Anti-Glycoprotein GPIIb/IIIa complex [314.1]
Catalogue Number: AB03112-1.1-ABA
| Manufacturer: | Vector Laboratories, Inc (ABA) |
| Type: | Recombinant Monoclonal |
| Alias: | Integrin beta-3; Platelet membrane glycoprotein IIIa; GPIIIa; CD61 |
| Shipping Condition: | Blue Ice |
| Unit(s): | 200 ug |
| Host name: | Mouse |
| Clone: | 314.1 |
| Isotype: | IgG1 |
| Immunogen: | The original antibody was generated by immunizing BALB/c mice with a mixture of quinine-linked GPIIb/IIIa, unlinked GPIIb/IIIa, and soluble quinine. |
| Application: | FC, InVitroA, InVivoA, SPR, Crstion |
Additional Text
Gene Name
ITGB3
Gene ID
3690
Uniprot ID
P05106
Purification
Purified
Antibody Clonality
Recombinant Monoclonal
Storage Note
Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Application Notes
The antibody reacted with normal human platelets in the presence of quinine, as shown by flow cytometry. The reactions of the antibody with CHO cells expressing all-human GPIIb/IIIa (H/H), all-rat GPIIb/IIIa (R/R), or human/rat mixed GPIIb/IIIa integrins (H/R, R/H) were studied by flow cytometry. Quinine dependent antibody binding occurred with constructs H/H and H/R, but not with R/R or R/H (Bougie et al., 2009; PMID: 18948570). Nonobese diabetic/severe combined immunodeficient (NOD/scid) mouse was used as a model to study drug-dependent clearance of platelets in vivo. Mice were first infused with human platelets and then injected with the antibody and quinine or buffer; platelets were cleared from the circulation when the antibody and quinine were injected, whereas the antibody alone was without effect. (Bougie et al., 2010; PMID: 20587782) GPIIb/IIIa bound monovalently to the immobilized antibody with low affinity in the absence of quinine and with fivefold greater affinity when quinine was present (KD ~ 2.2*10^-6), as shown by SPR analysis. Measurements of quinine-dependent binding of intact antibody and Fab fragment to platelets showed that affinity is increased 10 000- to 100 000-fold by bivalent interaction between antibody and its target, as determined by flow cytometry (Bougie et al., 2015; PMID: 26353910). The crystal structures of the Fab fragment and its complex with quinine were determined. Quinine induced structural modifications of the Fab fragment; the authors propose that quinine remodels the Fab paratope and enables binding to the platelet GPIIb/IIIa. The monovalent KD values for quinine binding to the IgG fragment measured was 58 nM (Zhu et al., 2015; PMID: 26282540).
AB03112-1.1 Datasheet
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