Modifying Enzymes
Cayman Chemical Oleoyl SerotonIn-d17 100UG
An internal standard for the quantification of oleoyl serotonin by GC- or LC-MS
Enzo Life Sciences MMP-8 (catalytic domain) (human), (recombinant) (10 µg)
Alternative name: Matrix metalloproteinase 8, Neutrophil collagenase, Collagenase 2. Purity: ≥90% (SDS-PAGE). Formulation: Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol. Source: Produced in E. coli. Active Matrix Metalloproteinase-8 (MMP-8, neutrophil collagenase, collagenase-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-8 (Phe99-Gln269, NM_002424) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-8 which lacks the C-terminal hemopexin domain1. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. Long Term Storage: -80°C.
ABclonal Technology T4 RNA Ligase 1
T4 RNA ligase 1 catalyzes the formation of a 3 to 5 phosphodiester bond by joining the 5 phosphate end of a nucleotide to the 3 hydroxyl end, accompanied by the hydrolysis of ATP to AMP and PPi. Substrates include single-stranded RNA, DNA, and dinucleoside pyrophosphates.
Sigma Aldrich Fine Chemicals Biosciences Neuraminidase (Sialidase) from Vibrio cholerae
Neuraminidase is an acylneuraminyl hydrolase which hydrolyzes terminal N- or O-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate: α2,6 > α2,3 > α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids. Noteworthy, for the hydrolysis of glycolipids, the presence of a detergent is necessary. Because of the broad substrate specificity, the enzyme is very well suited for the complete removal of sialic acids from glycoconjugates of a wide variety of biological materials.
ABclonal Technology Endonuclease III (Nth)
Endonuclease III (Nth) protein acts as both N-glycosylase and a AP-lyase.The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating a basic (AP site). The AP-lyase activity of the enzyme cleaves 3? to the AP site leaving a 5? phosphate and a 3? ring opened sugar.
Cayman Chemical N-Oleoyl ValIn 50mg
An endogenous N-acyl amine; antagonist at TRPV3; increases after acute lung injury in mouse lung tissue
New England Biolabs, Inc. Exonuclease V (RecBCD) – 1000 units
Exonuclease V, a RecBCD complex from E. coli has several different enzyme activities, including an ATP-dependent single-stranded DNA endonuclease activity, ss- and ds- DNA exonuclease activity. The hydrolysis in each case is bi-directional (from both the 3' and 5' ends) and processive, producing oligonucleotides. All Exonuclease V activities have divalent cation requirements. Mg2+ is required for the exonuclease activity, while Ca2+ inhibits the exonuclease activity and allows double-stranded DNA unwinding (helicase activity) without hydrolysis.
Apexbio Technology LLC Dyngo-4a 10mg. 1620401-82-2. MFCD28167817
Dyngo-4a 10mg. 1620401-82-2. MFCD28167817
Supelco Inc HYALURONIDASE TYPE 1V-S
Hyaluronidase, Type IV-S, lyophilized powder (essentially salt-free), 750-3000A units/mg solid
ABclonal Technology T4 RNA Ligase 2, truncated
T4 RNA Ligase 2, truncated (T4 Rnl2 truncated) specifically ligates the pre-adenylated 5 end of DNA or RNA to the 3 end of RNA. The enzyme does not require ATP for ligation but does need the pre-adenylated substrate. T4 Rnl2 truncated is expressed from a plasmid in E. coli which encodes the first 249 amino acids of the full length T4 RNA Ligase 2. Unlike the full length ligase, T4 Rnl2 truncated is unable to adenylate the 5 end of the substrate, and as a result it cannot ligate the phosphorylated 5? end of RNA or DNA to the 3? end of RNA. This enzyme, also known as Rnl2 (1-250) has been used for optimized linker ligation for the cloning of microRNAs. This enzyme reduces background ligation because it can only use adenylated primers.
Sigma Aldrich Fine Chemicals Biosciences Glucose-6-phosphate Dehydrogenase from baker's yeast (S. cerevisiae) Type XV, lyophilized powder, 200-400 units/mg protein (modified Warburg-Christian) | 9001-40-5 | MFCD00081656 | 2ku
Glucose-6-phosphate Dehydrogenase from baker's yeast (S. cerevisiae) Type XV, lyophilized powder, 200-400 units/mg protein (modified Warburg-Christian)Purity: | 9001-40-5 | MFCD00081656 | 2ku
Biotium CD45 / LCA (Leucocyte Marker)(Bra55), CF594 conjugate, 0.1mg/mL
CD45R, also designated CD45 and PTPRC, has been identified as a transmembrane glycoprotein, broadly expressed among hematopoietic cells. Multiple isoforms of CD45R are distributed throughout the immune system according to cell type. These isoforms arise because of alternative splicing of exons 4, 5, and 6. The corresponding protein domains are characterized by the binding of monoclonal antibodies specific for CD45RA (exon 4), CD45RB (exon 5), CD45RC (exon 6) and CD45RO (exons 4 to 6 spliced out). The variation in these isoforms is localized to the extracellular domain of CD45R, while the intracellular domain is conserved. CD45R functions as a phosphor-tyrosine phosphatase. Antibody to CD45 is useful in differential diagnosis of lymphoid tumors from non-hematopoietic undifferentiated neoplasms.
ABclonal Technology Acetyl-CoA Carboxylase
Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA the rate-limiting step in fatty acid synthesis There are two ACC forms alpha and beta encoded by two different genes ACC-alpha is highly enriched in lipogenic tissues The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA Multiple alternatively spliced transcript variants divergent in the 5 sequence and encoding distinct isoforms have been found for this gene
ABclonal Technology Topoisomerase II alpha/TOP2A
This gene encodes a DNA topoisomerase an enzyme that controls and alters the topologic states of DNA during transcription This nuclear enzyme is involved in processes such as chromosome condensation chromatid separation and the relief of torsional stress that occurs during DNA transcription and replication It catalyzes the transient breaking and rejoining of two strands of duplex DNA which allows the strands to pass through one another thus altering the topology of DNA Two forms of this enzyme exist as likely products of a gene duplication event The gene encoding this form alpha is localized to chromosome 17 and the beta gene is localized to chromosome 3 The gene encoding this enzyme functions as the target for several anticancer agents and a variety of mutations in this gene have been associated with the development of drug resistance Reduced activity of this enzyme may also play a role in ataxia-telangiectasia
ABclonal Technology Taq DNA Ligase
Taq DNA Ligase is a thermostable ligase that catalyzes the formation of a phosphodiester bond between the 5?-phosphate and the 3?-hydroxyl of two adjacent DNA strands. The target strands need to be hybridized and accurately paired, with no gap, to a complementary DNA strand; allowing resolution of single nucleotide variants. Taq DNA Ligase uses NAD as a cofactor and it is active at elevated temperatures (37°C-75°C). It is applicable to Allele-specific gene detection using Ligase Detection Reaction and Ligase Chain Reaction, as well as Mutagenesis by incorporation of a phosphorylated oligonucleotide during primer extension amplification.