Neuraminidase Agarose from Clostridium perfringens (C. welchii)

• Description:

  Neuraminidase Agarose from Clostridium perfringens (C. welchii)_x000D_ Catalog number: B2018834_x000D_ Lot number: Batch Dependent_x000D_ Expiration Date: Batch dependent_x000D_ Amount: 1 Unit_x000D_ Molecular Weight or Concentration: N/A_x000D_ Supplied as: Suspension_x000D_ Applications: a molecular tool for various biochemical applications_x000D_ Storage: 2-8°C_x000D_ Keywords: Acylneuraminyl hydrolase, Receptor-destroying enzyme, Sialidase_x000D_ Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ References:_x000D_ 1: Bidondo L, Landeira M, Festari F, Freire T, Giacomini C. A biotechnological tool for glycoprotein desialylation based on immobilized neuraminidase from Clostridium perfringens Biochem Biophys Rep. 2021 Mar 2;26:100940._x000D_ 2: Chien CH, Wei YH, Yeh SF, Li CP. An immobilized-enzyme system for the determination of sialic acid using cloned neuraminidase from Clostridium perfringens A.T.C.C. 10543 Biotechnol Appl Biochem. 1994 Feb;19(1):51-60._x000D_ 3: Kruse S, Kleineidam RG, Roggentin P, Schauer R. Expression and purification of a recombinant "small" sialidase from Clostridium perfringens A99 Protein Expr Purif. 1996 Jun;7(4):415-22._x000D_ 4: Parker TL, Corfield AP, Veh RW, Schauer R. Immobilized Clostridium perfringens neuraminidase. Substrate cleavage and enzyme release during incubation Hoppe Seylers Z Physiol Chem. 1977 Jul;358(7):789-95._x000D_ 5: Attie AD, Weinstein DB, Freeze HH, Pittman RC, Steinberg D. Unaltered catabolism of desialylated low-density lipoprotein in the pig and in cultured rat hepatocytes Biochem J. 1979 Jun 15;180(3):647-54._x000D_ 6: Kato H, Nakanishi T, Arai H, Nishida HI, Nishida T. Purification, microheterogeneity, and stability of human lipid transfer protein J Biol Chem. 1989 Mar 5;264(7):4082-7._x000D_ 7: LaMont JT, Ventola AS. Purification and composition of colonic epithelial mucin Biochim Biophys Acta. 1980 Nov 20;626(1):234-43._x000D_ 8: Furthmayr H, Marchesi VT. Subunit structure of human erythrocyte glycophorin A Biochemistry. 1976 Mar 9;15(5):1137-44._x000D_ 9: Geisow MJ. An improved method for purifying sialidase Biochem J. 1975 Oct;151(1):181-3._x000D_ 10: Kumarasamy R, Blough HA. Galactose-rich glycoproteins are on the cell surface of herpes virus-infected cells. 1. Surface labeling and serial lectin binding studies of Asn-linked oligosaccharides of glycoprotein gC Arch Biochem Biophys. 1985 Feb 1;236(2):593-602. _x000D_ _x000D_ Products Related to Neuraminidase Agarose from Clostridium perfringens (C. welchii) can be found at Proteins

• Short Description:

  Catalog Number: B2018834 (1 Unit)_x000D_ Neuraminidase Agarose is derived from Clostridium perfringens. It cleaves sialic acid residues from glycoproteins and glycolipids, playing a role in biological processes like cell signaling. This agarose form is valuable for studying sialic acid interactions and bacterial mechanisms. This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request._x000D_ _x000D_

• Weight:

  0.15

• Length:

  2

• Width:

  0.5

• Height :

  0.5