Terminal α-linked Galactose & N- Acetylgalactosamine (GalNAc) Reference: RPL-αGal Monomer MW: 14,161 Da. Protein is a dimer under physiological conditions (PBS pH7.2).
Terminal β-linked Galactose & N-Acetyllactosamine (LacNAc) Reference: RPL-Gal1 Monomer MW: 14,066 Da. Protein is a dimer under physiological conditions (PBS pH7.2).
Terminal α-linked Galactose Reference: RPL-Gal3 Monomer MW: 14,081 Da. Protein is a tetramer under physiological conditions (PBS pH7.2).
Terminal β-linked Galactose, N-Acetyllactosamine (LacNAc) & Lewis x (Lex) Reference: RPL-Gal4 Monomer MW: 14,595 Da. Protein is a tetramer under physiological conditions (PBS pH7.2).
Fucose/Mannose: Lewis a (Lea), Lewis x (Lex) & terminal a-mannose Reference: RPL-αMan Monomer MW: 13,130 Da Exists as dimer under physiological conditions (PBS, pH7.2).
Terminal α-mannose Reference: RPL-Man2 Monomer MW: 15,163 Da. Exists as a dimer under physiological conditions (PBS, pH7.2).
Terminal α2-3-linked Sialic Acid (Neu5Ac) — on both Nlinked and O-Linked Reference: RPL-Sia1 Monomer MW: 27,407.14 Da. Exists a monomer under physiological conditions (PBS pH7.2).
Terminal α2-3-linked Sialic Acid (Neu5Ac) — on O-Linked Glycans Reference: RPL-Sia2 Monomer MW: 40,725.17 Da. Exists as a monomer under physiological conditions (PBS pH7.2).
Terminal α-linked Neu5Ac Reference: RPL-Sia3 Monomer MW: 19,584.89 Da. Exists as a monomer under physiological conditions (PBS pH7.2).
Recombinant Human FGF2 Protein Reference: R00121 Fibroblast Growth Factor basic (FGF-basic/FGF-2) is a single-chain polypeptide growth factor that plays a significant role in the process of wound healing and is a potent inducer of angiogenesis. Several different forms of the human protein exist ranging from 18-24 kDa in size due to the use of alternative start sites within the fgf-2 gene. It has a 55 percent amino acid residue identity to FGF-1 and has potent heparin-binding activity. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor. Other homologous FGF belonging to the same family are int-2 (FGF-3), FGF-5, FGF-6, K-FGF and KGF ( keratinocyte growth factor = FGF-7). All factors are products of different genes, some of which are Oncogene products ( FGF-3, FGF-4, FGF-5 ).
Recombinant Mouse FGF2 Protein Reference: R00121-1 Fibroblast Growth Factor basic (FGF-basic/FGF-2) is a single-chain polypeptide growth factor that plays a significant role in the process of wound healing and is a potent inducer of angiogenesis. Several different forms of the human protein exist ranging from 18-24 kDa in size due to the use of alternative start sites within the fgf-2 gene. It has a 55 percent amino acid residue identity to FGF-1 and has potent heparin-binding activity. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor. Other homologous FGF belonging to the same family are int-2 (FGF-3), FGF-5, FGF-6, K-FGF and KGF (keratinocyte growth factor = FGF-7). All factors are products of different genes, some of which are Oncogene products (FGF-3, FGF-4, FGF-5).