Agrin Antibody (Agr 33) [Janelia Fluor® 646] Summary
Immunogen |
Recombinant rat agrin, C-terminal construct. |
Epitope |
Epitope has been mapped near the 2nd laminin domain homology region and causes a marked reduction in the number of nicotinic acetylcholine receptor (nAChR) clusters. Insertion of an 8aa peptide at splicing site Z increases the clustering activity |
Localization |
Synaptic basal lamina at the neuromuscular junction. |
Specificity |
detects all isoforms of agrin. |
Isotype |
IgG1 |
Clonality |
Monoclonal |
Host |
Mouse |
Gene |
AGRN |
Purity |
Protein G purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Immunocytochemistry/ Immunofluorescence
- Immunohistochemistry
- Immunohistochemistry-Paraffin
- Western Blot
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Reactivity Notes
Cross-reacts with Mouse and Rat. Not yet tested in other species. Please note that this antibody is reactive to Mouse and derived from the same host, Mouse. Additional Mouse on Mouse blocking steps may be required for IHC and ICC experiments. Please contact Technical Support for more information.
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. |
Buffer |
50mM Sodium Borate |
Preservative |
0.05% Sodium Azide |
Purity |
Protein G purified |
Notes
Sold under license from the Howard Hughes Medical Institute, Janelia Research Campus.
Alternate Names for Agrin Antibody (Agr 33) [Janelia Fluor® 646]
Background
Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins during development at the neuromuscular junction. Agrin, MuSK and Rapsyn are all essential components for AChR aggregation, through an unknown mechanism. The C-terminal region of agrin is released into the medium, interacts with receptors on the muscle surface and induces AChR aggregation. The central region contains two O-linked glycosylation sites and a domain homologous to domain III of laminin. The N-terminal region anchors agrin to the extracellular matrix via other basal membrane components. This region also contains a protease inhibitor domain and glycosaminoglycan attachment sites; increasing the predicted MW from 200kDa to ~600kDa.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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