Product nameRecombinant Human UNC5C protein
Protein lengthProtein fragment
Amino Acid Sequence
Amino acids498 to 597
Tagsproprietary tag N-Terminus
Our Abpromise guarantee covers the use of ab160125 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesProtein concentration is above or equal to 0.05 mg/ml.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.31% Glutathione, 0.79% Tris HCl
- homolog of C. elegans transmembrane receptor Unc5
- Netrin receptor UNC5C
- Protein unc 5 homolog C
FunctionReceptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion. Also involved in corticospinal tract axon guidances independently of DCC. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand.
Tissue specificityMainly expressed in brain. Also expressed in kidney. Not expressed in developing or adult lung.
Sequence similaritiesBelongs to the unc-5 family.
Contains 1 death domain.
Contains 1 Ig-like (immunoglobulin-like) domain.
Contains 1 Ig-like C2-type (immunoglobulin-like) domain.
Contains 2 TSP type-1 domains.
Contains 1 ZU5 domain.
modificationsPhosphorylated on different cytoplasmic tyrosine residues. Phosphorylation of Tyr-568 leads to an interaction with PTPN11 phosphatase, suggesting that its activity is regulated by phosphorylation/dephosphorylation. Tyrosine phosphorylation is netrin-dependent.
Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis.
- Information by UniProt
ab160125 has not yet been referenced specifically in any publications.