| Description | Human IgG3, Recombinant (IB3), Isotype Control, could be used for Flow Cytometry | Product DescriptionEndo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, Product DescriptionEndo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact.Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is therefore more suitable for deglycosylation of native proteins. However, for optimal results, denaturation of the glycoprotein is recommended.Contents60 µl aliquot of enzyme (0.3 U) in 10 mM sodium acetate 25mM NaCl, pH 4.5Included with 20 µL and 60 µL pack sizes:5x Reaction Buffer – 250 mM sodium acetate, pH 4.5Molecular weight 32,000 daltonsSpecific Activity Defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of denatured porcine fibrinogen in 1 minute at 37°C, pH 5.5. Cleavage is monitored by SDS-PAGE (cleaved fibrinogen migrates faster).Formulation The enzyme is provided as a sterile-filtered solution in 10 mM sodium acetate, 25mM NaCl, pH 4.5Specificity Endo F2 cleaves Asparagine-linked biantennary and high mannose glycans (at a 40X reduced rate). It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is therefore more suitable for deglycosylation of native proteins. However for optimal results, denaturation of the glycoprotein is recommended.Quality & Purity Endo F2 is tested for contaminating protease as follows: 10 µg of denatured BSA is incubated at 37°C for 24 hours with 2 µl of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation. The production host strain has been extensively tested and does not produce any detectable glycosidases.Stability Several days exposure to ambient temperatures will not reduce activity. Stable at least 12 months when stored properly.Directions for use 1. Add up to 200 µg of glycoprotein to an Eppendorf tube. Adjust to 38 µl final volume with de-ionized water. 2. Add 10 µl 5x Reaction Buffer 4.5 3. Add 2.0 µl of Endo F2 to the reaction. Incubate 1 hour at 37°C. Monitor cleavage by SDS-PAGEThe production host strain has been extensively tested and does not produce any detectable glycosidases... Read More | Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with anaerobic metabolism and pyruvate reduction.Catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+Recombinant rabbit muscle Lactate Dehydrogenase produced in E.Coli. Chromatographically purified. A lyophilized powder... Read More | Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity. Malic dehydrogenase is a cytoplasmic isozyme Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity. Malic dehydrogenase is a cytoplasmic isozyme and an important catalyst in the tricarboxylic acid cycle.ReagentsA. 0.1 M Tris-HCl buffer (pH7.8)B. 0.01 M Phosphate buffer (KH2PO4-NaOH, pH 7.0)C. Triton X-100 solution (50 mg/ml)D. 0.01 M Phosphate buffer containing 0.1% Triton X-100 (KH2PO4-NaOH, pH 7.0)Dilute 20 ml of Triton X-100 solution (C) with approx. 800 ml of 0.01M Phosphate buffer (B). Fill up to 1,000 ml with 0.01M Phosphate buffer (B).E. NADH soluton Weigh 9 mg of NADH and dissolve in 0.1M Tris-HCl bufer (A). Fill up to 50 ml with 0.1M Tris-HCl Buffer (A). (Can be used for 5 days if kept refrigerated)F. Substrate solutionWeigh 11 mg of oxaloacetic acid and dissolve in 0.1M Tris-HCl buffer (A). Fill up to 50 ml with 0.1M Tris-HCl buffer (A) (Make a fresh solution for each use.)G. Enzyme solutionWeigh out Malate Dehydrogenase and dissolve in chilled 0.01M Phosphate Bufer containing 0.1% Triton X-100 (D). Enzyme solution should be prepared so that the value of AOD/minute becomes in the range of 0.025 ± 0.010.ProcedurePipette 2.0 ml of NADH solution (E) and 0.90 ml of Substrate solution (F) respectively into a quartz cell (d=10 mm) and keep at 25 + 0.5'℃ for 5 minutes. Then, pipete 0.10 ml of Enzyme solution (G) into the quartz cell and mix well immediately. Keep the reaction mixture at 25 ±0.5'C.Exaclly at 2 minutes and 5 minutes after the addition of Enzyme solution (G), measure the absorbances of the reaction mixture at 340 nm(A2 and A5).As a blank, pipette 0.01M Phosphate buffer (D) into another quartz cel (d=10 mm) instead of the Enzyme solution (G) and follow the same procedure described above (Ab2 and Ab5).CalculationMalate dehydrogenase activity (u/mg)=[(A2-A5)-(Ab2-Ab5)]/3*(1/6.22)*(n/0.1) ApplicationThis enzyme is used for the enzymatic determination of L-malate and gluamate oxalo-acetate transaminase(GOT)in clinical diagnosis... Read More | Purity>98% SDS-PAGE. purified using conventional chromatography techniques.FunctionChemotactic activity for lymphocytes but not for monocytes or neutrophils.Chemokine (C motif) ligand (XCL1), as known as lymphotactin, is the only known member of the C-chemokine family and signals through the Purity>98% SDS-PAGE. purified using conventional chromatography techniques.FunctionChemotactic activity for lymphocytes but not for monocytes or neutrophils.Chemokine (C motif) ligand (XCL1), as known as lymphotactin, is the only known member of the C-chemokine family and signals through the receptor XCR1, formally known as GPR5. The expression of lymphotactin is abundant in some activated T cells such as activated CD8+ T cells and other class I MHC restricted T cells. It is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. XCL1 induces its chemotactic function by binding to a chemokine receptor called XCR1. Recombinant Human XCL1 which is a single non-glycosylated polypeptide chains containing 92 amino acids and it shares approximately 60 % amino acid sequence homology with the murine and rat protein... Read More |