| Description | Glycine 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 Glycine 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. 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. 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. ● Ultrapure quality ● Binding specificity for N-acetyl-D-galactosamine ● Specificity for blood group: A1 > A2 >> B ● Lyophilized powder Studies of SBA-binding normal and tumour cells;Blood group agglutination;Glycoprotein studies;Cell agglutination studies... Read More | Store at +4°C. Store under desiccating conditions. The product can be stored for up to 12 months | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 4.19 | Purity＞97% by SDS-PAGE and HPLC analyses.FunctionPigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a Purity＞97% by SDS-PAGE and HPLC analyses.FunctionPigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418 a.a. about 50kDa precursor that contains a 19 a.a. signal sequence and a 399 a.a. mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity. PEDF has functions of inducing extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. PEDF is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer... Read More | Purity>97% by SDS-PAGE and HPLC analyses.FunctionPlays an important role in the organization of the cytoskeleton (By similarity). Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization. Seraspenide inhibits the entry of hematopoeitic pluripotent stem cells Purity>97% by SDS-PAGE and HPLC analyses.FunctionPlays an important role in the organization of the cytoskeleton (By similarity). Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization. Seraspenide inhibits the entry of hematopoeitic pluripotent stem cells into the S-phase... Read More |