C1QBP Antikörper (Complement Component 1, Q Subcomponent Binding Protein) Primary Antibody
- Target Alle C1QBP Antikörper anzeigen
- Dieser C1QBP Antikörper ist unkonjugiert
- Functional Studies (Func), Immunoassay (IA), Flow Cytometry (FACS), Immunoprecipitation (IP), Western Blotting (WB)
- Kreuzreaktivität (Details)
- Cross reactivity: Rat : Yes, Syrian hamster : Yes
- 0.2 μm filtered
anti-Complement Component 1, Q Subcomponent Binding Protein (C1QBP) antibody Primary Antibody
C1QBP Reaktivität: Human, Fledermaus, Hund, Pferd ELISA, IHC, IHC (p) Wirt: Kaninchen Polyclonal unconjugatedanti-Complement Component 1, Q Subcomponent Binding Protein (C1QBP) (Internal Region) antibody Primary Antibody
C1QBP Reaktivität: Human, Maus, Ratte ELISA, ICC, IF, IHC, WB Wirt: Kaninchen Polyclonal unconjugated
- For flow cytometry and Western blotting, dilutions to be used depend on detection system applied. It is recommended that users test the reagent and determine their own optimal dilutions. The typical starting working dilution is 1:50. For functional studies, in vitro dilutions have to be optimized in user's experimental setting. Website:
- Nur für Forschungszwecke einsetzbar
- PBS, containing 0.1 % bovine serum albumin.
- 4 °C
- Informationen zur Lagerung
- Product should be stored at 4 °C. Under recommended storage conditions, product is stable for one year.
- 12 months
Role of the receptor for the globular domain of C1q protein in the pathogenesis of hepatitis C virus-related cryoglobulin vascular damage." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 183, Issue 9, pp. 6013-20, (2009) (PubMed).
: "gC1qR/p33 blockade reduces Staphylococcus aureus colonization of target tissues in an animal model of infective endocarditis." in: Infection and immunity, Vol. 74, Issue 8, pp. 4418-23, (2006) (PubMed).
: "Surface expression of complement receptor gC1q-R/p33 is increased on the plasma membrane of human spermatozoa after capacitation." in: Biology of reproduction, Vol. 66, Issue 3, pp. 823-9, (2002) (PubMed).
: "gC1q-R/p33, a member of a new class of multifunctional and multicompartmental cellular proteins, is involved in inflammation and infection." in: Immunological reviews, Vol. 180, pp. 65-77, (2001) (PubMed).
: "Identification of functional domains on gC1Q-R, a cell surface protein that binds to the globular "heads" of C1Q, using monoclonal antibodies and synthetic peptides." in: Hybridoma, Vol. 15, Issue 5, pp. 333-42, (1997) (PubMed).
: "Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-R, associate to form a complex." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 159, Issue 3, pp. 1429-36, (1997) (PubMed).
- Role of the receptor for the globular domain of C1q protein in the pathogenesis of hepatitis C virus-related cryoglobulin vascular damage." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 183, Issue 9, pp. 6013-20, (2009) (PubMed).
- C1QBP Produkte
- SF2, X38k, gC1qR, C1QBP, GC1QBP, HABP1, SF2p32, gC1Q-R, p32, AA407365, AA986492, D11Wsu182e, P32, gC1qBP, Habp1, complement C1q binding protein, complement component 1, q subcomponent binding protein S homeolog, complement component 1, q subcomponent binding protein, C1QBP, c1qbp.S, LOC100227158, C1qbp
- The monoclonal antibody 60.11 recognizes a cell membrane C1q binding molecule that recognises the globular heads of C1q. It is also present in plasma and the extracellular matrix. The molecule is an unusually acidic, single chain protein with an apparent molecular weight of 33 kDa. It does not possess a conventional sequence motif compatible with a membrane spanning segment nor a consensus site for a GPI anchor. gC1q-R migrates as a single chain under both reducing and non-reducing conditions, but it behaves as an oligomer on gel-filtration in non-dissociating conditions. Its multimer formation may be a critical process by which the gC1q-R molecule increases its affinity for multivalent ligands such as C1q. gC1q-R has been shown to inhibit complement activation by preventing the binding of C1q to antibodies, suggesting that the binding site for gC1q-R and the binding site for immune complexes, which are present on the C1q globular 'heads', may be located at the same position. gC1q-R is capable of interacting with several proteins involved in blood clotting, namely, thrombin, prothrombin, the heparinbinding form of vitronectin, the ternary complex, vitronectin-thrombin-antithrombin, as well as high-molecular-weight kininogen and Hageman factor. Besides its role in the complement pathway, gC1q-R participates in enhancement of Fc-receptor and CR1-mediated phagocytosis, procoagulant activity on platelets, and chemotactic activity on mast cells, eosinophils, neutrophils, and fibroblasts. gC1q-R is expressed on a wide variety of cells and can serve as a binding site for plasma and microbial proteins. Its antigenic sites may be cryptic on cells in suspension but become exposed when the cells are fixed by bifunctional cross-linkers. Probably it is also expressed on the cell membrane as a tetramer. Crosslinking or activation may thus bring about a tetrameric assembly of gC1q-R followed by a conformational change within the molecule, thereby exposing epitopes which are otherwise hidden. A form of GC1q-R is also found inside the cell. Intracellular gC1q-R has been shown to bind the cytoplasmic tail of the α1B-adrenergic receptor and to PKCμ. The monoclonal antibody 60.11 is directed against epitopes situated within the NH2-terminal stretch of gC1q-R corresponding to residues 76-93.
- Ribonucleoprotein Complex Subunit Organization, Ribosome Assembly