Vector Labs Ab03112-1.1 Anti-Glycoprotein GPIIb/IIIa complex [314.1], Mouse IgG1, kappa (200 μg) Centrifuge Bundle Savings at Sycamore Life Sciences

Description

Product Class: Purified
Clone ID: 314.1
Synonyms: Integrin beta-3; Platelet membrane glycoprotein IIIa; GPIIIa; CD61
Amount: 200 μg
Application Codes Clone: FC; Crystallization; in vivo; in vitro; SPR
Shipping Temperature: Wet Ice
Buffer Composition: PBS with 0.02% Proclin 300.
Original Format: IgG1
Storage Temperature: Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Specificity Statement: The antibody recognizes the N terminus of the GPIIb beta propeller domain only when soluble quinine is present.
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).

Product Class:	Purified
Clone ID:	314.1
Synonyms:	Integrin beta-3; Platelet membrane glycoprotein IIIa; GPIIIa; CD61
Amount:	200 μg
Application Codes Clone:	FC; Crystallization; in vivo; in vitro; SPR
Shipping Temperature:	Wet Ice
Buffer Composition:	PBS with 0.02% Proclin 300.
Original Format:	IgG1
Storage Temperature:	Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Specificity Statement:	The antibody recognizes the N terminus of the GPIIb beta propeller domain only when soluble quinine is present.
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).

Specifications

More Information
Brand	Vector Labs
UNSPSC	12161500

Reviews