Hi-Affi™ Recombinant Anti-Human VWF (A1 domain) Monoclonal antibody
Hi-Affi™ Recombinant Human Anti-Human VWF (A1 domain) Monoclonal antibody for Inhib, IP, ELISA
COA
Key features and details
- Specificity: The NMC-4 antibody binds the GP1b-α binding site on the A1 domain of human von Willebrand factor (also know as vWF or Factor VIII related antigen).
- Isotype: IgG
- Application: Inhib, IP, ELISA
- Multiplex assay ready: PBS only formulation, ready for custom conjugation.
Specifications
Antibody Isotype
IgG
Clone
NMC-4
Species Reactivity
Human
Immunogen
The original antibody was generated by immunization of BALB/C mice with FVIII/vWF fraction and fusion of spleen cells with NS-1 murine myeloma cells.
Conjugate
Unconjugated
Applications
Application Notes
Suitable for use in Inhib, IP, ELISA.
Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
General Notes
Recombinant monoclonal antibody to VWF. Produced utilizing a recombinant platform technology. It can be used in Inhib, IP, ELISA.
Target
Alternative Names
von Willebrand Factor; VWF
Custom Antibody Labeling
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More
Citations
Publication (1)
Publication (1)
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Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab.
(1998) Nat Struct Biol 5: 189-194
Authors: Celikel, R., Varughese, K.I., Madhusudan, Yoshioka, A., Ware, J., Ruggeri, Z.M.
The presence of one or more copies of von Willebrand factor type A domains identifies a superfamily of proteins usually involved in biological processes controlled by specific molecular interactions, often adhesive in nature. We have solved the crystal structure of the prototypic von Willebrand factor A1 domain, essential for the antihemorrhagic activity of platelets, in complex with the function blocking antibody, NMC-4, at 2.2 A resolution. This has led to the recognition of a putative binding groove for the platelet receptor, glycoprotein Ib alpha, formed by two adjacent alpha-helices and a beta-strand. The structure also shows a contact interface between A1 domain pairs, suggesting a hypothetical mechanism for the regulation of protein assembly and heterologous ligand binding mediated by homophilic interactions of type A domains.
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Catalog # DMAB-CS25317
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