| Description | Features Ultrapure qualityBinding specificity for N-acetyl-D-galactosamineSpecificity for blood group: A1 > A2 >> BLyophilized powderProduct descriptionGlycine max lectin is isolated from soy bean (Soy bean agglutinin, SBA) and purified by affinity chromatography. The molecular weight of Features Ultrapure qualityBinding specificity for N-acetyl-D-galactosamineSpecificity for blood group: A1 > A2 >> BLyophilized powderProduct descriptionGlycine max lectin is isolated from soy bean (Soy bean agglutinin, SBA) and purified by affinity chromatography. The molecular weight of the lectin is 120 kDa, it consists of four identical subunits of 30 kDa each and it displays carbohydrate binding specifity for N-acetyl-D-galactosamine and galactopyranosyl residues of glycoproteins (1).SBA has specificity for blood groups A1, A2 and B. The lectin interacts better with neuramidase-treated cells than with untreated cells. It has selective affinity for lymphocytes and human CD34+ hematopoietic stem cells. Immobilized conjugates of SBA are therefore important tools for removing T-cells in bone marrow transplantation.Medicago’s Glycine max lectin is supplied as a white to cream coloured lyophilized powder from a buffer containing 50 mM NH4HCO3, no preservatives are added. The material is made from a single production batch and is homogenous. It is not derived from any material of animal origin.ApplicationsStudies of SBA-binding normal and tumour cellsBlood group agglutinationGlycoprotein studiesCell agglutination studies Directions for useThe lectin may be reconstituted with 2 ml of deionized water before use. Spin the vial gently until full dissolution. Aggregation is thought to occur in the presence of high concentrations of 2-mercaptoethanol. The solution may be reconstituted in this buffer to desired working concentration. In absence of lactose the lectin will polymerize and storage at pH 8.6–8.8 causes precipitation.Shipping and storageThe product is shipped at -20°C however for over-the-day transport it may be shipped at ambient temperature. The lyophilized powder is stable for more than three years from production date when stored below -20°C. After reconstitution with deionized water, the solution may be stored frozen in working aliquots for up to 12 months... Read More | Inquire | Purified pectinase is a multi-component preparation highly effective in depolymerizing plant pectins with varying degrees of esterification. The product contains substantial hemicellulase, cellulase, pectinesterase and xylanase activities which together with pectin lyase and polygalacturonase work Purified pectinase is a multi-component preparation highly effective in depolymerizing plant pectins with varying degrees of esterification. The product contains substantial hemicellulase, cellulase, pectinesterase and xylanase activities which together with pectin lyase and polygalacturonase work synergistically to digest plant cell wall tissues. When used with Worthington purified cellulase, purified pectinase has been found to be highly successful for generating good yields of viable protoplasts in several plant systems, e.g., corn, soybean, red beet, sunflower, tomato and citrus. In general, a concentration range of 0.1% to 0.5% pectinase (with accompanying 0.5% to 1.5% cellulase) used at 24°C to 37°C for periods of 1 to 16 hours will yield good results... Read More | Inquire | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, morphogenesis, angiogenesis, wound healing, and tumorigenesis (1-4). KGF expression is restricted to cells of mesenchymal origin. When secreted, it acts as a paracrine growth factor for nearby epithelial cells (1). KGF speeds wound healing by being dramatically upregulated in response to damage to skin or internal structures that results in high local concentrations of inflammatory mediators such as IL-1 and TNF-alpha. (2, 5). KGF promotes cell migration and invasion, and mediates melanocyte transfer to keratinocytes upon UVB radiation (6, 7). It has been used ectopically to avoid chemotherapy-induced oral mucositis in patients with hematological malignancies (1). Deletion of KGF affects kidney development, producing abnormally small ureteric buds and fewer nephrons (8). It also impedes hair follicle differentiation (9). The 194 amino acid (aa) KGF precursor contains a 31 aa signal sequence and, like all other FGFs, an ~120 aa beta -trefoil scaffold that includes receptor- and heparin-binding sites. KGF signals only through the IIIb splice form of the tyrosine kinase receptor, FGF R2 (FGF R2-IIIb/KGF R) (10). Receptor dimerization requires an octameric or larger heparin or heparin sulfate proteoglycan (11). FGF-10, also called KGF2, shares 51% aa identity and similar function to KGF, but shows more limited expression than KGF and uses an additional receptor, FGF R2-IIIc (12). Following receptor engagement, KGF is typically degraded, while FGF-10 is recycled (12). Mature human KGF, which is active across species, shares 98% aa sequence identity with bovine, equine, ovine and canine, 96% with mouse and porcine, and 92% with rat KGF, respectively... Read More |