| Description | Format:1-ComponentEnzyme:Alkaline Phosphatase | 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% SDS-PAGEFunctionHas hepatocyte mitogenic activity | IFN-αs are proteins secreted by leukocyte. They are mainly involved in innate immune response against viral infection. The IFN-α family has 13 subtypes and 23 different variants. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166IFN-αs are proteins secreted by leukocyte. They are mainly involved in innate immune response against viral infection. The IFN-α family has 13 subtypes and 23 different variants. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Neural cell adhesion molecule 1 (NCAM-1) is a multifunctional member of the Ig superfamily. It belongs to a family of membrane-bound glycoproteins that are involved in Ca++ independent cell matrix and homophilic orPurity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Neural cell adhesion molecule 1 (NCAM-1) is a multifunctional member of the Ig superfamily. It belongs to a family of membrane-bound glycoproteins that are involved in Ca++ independent cell matrix and homophilic or heterophilic cell-cell interactions. NCAM-1 specifically binds to heparan sulfate proteoglycans, the extracellular matrix protein agrin, and several chondroitin sulfate proteoglycans that include neurocan and phosphocan. There are three main forms of human NCAM-1 that arise by alternate splicing. These are designated NCAM-120/NCAM-1 (761 amino acids [aa]), NCAM‑140 (848 aa), and NCAM-180 (1120 aa). NCAM-120 is GPI-linked, while NCAM‑140 and NCAM-180 are type I transmembrane glycoproteins. Additional alternate splicing adds considerable diversity to all three forms, and extracellular proteolytic processing is possible for NCAM-180. NCAM-1 is synthesized as a 761 aa preproprecursor that contains a 19 aa signal sequence, a 722 aa GPI-linked mature region, and a 20 aa C-terminal prosegment. The molecule contains five C-2 type Ig-like domains and two fibronectin type-III domains. Human to mouse, NCAM-1 is 93% aa identical. NCAM-1 appears to be highly sialylated. The polysialyation of NCAM-1 reduces its adhesive property and increases its neurite outgrowth promoting features. NCAM-1 in the adult brain shows a decline of sialylation relative to earlier developmental periods. In regions that retain a high degree of neuronal plasticity, however, the adult brain continues to express polysialylation-NCAM-1, suggesting sialylation of NCAM-1 is involved in regenerative processes and synaptic plasticity... Read More |