Fibrinogen From Human Plasma, Alexa Fluor™ 647 Conjugate
Fibrinogen From Human Plasma, Alexa Fluor™ 647 Conjugate
Invitrogen™

Fibrinogen From Human Plasma, Alexa Fluor™ 647 Conjugate

Molecular Probes™ fibrinogen conjugates are prepared by attaching fluorescent dye molecules to purified human fibrinogen (approximately 15 dye molecules forMás información
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Número de catálogoCantidad
F352005 mg
Número de catálogo F35200
Precio (CLP)
-
Cantidad:
5 mg
Molecular Probes™ fibrinogen conjugates are prepared by attaching fluorescent dye molecules to purified human fibrinogen (approximately 15 dye molecules for each fibrinogen molecule), purifying the conjugate to remove unreacted dye, and then lyophilizing for storage.

Fluorescently labeled fibrinogen has proven to be a valuable tool for investigating platelet activation and subsequent fibrinogen binding. For instance, fluorescein-labeled fibrinogen has been used to detect fibrinogen bound to activated platelets by flow cytometry.

Human Fibrinogen Conjugate Specifications:
• Label (Ex/Em): Alexa Fluor™ 647 (∼650/668 nm)
• Spectrally similar to Cy™5 dye conjugates
• Lyophilized product can be dissolved in buffer (e.g., sodium bicarbonate, pH 8.3) for use
• Fluorescence is typically detected using fluorescence microscopy or flow cytometry


Find More Probes for Cell Adhesion and Receptor Binding
Review Probes for Cell Adhesion, Chemotaxis, Multidrug Resistance and Glutathione—Section 15.6 and Probes for Following Receptor Binding and Phagocytosis—Section 16.1 in the Molecular Probes™ Handbook for more information on these probes.

For Research Use Only. Not for human or animal therapeutic or diagnostic use.
For Research Use Only. Not for use in diagnostic procedures.
Especificaciones
Tipo de etiquetaAlexa Fluor Dyes
Línea de productosAlexa Fluor
Subtipo de proteínaFibrinogen
Cantidad5 mg
Condiciones de envíoRoom Temperature
ConjugadoAlexa Fluor 647
FormularioLyophilized
EspecieHuman
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador (de -5 a -30 °C) y proteger de la luz.

Citations & References (14)

Citations & References
Abstract
Control of integrin alphaIIb beta3 outside-in signaling and platelet adhesion by sensing the physical properties of fibrin(ogen) substrates.
Authors:Podolnikova NP, Yermolenko IS, Fuhrmann A, Lishko VK, Magonov S, Bowen B, Enderlein J, Podolnikov AV, Ros R, Ugarova TP,
Journal:Biochemistry
PubMed ID:19929007
The physical properties of substrates are known to control cell adhesion via integrin-mediated signaling. Fibrin and fibrinogen, the principal components of hemostatic and pathological thrombi, may represent biologically relevant substrates whose variable physical properties control adhesion of leukocytes and platelets. In our previous work, we have shown that binding of ... More
mTOR-dependent synthesis of Bcl-3 controls the retraction of fibrin clots by activated human platelets.
Authors:Weyrich AS, Denis MM, Schwertz H, Tolley ND, Foulks J, Spencer E, Kraiss LW, Albertine KH, McIntyre TM, Zimmerman GA,
Journal:Blood
PubMed ID:17110454
'New activities of human platelets continue to emerge. One unexpected response is new synthesis of proteins from previously transcribed RNAs in response to activating signals. We previously reported that activated human platelets synthesize B-cell lymphoma-3 (Bcl-3) under translational control by mammalian target of rapamycin (mTOR). Characterization of the ontogeny and ... More
Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets.
Authors:Zou Z, Chen H, Schmaier AA, Hynes RO, Kahn ML,
Journal:Blood
PubMed ID:17170121
A unique aspect of integrin receptor function is the transmission of bidirectional signals. In platelets alphaIIbbeta3 integrins require
Requirements of SLP76 tyrosines in ITAM and integrin receptor signaling and in platelet function in vivo.
Authors:Bezman NA, Lian L, Abrams CS, Brass LF, Kahn ML, Jordan MS, Koretzky GA,
Journal:J Exp Med
PubMed ID:18663126
Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP76), an adaptor that plays a critical role in platelet activation in vitro, contains three N-terminal tyrosine residues that are essential for its function. We demonstrate that mice containing complementary tyrosine to phenylalanine mutations in Y145 (Y145F) and Y112 and Y128 ... More
Force-FAK signaling coupling at individual focal adhesions coordinates mechanosensing and microtissue repair.
Authors:
Journal:Nat Commun
PubMed ID:33883558