| Description | Wheat germ lectin (WGA) from Triticum vulgaris exists as a homodimer and has multiple N-acetyl glucosamine (GlcNAc) binding sites. It is resistant to protein denaturation agents and is used for the detection of O-GlcNAc proteins. WGA binding to N-glycolylneuraminic acid (Neu5Ac) may modulate pro-Wheat germ lectin (WGA) from Triticum vulgaris exists as a homodimer and has multiple N-acetyl glucosamine (GlcNAc) binding sites. It is resistant to protein denaturation agents and is used for the detection of O-GlcNAc proteins. WGA binding to N-glycolylneuraminic acid (Neu5Ac) may modulate pro-inflammatory immune response.Application:Lectin from Triticum vulgaris (wheat) has been used:in lectin binding assay of samples from intrauterine stages of filarial parasitesin the histological studies of mice myocytesfor the generation bead-biotin-WGA complex with Dynabeads M-280 Streptavidin magnetic beads for lectin magnetic separation of Toxoplasma gondii oocytes from water samples... Read More | Inquire | Purity>95% as determined by SDS-PAGE and Coomassie blue stainingFunctionThe heparin-binding fibroblast growth factors play important roles in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. They are potent mitogens in vitro.Sequence Purity>95% as determined by SDS-PAGE and Coomassie blue stainingFunctionThe heparin-binding fibroblast growth factors play important roles in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. They are potent mitogens in vitro.Sequence similaritiesBelongs to the heparin-binding growth factors family.Cellular localizationSecreted. Cytoplasm. Cytoplasm > cell cortex. Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes (By similarity). Acts as a transcriptional activator or repressor (By similarity). Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3' (By similarity). When overexpressed, promotes cells to enter into S phase and proliferation... Read More | 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 |