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Gewähltes Kit
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96-Well Plate
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
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Purified immunoglobulin. The antibody is supplied in 25mM Tris-HCl, 0.4M NaCl, pH 8.0 containing 0.2% bovine serum albumin and 0.1% sodium azide. The characteristics of each lot are tested by electrophoresis and flow cytometry.
Anti-CD42a Antibody, platelet lb-IX, clone FMC-25 detects level of CD42a & has been published & validated for use in FC, IC, IH.
Key Applications
Flow Cytometry
Immunocytochemistry
Immunohistochemistry
Application Notes
The glycoprotein Ib-IX complex on the surface of normal platelets is a heterotrimer of Ib-alpha, Ib-beta and IX subunits (Berndt, 1989). Ib-IX complex is an essential component of platelet adhesion to vascular subendothelium and is also important in the maintenance of platelet shape (Berndt et al., 1988).
This antibody is suitable for enumeration of platelets by flow cytometry and immunoperoxidase staining of frozen tissue sections or air dried smear preparations (San Miguel et al., 1986), and for identification of megakaryoblasts in acute myeloid leukemia or acute myelofibrosis (San Miguel et al., 1985; San Miguel et al., 1986).
SUGGESTED USAGE DILUTION
1. Flow cytometry and indirect immunofluorescence 1:25
Dilute with isotonic buffer. Use 50 μl of diluted antibody per 1 x 10E6 platelets in 100 μl of buffer.
2. Indirect immunoperoxidase staining - the final dilution will depend on the assay conditions and detection system employed. However, a dilution of at least 1:20 will be applicable to most commonly used systems.
Biological Information
Immunogen
Peripheral blood mononuclear cells isolated on Ficoll™ hypaque.
Epitope
platelet lbalpha complex
Clone
FMC-25
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Mouse
Specificity
This antibody belongs to CD42a (assigned at the Fourth International Workshop on Leukocyte Differentiation Antigens, Vienna, 1989) (Knapp, 1989), and binds to the 22,000 dalton IX subunit of the glycoprotein Ib-IX complex (Zola et al., 1984; Berndt et al., 1985a,b). FMC-25 failed to bind to platelets from patients with Bernard-Soulier Syndrome (Berndt et al., 1983). The antibody is specific for cells of the platelet megakaryocyte lineage. It reacts with a proportion of acute myeloid leukemias being useful in identifying those of the megakaryoblastic subtype (San Miguel et al., 1985, 1986).
Cell reactivity:
The antibody is specific for cells of the platelet megakaryocyte lineage. It reacts with a proportion of acute myeloid leukemias being useful in identifying those of the megakaryoblastic subtype(San Miguel et al., 1985, 1986).
Platelet glycoprotein IX (GP9) is a small membrane glycoprotein found on the surface of human platelets. It forms a 1-to-1 noncovalent complex with glycoprotein Ib (GP Ib), a platelet surface membrane glycoprotein complex that functions as a receptor for von Willebrand factor (VWF; MIM 193400). The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with GP9 and platelet glycoprotein V (GP5; MIM 173511).[supplied by OMIM]
FUNCTION: SwissProt: P14770 # The GPIb-V-IX complex functions as the von Willebrand factor receptor and mediates von willebrand factor-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib. SIZE: 177 amino acids; 19046 Da SUBUNIT: GP-Ib alpha and beta are disulfide linked. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. DISEASE:SwissProt: P14770 # Defects in GP9 are a cause of Bernard-Soulier syndrome (BSS) [MIM:231200]; also known as giant platelet disease (GPD). BSS patients have unusually large platelets and have a clinical bleeding tendency. SIMILARITY: SwissProt: P14770 ## Contains 1 LRR (leucine-rich) repeat. MISCELLANEOUS: Platelet activation apparently involves disruption of the macromolecular complex of GP-Ib with the platelet glycoprotein IX (GP-IX) and dissociation of GP-Ib from the actin- binding protein.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Store at 2 to 8°C, for up to 6 months. For prolonged periods, store below -20°C in undiluted aliquots. AVOID REPEATED FREEZE/THAW CYCLES.
WARNING: The monoclonal reagent solution contains 0.1% sodium azide as a preservative. Due to potential hazards arising from the build up of this material in pipes, spent reagent should be disposed of with liberal volumes of water.
Trp207Gly in platelet glycoprotein Ibalpha is a novel mutation that disrupts the connection between the leucine-rich repeat domain and the disulfide loop structure and causes Bernard-Soulier syndrome. Rosenberg, N, et al. J. Thromb. Haemost., 5: 378-86 (2007)
2007
BACKGROUND: Bernard-Soulier syndrome (BSS) is a severe inherited bleeding disorder that is caused by a defect in glycoprotein (GP)Ib-IX-V complex, the platelet membrane receptor for von Willebrand factor. PATIENTS: The diagnosis of BSS was made in two members of a Bukharian Jewish family who had life-long thrombocytopenia associated with mucocutaneous bleeding manifestations. METHODS AND RESULTS: Flow cytometry and Western blot analyses showed only trace amounts of GPIb and GPIX on the patients' platelets. Sequence analysis of the GPIbalpha gene revealed a homozygous T > G transversion at nucleotide 709 predicting Trp207Gly substitution in the mature protein. Introduction of the mutation into a mammalian expression construct abolished the surface expression of GPIbalpha in transfected baby hamster kidney cells. The crystal structure of the N-terminus of GPIbalpha (PDB: 1SQ0) indicates that Trp207 is completely buried and located in a disulfide loop structure that interacts with the leucine-rich repeat (LRR) domain. CONCLUSION: A novel mutation, Trp207Gly, causes BSS and predicts disruption of the interaction between a disulfide loop and the LRR domain that is essential for the integrity of GPIbalpha structure.
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