Modifying Enzymes
Carnabio Usa Inc ZAP70/10UG/FULL-LENGTH
ZAP70, Full-length, Wild type, Amino Acid 1-619, NP_001070.2, Expressed in Insect (sf21); 10microg
Carnabio Usa Inc TAOK2/10UG/CATALYTIC
TAOK2, Catalytic domain, Wild type, Amino Acid 1-319, NP_004774.1, Expressed in Insect (sf21); 10microg
Carnabio Usa Inc BTN - MET / 10UG
BTN-MET, Cytoplasmic domain, Wild type, Amino Acid 956-1390(end), NP_000236.2, Expressed in Insect (sf21); 10microg
Cayman Chemical MaLNyl Coenzyme AlIthIM5mg
A CoA derivative used in fatty acid and polyketide synthesis and in the transport of α-ketoglutarate across the mitochondrial membrane; may mediate cancer cell cytotoxicity induced by fatty acid synthase inhibition
MINNEBIO LLC Ultra-Active Nuclease (Serratia marcescens Nuclease, EC 3.1.30.2) Benzonase Alternative Purity 98%10 kU.
Ultra-Active Nuclease is extensively utilized across biopharmaceutical and academic research settings for its ability to streamline nucleic acid removal and improve sample processing. Beyond standard cell lysate applications, it enhances protein purification workflows by reducing nucleic acid contamination, facilitates viral vector and vaccine production by maintaining low-viscosity solutions, and supports antibody development by ensuring cleaner preparations for downstream analyses. Its broad compatibility allows use under diverse conditions, including high-salt buffers, detergents, or partially denatured samples, making it highly versatile for complex biological systems. Widely trusted by leading pharmaceutical companies, top research institutes, and university laboratories worldwide, this enzyme delivers reproducible results, contributes to higher assay accuracy, and reduces processing time in critical experimental and manufacturing workflows.
Rockland Immunochemicals Protease S. aureus 1 mg
Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 000 daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F- Cl- CH3COO- and NO3. Enzyme activity is determined by the casein digestion assay. Protease S. aureus is ideal for investigators involved in enzyme and infectious diease research.
LifeSensors SUMO Protease 1 250 Units
LifeSensors' industry leading SUMO Protease 1 (Ulp1), a highly active and robust recombinant protease, cleaves SUMO from recombinant fusion proteins. Unlike thrombin, EK, or TEV protease, which recognize short linear sequences, SUMO Protease 1 recognizes the tertiary structure of SUMO. As a result, SUMO Protease 1 will not cleave within the fused protein of interest. 1 unit will cleave >90 µg of hSUMO3-GFP in 1 hr at 37C.
LifeSensors SUMO Protease 1 500 Units
LifeSensors' industry leading SUMO Protease 1 (Ulp1), a highly active and robust recombinant protease, cleaves SUMO from recombinant fusion proteins. Unlike thrombin, EK, or TEV protease, which recognize short linear sequences, SUMO Protease 1 recognizes the tertiary structure of SUMO. As a result, SUMO Protease 1 will not cleave within the fused protein of interest. 1 unit will cleave >90 µg of hSUMO3-GFP in 1 hr at 37C.
INTACT GENOMICS INC T4 DNA Ligase 400,000 Units (2000 units/µl)
Intact Genomics T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5’-phosphate and 3’-hydroxyl termini in duplex DNA or RNA. This enzyme joins DNA fragments with either cohesive or blunt termini and repairs single stranded nicks in duplex DNA, RNA or DNA/RNA hybrids (1).Applications• Cloning of restriction enzyme generated DNA fragments• Cloning of PCR products• Next-gen library preparation• Joining linkers and adapters to cohesive or blunt-ended DNA• Nick repair in duplex DNA, RNA or DNA/RNA hybrids• Self-circularization of linear DNA
New England Biolabs, Inc. Exonuclease III (E.coli) – 25000 units
Catalyzes the stepwise removal of mononucleotides from 3'-hydroxyl termini of duplex DNA. A limited number of nucleotides are removed during each binding event, resulting in coordinated progressive deletions within the population of DNA molecules. The preferred substrates are blunt or recessed 3'-termini, although the enzyme also acts at nicks in duplex DNA to produce single-strand gaps. 3'-protruding termini are resistant to cleavage; the degree of resistance depends on the length of the extension,with extensions 4 bases or longer being essentially resistant to cleavage. Exonuclease III activity depends partially on helical structure and displays sequence dependence (C>A=T>G). Temperature, salt concentration and the ratio of enzyme to DNA greatly affect enzyme activity, requiring reaction conditions to be tailored to specific applications. Exonuclease III has also been reported to have RNase H, 3'-phosphatase and AP-endonuclease activities.
New England Biolabs, Inc. RtcB Ligase – 25 reactions
RtcB Ligase from E. coli joins single stranded RNA with a 3' -phosphate or 2' ,3' -cyclic phosphate to another RNA with a 5' -hydroxyl. Ligation requires both GTP and MnCl2 and proceeds through a 3' -guanylate intermediate . For substrates with a 2' ,3' -cyclic phosphate end, hydrolysis to a 3' -phosphate precedes 3' end activation with GMP and ligation.
Sigma Aldrich Fine Chemicals Biosciences ISOBUTYRYL COENZYME A LITHIUM
NC3840085 ISOBUTYRYL COENZYME A LITHIUM
Sigma Aldrich Fine Chemicals Biosciences Peroxidase, Nitrospira sp., recombinant >=10.0 U/g | 9003-99-0 | 10MG
Peroxidase, Nitrospira sp., recombinant >=10.0 U/g | 9003-99-0 | 10MG