- Peptide (C)RVRIRSKVFGLHSVSR, corresponding to amino acid residues 481-496 of rat CRMP1 (Accession Q62950). Intracellular.
- Western blot analysis of mouse brain (lanes 1 and 5), rat cortex (lanes 2 and 6), rat new born brain (lanes 3 and 7) and human brain glioblastoma (U-87 MG) cell line lysates:1-4. Anti-CRMP1 Antibody (#AIP-028), (1:200).
5-8. Anti-CRMP1 Antibody, preincubated with CRMP1 Blocking Peptide (#BLP-IP028).
Collapsin response mediator proteins (CRMPs) are a family of cytosolic phosphoproteins that were originally identified in developing nervous tissue. They are characterized as intracellular mediators of Semaphorin 3A signaling pathway, which is involved in axon differentiation during neural development.
The CRMP family includes five members; CRMP-1 to CRMP-5. All five isoforms share a significant similarity in sequence with liver dihydropyrimidinase (DHPase) and with each other. CRMP-1 to CRMP-4 share 75% identical sequence, while CRMP-5 shares 50% identity with the other CRMPs.
CRMP-1 is involved in cortical neuronal migration through reelin signaling. CRMP-1 inhibits the migration and invasion of non-small cell lung cancer (NSCLC). CRMP-1 includes a long form isoform, LCRMP-1, which promotes filopodia formation, cancer cell migration and invasion, resulting in poor clinical outcomes in NSCLC patients, therefore the long form is considered to be an invasion enhancer in NSCLC1-3.
Human CRMP-1 overall structure is very similar to mouse CRMP-1. The human protein generally comprises a heterotetrameric assembly with a randomly coiled link that connects the protomers to each other. The proteins can form homotetramers when purified from bovine brain. CRMPs contains a positively charged C-terminal region that is highly susceptible to proteolysis2,3.
Species reactivity key:
Anti-CRMP1 Antibody (#AIP-028) is a highly selective antibody directed against an epitope of the rat protein. The antibody can be used in western blot analysis. It has been designed to recognize CRMP-1 from human, mouse, and rat samples.