucleases in the field of molecular biology, it is widely used in the pharmaceutical and food industries. Nuclease P1 can be obtained by fermentation of Penicillium citrinum: through extraction process, ultrafiltration concentration, drying and purification, etc.

Nuclease S1, Aspergillus oryzae is a specific endonuclease that degrades single stranded DNA (ssDNA) and RNA. Nuclease S1 can also remove protruding single-strand ends from double-stranded DNA.

Ribonulease T1, Aspergillus oryzae (Rnase T1), is commonly used in biochemical research. Ribonuclease T1 is an endonuclease that can specifically degrade single stranded RNA. Ribonuclease T1 can form nucleoside 2 ', 3 '-cyclic phosphoric acid intermediates to cut the phosphodiester bond between 3' -guanosine residues and adjacent nucleoside 5 '-OH groups to produce 3' -GMP terminal oligonucleotides.

RNase A (Bovine pancreatic RNase) is a widely used Endonuclease in DNA purification by specifically hydrolyzing cytosine or uracil residues of RNA. RNase A degrades the RNA in the RNA/DNA duplex. RNase A catalyses the breakdown of 3',5'-phosphodiester linkages of single stranded RNA. RNase A family members in organisms are tightly involved in various physiological and pathological processes including cell growth and development, proliferation, differentiation and migration. Dysregulation of RNase A activity or expression level is closely related to pancreatic, ovarian, bladder and thyroid cancer. RNase A has tumor cell-killing ability. RNase A, Recombinant (animal free) is recombinant RNase A with no animal-derived components.

DNase I is an enzyme that degrades DNA. DNase I is mainly produced by digestive system organs, such as the pancreas and parotid gland. Three types of DNase I are known in mammals: pancreatic type, parotid type, and pancreatico-parotid type. DNase I plays a key role in the cleavage of extracellular DNA, and is critical for limiting inflammatory responses and maintaining homeostasis. DNase I is responsible for digesting extracellular nucleoproteins, which may be essential for preventing autoimmune reactions. Decreased DNase I activity may be associated with the occurrence and development of systemic lupus erythematosus (SLE). DNase I (filtered) is filtered through a 0.22 μM membrane and is not tested for pyrogenicity.

RNase H2 is the predominant source of RNase H activity in mammalian and human cells. RNase H2 protects genome integrity. RNase H2 has been associated with ribonucleotide removal from genomic DNA in yeast and mouse, where it is required for embryonic development.

RNase A (Bovine pancreatic RNase) is a widely used Endonuclease in DNA purification by specifically hydrolyzing cytosine or uracil residues of RNA. RNase A degrades the RNA in the RNA/DNA duplex. RNase A catalyses the breakdown of 3',5'-phosphodiester linkages of single stranded RNA. RNase A family members in organisms are tightly involved in various physiological and pathological processes including cell growth and development, proliferation, differentiation and migration. Dysregulation of RNase A activity or expression level is closely related to pancreatic, ovarian, bladder and thyroid cancer. RNase A has tumor cell-killing ability. RNase A, Recombinant (Ribonuclease A, Recombinant) is a recombinant form of RNase A.

DNase I is an enzyme that degrades DNA. DNase I is mainly produced by digestive system organs, such as the pancreas and parotid gland. Three types of DNase I are known in mammals: pancreatic type, parotid type, and pancreatico-parotid type. DNase I plays a key role in the cleavage of extracellular DNA, and is critical for limiting inflammatory responses and maintaining homeostasis. DNase I is responsible for digesting extracellular nucleoproteins, which may be essential for preventing autoimmune responses. Decreased DNase I activity may be associated with the onset and progression of systemic lupus erythematosus (SLE). DNase I (RNase & Protease free) is a molecular biology-grade DNase I purified by chromatography to remove RNase and protease.

NADase is an ectoenzyme/membrane-bound enzyme targeting nicotinamide adenine dinucleotide (NAD⁺). NADase regulates intracellular NAD⁺ homeostasis by hydrolyzing NAD⁺ into nicotinamide mononucleotide (NMN) and ADP-ribose. NADase is promising for research of autoimmune diseases (e.g., systemic sclerosis, systemic lupus erythematosus) and aging-related disorders.