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C1qC [A-12]
Description C1q, a subcomponent of the classical complement pathway, is composed of nine subunits that mediate classical complement activation and thereby play an important role in the immune response. Six of these subunits are disulfide-linked dimers of chains A and B, while three of these subunits, designated C1q-A through C1q-C, are disulfide-linked dimers of chain C. The presence of receptors for C1q on effector cells modulates its activity, which may be antibody-dependent or independent. Macrophages are the primary source of C1q, while anti-inflammatory drugs as well as cytokines differentially regulate expression of the mRNA, as well as the protein. However, its ability to modulate the interaction of platelets with collagen and immune complexes suggests C1q influences homeostasis as well as other immune activities, and perhaps thrombotic complications resulting from immune injury. Defects in C1q-A, C1q-B and C1q-C cause inactivation of the classical pathway, leading to a rare genetic disorde Host Mouse Application ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human -
C5b9/TCC/MAC [aE11]
Description The complement component proteins: C2, C3, C4 and C5 are potent anaphylatoxins that are released during complement activation. Binding of these proteins to their respective G protein-coupled receptors, C3aR, C1R and C5aR, induces proinflammatory events, such as cellular degranulation, smooth muscle contraction, arachidonic acid metabolism, cytokine release, leukocyte activation and cellular chemotaxis. Activation of the complement system leads to the formation of C5b-9 terminal complex, and while C5b-9 can promote cell lysis, the sublytic assembly of C5b-9 on plasma membranes causes an opposite result and induces cell cycle activation and survival. C5b-9 can rescue oligodendrocytes from FAS-mediated apoptosis by regulating caspase-8 processing via PI 3-K signaling. C5b-9 may play a pro-inflammatory role in the acute phase of multiple sclerosis, but may also be neuroprotective during the chronic phase of the disease. (Shipping Cost: €200.00) Host Mouse Application ELISA, Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC)-F Reactivity Human, Horse,Pig (Porcine), Monkey, Baboon -
CD130/gp130/IL-6RB [AN-H2]
Description The activation of the IL-6 protein is dependent upon the binding of cytokines to their receptors. vIL6, a protein related to IL-6 and encoded by the Kaposi sarcoma-associated herpesvirus, can bypass the IL-6 receptor (IL-6R) and directly activate this protein. IL-6 first binds to IL-6R which subsequently associates with a gp130 dimer. The active signaling complex consists of at minimum IL-6, IL-6R and a dimer of two gp130 proteins that are linked by a disulfide bond. The second subunit of the IL-6 complex, gp130, also functions as a component of several additional receptor complexes including leukemia inhibitory factor (LIF), oncostatin M (OSM), ciliary neurotrophic factor (CNTF) and IL-11. LIF binds to the LIF receptor with low affinity and to a complex of the LIF receptor and gp130 with high affinity while OSM appears to bind to gp130 with low affinity and to a complex of gp130 and the LIF receptor with high affinity. The protein encoded by this gene is a signal transducer shared by Host Mouse Application ELISA, Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human -
CD130/gp130/IL-6RB [AN-H2]
Description The activation of the IL-6 protein is dependent upon the binding of cytokines to their receptors. vIL6, a protein related to IL-6 and encoded by the Kaposi sarcoma-associated herpesvirus, can bypass the IL-6 receptor (IL-6R) and directly activate this protein. IL-6 first binds to IL-6R which subsequently associates with a gp130 dimer. The active signaling complex consists of at minimum IL-6, IL-6R and a dimer of two gp130 proteins that are linked by a disulfide bond. The second subunit of the IL-6 complex, gp130, also functions as a component of several additional receptor complexes including leukemia inhibitory factor (LIF), oncostatin M (OSM), ciliary neurotrophic factor (CNTF) and IL-11. LIF binds to the LIF receptor with low affinity and to a complex of the LIF receptor and gp130 with high affinity while OSM appears to bind to gp130 with low affinity and to a complex of gp130 and the LIF receptor with high affinity. The protein encoded by this gene is a signal transducer shared by Host Mouse Application ELISA, Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human -
CD162 (Selectin P Ligand [PSGL1/1601]
Description CD162 glycoprotein functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of this gene and polymorphisms in this gene are associated with defects in the innate and adaptive immune response. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human -
CD162 (Selectin P Ligand [PSGL1/1601]
Description CD162 glycoprotein functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of this gene and polymorphisms in this gene are associated with defects in the innate and adaptive immune response. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human -
CD42a [A9]
Description The CD42a antibody recognizes a 17 to 22-kilodalton (kDa) single-chain, platelet membrane glycoprotein, also known as gpIX that forms a noncovalent complex with gpIb and gpV. Glycoprotein Ib consists of an α–chain disulfide-linked to a β chain. Glycoproteins Ibα (140 to 145 kDa), Ibβ (24 to 25 kDa), and V (82 to 86 kDa) have been designated as CD42b, CD42c and CD42d respectively. CD42a has been reported to react with both gpIX and the gpIb-IX-V complex. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
CD42b [42C01]
Description The CD42b glycoprotein, also known as GPIb, is a co-factor of ristocetin-induced aggregation and is involved in the binding of platelets to blood vessel walls. The CD42b antigen is expressed on platelets and on megakaryocytes in bone marrow. The absence of CD42b antigen on platelets may indicate Bernard-Soulier disease. CD42b is a platelet activation marker involved in the process of coagulation as an aggregating factor. It interacts with extracellular matrix as well as with adhesion molecules. Its expression and activation seems to be regulated by VEGF and PDGF. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
CD42b [42C01]
Description The CD42b glycoprotein, also known as GPIb, is a co-factor of ristocetin-induced aggregation and is involved in the binding of platelets to blood vessel walls. The CD42b antigen is expressed on platelets and on megakaryocytes in bone marrow. The absence of CD42b antigen on platelets may indicate Bernard-Soulier disease. CD42b is a platelet activation marker involved in the process of coagulation as an aggregating factor. It interacts with extracellular matrix as well as with adhesion molecules. Its expression and activation seems to be regulated by VEGF and PDGF. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
CD64/IGFR1 Polyclonal
Description This antibody recognizes CD64 also known as FcRI. CD64 is a high affinity activatory receptor for IgG2a and a low affinity receptor for IgG2b and IgG3 type antibodies. The interaction between Fc receptors and antibodies play important roles in both the innate and adaptive immune responses. CD64 through binding of the Fc segment of IgG, mediates phagocytosis and plays a role in antibody-dependent cellular cytotoxicity and clearance of immune complexes. In addition, CD64 also functions as an antigen capture for presentation to T-cells and also mediates the release of cytokines and reactive oxygen intermediates including interleukin (IL)-1, IL-6 and tumor necrosis factor (TNF) alpha. It is constitutively expressed on monocytes and macrophages, germinal centre dendritic cells and early myeloid lineage cells, but not lymphocytes. Expression on monocytes can be strongly upregulated by treatment with interferon (IFN) gamma or G-CSF, and can be induced on neutrophils and eosinophils by IFN gam Host Rabbit Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Mouse, Rat