| Quantity | 5mg, 1mg, 25mg | 100mg, 5mg, 2mg, 1mg, 25mg | 500µg, 1mg | 100g, 500mg, 25g, 25mg, 100mg, 1g, 5g | 100µg, 10µg, 50µg, 1mg |
| Description | Pancreatic lipase,when prepared essentially free of colipase,is strongly inhibited by conjugated bile salts at or above their critical micelleconcentration. The addition of colipase restores activity to the bile-salt-inhibited lipase,and gel filtration experiments indicate that colipase in bile saltPancreatic lipase,when prepared essentially free of colipase,is strongly inhibited by conjugated bile salts at or above their critical micelleconcentration. The addition of colipase restores activity to the bile-salt-inhibited lipase,and gel filtration experiments indicate that colipase in bile salt solution formsa dimer,which createsa 1:1 complex with lipase.PROPERTIESLipase and colipase interact in a stoichiometric relationship, with colipase classified as a co-enzyme for lipase. Colipase is a single-chain polypeptide with a molecular weight of approximately 11,000, containing fivedisulfide bridges and an isoelectric point of 5.0.APPLICATIONUse colipase as a co-emulsifier in diagnostic tests for the determination of lipase activity in combination with a chromogenic lipase substrate.ATTENTIONFor your safety and health, please wear a lab coat and disposable gloves... Read More | Amyloid β-Protein Fragment 25-35 (Aβ25-35) is derived from the amyloid-β protein.amyloid-β protein, which is mapped to human chromosome 21q21.Aβ25-35 lacks the N-terminal domain and the metal binding site and is majorly generated by proteolytic cleavage of Aβ(1−40Amyloid β-Protein Fragment 25-35 (Aβ25-35) is derived from the amyloid-β protein.amyloid-β protein, which is mapped to human chromosome 21q21.Aβ25-35 lacks the N-terminal domain and the metal binding site and is majorly generated by proteolytic cleavage of Aβ(1−40) peptides. It has a β-sheet and β-turn structure. Amino Acid Sequence Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-MetFunctional domain of Aβ required for both neurotrophic and neurotoxic effects... Read More | Inquire | 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.Additional sequence informationFull length mature chain without signal peptide.FunctionLineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be Purity>95% SDS-PAGE.Additional sequence informationFull length mature chain without signal peptide.FunctionLineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets... Read More |