金山科研平台，产品价格货期咨询微信：jinshanbio Source:Spodoptera frugiperda, Sf 21 (baculovirus)-derived, Met1-Thr529, with a C-terminal 6-His tag Accession #:P06865 N-terminal Sequence Analysis:Leu23 Purity:>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 µg per lane. Endotoxin Level: Predicted Molecular Mass:59 kDa SDS-PAGE:57-61 kDa, reducing conditions Activity:Measured by its ability to hydrolyze 4-methylumbelliferyl-N-acetyl-beta -D-glucosaminide (4-MU-GlcNAc)The specific activity is >1,250 pmol/min/µg, as measured under the described conditions. Formulation:Supplied as a 0.2 µm filtered solution in Tris and NaCl.See Certificate of Analysis for details. Molecule Information: Hexosaminidase A/HEXA Aliases: TSD Entrez Gene IDs: 3073 (Human) Background: HEXA beta-Hexosaminidases are enzymes involved in the hydrolysis of terminal N-acetyl-D-hexosamine residues in GM2 gangliosides and globo-sphingolipids in lysosomes. The enzymes are composed of two alpha and/or beta subunits, which are coded by HEXA and HEXB genes, respectively. Different associations of the alpha and beta subunits gives rise to beta-hexosaminidase isoforms A, B and S (Hex A, B and S), which have the composition of alpha/beta, beta/beta and alpha/alpha, respectively. Our recombinant HEXA is presumably isoform Hex S, because only alpha subunit was expressed. Hex S is suggested to release non-reducing end N-acetylgalactosamine residues from dermatan sulfate, chondroitin sulfate and sulfated glycolipid SM2. Recombinant HEXA is also highly active on 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide. Mutations in HEXA and HEXB genes cause lysosomal lipid storage disorders. Specifically, mutations of HEXA cause Tay-Sachs disease, manifested by the harmful accumulation of ganglioside GM2 in tissues and nerve cells in the brain. Children with this disease usually die by age 4.