Easy access to products and protocols for research use only in the identification of 2019-nCoV based on Centers for Disease Control and Prevention (CDC) recommendations
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Enzymes accelerate, or catalyze, chemical reactions, and they are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Choose specific enzymes for cleaving bonds, removing genomic DNA from RNA preparations, for producing fragments of proteins, or for use in ion exchange chromatography. Enzymes are used in the chemical industry and other industrial applications when extremely specific catalysts are required.
Description:
cAMP-Dependent Protein Kinase phosphorylates a wide range of target proteins in response to changes in intracellular cAMP levels (1). The holoenzyme consists of four subunits: two regulatory and two catalytic (C) subunits.
Description:
Proteinase K (PK) Solution, produced by the fungus Tritirachium album Limber, is a serine protease that exhibits broad cleavage activity, stability: urea and SDS, Application: pulsed-field gel electrophoresis, protein fingerprinting, Concentration: 20mg/ml, Size: 16ml
Description:
Nb.BssSI - 1,000 units Nicking Endonucleases can generate nicked or gapped duplex DNA for studies of DNA mismatch repair and for diagnostic applications. The long overhangs that nicking enzymes make can be used in DNA fragment assembly.
Description:
Modifying enzyme. Labeling in vitro, sequencing, mapping, mutagenesis, duplex shortening. 150-200 units/uL. Size: 5000 units. In a tamper-evident, clear plastic sealed packet with enzyme tube, its buffer(s) and a lot-specific Promega* Product Information insert. 24-month lifetime.
Description:
PNGase A, Concentration: 5,000 units/ml, Source: Cloned from Oryza sativa (rice) and expressed in Pichia pastoris, recombinant amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and short complex oligosaccharides, Size: 750units
Description:
Endoglycoceramidase I (EGCase I), Concentration: 6 units/ml, Catalyzes the hydrolysis of the B-glycosidic linkage between oligosaccharides and ceramides in various glycosphingolipids, Oligosaccharide and ceramide remain intact, Size: 150 milliunits
Description:
Kynurenine Aminotransferase II Recombinant Protein, Species: human, Source: E. Coli, Sequence: full-length KAT II is fused at the N-terminus, Fusion tag: His Tag, Purity: >97% (SDS-PAGE), Physical state: Liquid, Synonyms: hKAT II, Size: 50ug
Description:
NAD Nucleotidase H. Influenzae Recombinant Protein, Source: E. Coli, Sequence: Full-length NAD 5’-nucleotidase without the signal peptide corresponding to the first 26 aa, Fusion tag: Tag Free, Purity: >98% (SDS-PAGE), Size: 50ug
Description:
a-Lytic Protease, Cleaves after Threonine (T), Alanine (A), Serine (S) and Valine (V) residues. Its specificity makes it an orthogonal and alternative protease to others commonly used in proteomics applications, Conc: 0.4 mg/ml, Size: 20ug
Description:
Trypsin. Modified Mass Spec-Bovine, Highly Purified Mass Spectroscopy grade Trypsin. A serine endopeptidase, cleaves the carboxy side of arginine, lysine and s-aminoethyl cysteine, suitable for mass spectrometry and sequence analysis. 20ug/vial. Pack of 5 vials.
Description:
Histo/Zyme (Ready to Use) stabilized enzyme in buffered solution, designed to unmask immunoreactive sites altered by fixation and/or the embedding process. It requires only a brief incubation at room temperature. Primary antibody may have to be diluted 5 to 10 fold to achieve optimal staining.
Description:
Highly Purified Mass Spectroscopy grade Glutamic-C. A serine endopeptidase, cleaves at the carboxy side of either aspartic or glutamic acid, suitable for mass spectrometry and sequence analysis. 2 vials, 10ug/vial.
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