| Description | FBH1 Human Pre-designed siRNA Set A contains three designed siRNAs for FBH1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components FBH1 siRNA-1: 5 nmol (HPLC) FBH1 siRNA-2: 5 nmol (HPLC) FBH1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 FBH1 Human Pre-designed siRNA Set A contains three designed siRNAs for FBH1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components FBH1 siRNA-1: 5 nmol (HPLC) FBH1 siRNA-2: 5 nmol (HPLC) FBH1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Inquire | 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 | Product IntroduceProteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic Product IntroduceProteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic amino acids. aladdin's proteinase K is characterized by high purity, sterility, no bio-burden, and no presence of DNAse, RNAse, DNA, and RNA contaminants. It is a good partner in DNA and RNA extraction for you.Features1、According to the SDS-PAGE image,the purity of Proteinase K is more than 95% and the molecular weight is 28.9 kDa.2、Detect DNase residue by agarose gel electrophores.3、Detect Nucleic acid residue by agarose gel electrophores.4、Detect RNase residue by agarose gel electrophores.5、Using the absorbance A275 as the vertical axis and different concentrations of tyrosine as the horizontal axis, a standard curve was drawn, and the enzyme activity was calculated>30U/mg... Read More | Purity>95% SDS-PAGE.FunctionThe soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds toPurity>95% SDS-PAGE.FunctionThe soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds to CX3CR1.Post-translationalA soluble short 95 kDa form may be released by proteolytic cleavage from the long membrane-anchored form. O-glycosylated with core 1 or possibly core 8 glycans... Read More |