1mg

Fibroblast Growth Factor- acidic (FGF-acidic) is a mitogen targeting at the endothelial cells, and belongs to the heparin binding FGF family, which contains 22 members. FGF-acidic binds to the receptor family FGFR1-4 in vivo with the assistance of heparin. However, along with FGF -basic, FGF-acidic lacks the signal peptide segment, and thus is not secreted via endoplasmic reticulum (ER) and Golgi bodies. Studies have shown that FGF-acidic is highly regulated, and it is a direct angiogenesis factor. If unregulated, angiogenesis could contribute to several diseases including arthritis, diabetes, ocular neovascularization, and especially tumors. Therefore, FGF-acidic is treated as a potential oncogene, and its overexpression is correlated tightly with several cancers.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, bFGF has the β trefoil structure. In vivo, bFGF is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. bFGF regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. bFGF can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of bFGF can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as HBGF-2, is a non-glycosylated heparin-binding growth factor that belongs to the FGF family. FGF-basic is present in basement membranes and in the subendothelial extracellular matrix of blood vessels. FGF-basic signals through FGFR1, 2, 3 and 4 that plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomyocytes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast growth factor receptor 2 (FGFR2) also known as CD332 is a receptor for fibroblast growth factor and it has important roles in embryonic development and tissue repair, especially bone and blood vessels. FGFR2 has two naturally occurring isoforms, FGFR2IIIb and FGFR2IIIc, created by splicing of the third immunoglobulin-like domain. FGFR2IIIb is predominantly found in ectoderm derived tissues and endothelial organ lining. Like the other members of the fibroblast growth factor receptor family, these receptors signal by binding to their ligand and dimerisation (pairing of receptors), which causes the tyrosine kinase domains to initiate a cascade of intracellular signals. On a molecular level these signals mediate cell division, growth and differentiation.

Fibroblast growth factor receptor 3(FGFR3) also known as CD333 (cluster of differentiation 333) is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. The FGFR3 gene produces various forms of the FGFR3 protein and the location varies depending on the isoform of the FGFR3 protein. Since the different forms are found within different tissues, the protein is responsible for multiple growth factor interactions. Gain of function mutations in FGFR3 inhibits chondrocyte proliferation and underlies achondroplasia and hypochondroplasia.

Fibroblast growth factor receptor 4(FGFR4) also known as CD334 (cluster of differentiation 334) is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation.

FGL1 (Fibrinogen-like protein 1), also known as hepatocyte-derived fibrinogen-related protein 1 (HFREP-1), HP-041, hepassocin (HPS), and liver fibrinogen-related protein 1 (LFIRE-1), is a liver-specific secreted protein belonging to the fibrinogen superfamily whose members share a fibrinogen domain at their C-termini. FGL1 is an immune suppressive molecule that inhibits the activation of antigen-specific T cells by acting as a major ligand of LAG3, and binds LAG3 independently of MHC class II.

Molecular Formula : C35H58O11

Molecular Formula : C23 2H9 H27 N2 O2

Molecular Formula : C19H30D4ClNO2

Molecular Formula : C913C2H5Cl2F3N215N2

Molecular Formula : C1013C2H4Cl2F6N215N2O2S

Molecular Formula : C1013C2H4Cl2F6N215N2OS

Molecular Formula : C17 H20 O5 S

Molecular Formula : C17 2H4 H16 O5 S

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

Molecular Formula : C2213C5H33N9O15P2 xNH3

Molecular Formula : C17 H16 O4

Molecular Formula : C24H22D4ClNO4

Molecular Formula : C17 2H3 H17 F6 N2 O3

Molecular Formula : C17H16D4F6N2O3

Molecular Formula : C33H21D4F3O4

Molecular Formula : C15 D4 H14 F2 N6 O7 S2

Molecular Formula : C12D3H11Cl2FNO4S

Molecular Formula : C10H11D3FNO3S

Molecular Formula : C813CH11F15N2O5

Fms-related tyrosine kinase 3 ligand (Flt3L) is growth fator stimulates the proliferation and differentiation of hematopoietic multipotent progenitors and promotes proliferation of NK cells and dendritic cell subgroups by combination with other growth factors. Flt3L is produced by T cells and stromal fibroblasts, and targeted various cells including hematopoietic stem cells, B cells, T cells, dendritic cells, and NK cells. Flt3L binds to it cognate tyrosine kinase receptor Flt3 and activates JAK/STAT signaling pathway.Flt3L is a hematopoietic four helical bundle cytokine with structurally homologous to stem cell factor (SCF) and colony stimulating facor 1 (CSF-1) demonstrated four conserved cysteines and two glycosylation sites. Flt3L naturally as a non-disulfide-linked homodimer with multiple isoforms. The extracellular portion is approximately 160 amino acid residues in length and the cytoplasmic segment is approximately 20-30 amino acid residues in length.

Molecular Formula : C15H9D3BrClF4N2O2

Molecular Formula : C16 2H3 H9 F N3 O3

Molecular Formula : C17 H12 Br F N4

Molecular Formula : C15 13C4 H16 Cl F N3 Na O5 S

Molecular Formula : C13H12F2N6O2

Molecular Formula : C13 2H4 H8 F2 N6 O

Molecular Formula : C1013C2H6F2N2O2

Molecular Formula : C913C3H6F2N2O2

Molecular Formula : C21 H29 F O5

Molecular Formula : C21H24D5FO5

Molecular Formula : C14H6D4F3NO2

Molecular Formula : C21 D3 H8 Cl F6 N2 O3

Molecular Formula : C21H29FO4

Molecular Formula : C23 H31 F O5

Molecular Formula : C13H7D3FN3O3

Molecular Formula : 13C3 C11 H12 F N O3

Molecular Formula : C22H25D3F2O5

Molecular Formula : C26H20D8Cl2F2N2