100-059

Human CTLA-4 Fc Recombinant Protein

CTLA-4 and CD28 are receptors of the immunoglobulin superfamily that are expressed, along with the transmembrane glycoproteins B7-1 and B7-2, by antigen-presenting cells, and with these ligands constitute crucial co-stimulatory pathways for T and B cell regulatory responses. It is through engagement with CD28 and CTLA-4 that the B7 family ligands B7-1 and B7-2 play principal roles in immunity by activating immune response and maintaining immune tolerance. Co-stimulatory signals generated by B7-1 and B7-2 interactions with CD28 serve to stimulate T cell activation and prevent anergy through the amplification of T cell receptor (TCR) signaling. In contrast, interactions of the ligands with CTLA-4 serves to maintain T cell homeostasis and self-tolerance through the disruption of stimulatory signaling from B7 isoform-bound CD28 complexes, and by inducing powerful inhibitory signals in T cells. CTLA-4, like B7-1, is only poorly expressed on resting dendritic cells; therefore, up-regulation of their interaction and resultant amplification and regulation of T cell activity at peripheral inflammation sites is considerably delayed upon immune activation. Conversely, B7-2 and CD28 are constitutively expressed by resting hematopoietic and T cells, respectively, and as a result are able to rapidly induce up-regulation upon immune activation, making them critical to the early co-stimulatory signaling of immune response. Unlike B7-1 and B7-2, the ligands PD-L1 (or B7-H1) and B7-H2, which also belong to the B7 family, have not been shown to influence immunity through interaction with CTLA-4. B7-H2 has been shown to have restricted interaction with CD28. The difference in expression of B7-1, B7-2 and B7-H2 may enable temporally and spatially-specific regulation of T cell response through non-competitive CD28 interaction. Recombinant Human CTLA-4 Fc is a glycosylated, disulfide-linked homodimer of 714 amino acid residues whose monomer consists of the 124-amino-acid length extracellular portion of CTLA-4 fused to the 231-amino-acid length Fc portion of human IgG1 by two glycines. The calculated molecular weight of Recombinant Human CTLA-4 Fc dimer is 78.7 kDa; however, due to glycosylation, the monomer and dimer migrate at apparent molecular weights of approximately 45–50 kDa and 80–90 kDa by SDS-PAGE analysis under reducing conditions.

448.96 €

100-059S

Human CTLA-4 Fc Recombinant Protein

CTLA-4 and CD28 are receptors of the immunoglobulin superfamily that are expressed, along with the transmembrane glycoproteins B7-1 and B7-2, by antigen-presenting cells, and with these ligands constitute crucial co-stimulatory pathways for T and B cell regulatory responses. It is through engagement with CD28 and CTLA-4 that the B7 family ligands B7-1 and B7-2 play principal roles in immunity by activating immune response and maintaining immune tolerance. Co-stimulatory signals generated by B7-1 and B7-2 interactions with CD28 serve to stimulate T cell activation and prevent anergy through the amplification of T cell receptor (TCR) signaling. In contrast, interactions of the ligands with CTLA-4 serves to maintain T cell homeostasis and self-tolerance through the disruption of stimulatory signaling from B7 isoform-bound CD28 complexes, and by inducing powerful inhibitory signals in T cells. CTLA-4, like B7-1, is only poorly expressed on resting dendritic cells; therefore, up-regulation of their interaction and resultant amplification and regulation of T cell activity at peripheral inflammation sites is considerably delayed upon immune activation. Conversely, B7-2 and CD28 are constitutively expressed by resting hematopoietic and T cells, respectively, and as a result are able to rapidly induce up-regulation upon immune activation, making them critical to the early co-stimulatory signaling of immune response. Unlike B7-1 and B7-2, the ligands PD-L1 (or B7-H1) and B7-H2, which also belong to the B7 family, have not been shown to influence immunity through interaction with CTLA-4. B7-H2 has been shown to have restricted interaction with CD28. The difference in expression of B7-1, B7-2 and B7-H2 may enable temporally and spatially-specific regulation of T cell response through non-competitive CD28 interaction. Recombinant Human CTLA-4 Fc is a glycosylated, disulfide-linked homodimer of 714 amino acid residues whose monomer consists of the 124-amino-acid length extracellular portion of CTLA-4 fused to the 231-amino-acid length Fc portion of human IgG1 by two glycines. The calculated molecular weight of Recombinant Human CTLA-4 Fc dimer is 78.7 kDa; however, due to glycosylation, the monomer and dimer migrate at apparent molecular weights of approximately 45–50 kDa and 80–90 kDa by SDS-PAGE analysis under reducing conditions.

442.99 €

MBS692293-005mg

Human CTLA-4 Fc

573.17 €

SFC-021

Human FGFR-4/Fc Chimera, soluble Recombinant Protein

Recombinant human soluble FGFR-4 was fused with the Fc-part of human IgG1. Human recombinant soluble FGFR-4/Fc is a disulfide-linked heterodimeric protein. In the reduced form the glycosylated subunits of sFGFR-4 alpha/human Fc chimera display a molecular mass of 80-85 kDa. Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorigenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1 to -4, are known. All four genes for FGF-receptors encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the beta isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.

390.49 €

SFC-022

Human FGFR-4/Fc Chimera, soluble Recombinant Protein

Recombinant human soluble FGFR-4 was fused with the Fc-part of human IgG1. Human recombinant soluble FGFR-4/Fc is a disulfide-linked heterodimeric protein. In the reduced form the glycosylated subunits of sFGFR-4 alpha/human Fc chimera display a molecular mass of 80-85 kDa. Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorigenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the beta isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.

406.02 €

71170

Human CD137 (4-1BB), Fc fusion

Human secreted CD137, Fc fusion protein, also known as Tumor Necrosis Factor Receptor Superfamily member 9, TNFRSF9, and ILA, GenBank Accession No. NM_001561, a.a. 24-186 expressed in a HEK293 cell expression system. MW = 44 kDa (monomer). This protein runs at a higher MW by SDS-PAGE due to glycosylation.

643.88 €