Recombinant Mouse OCAM/NCAM2 His-tag Protein, CF

Immobilized Recombinant Mouse OCAM/NCAM2 His-tag (Catalog # 10154-CM)supports the adhesion of T47D humanbreast cancer cells. The ED50 for this effect is 0.6-3.6 μg/mL.

2 μg/lane of Recombinant Mouse OCAM/NCAM2 His-tag(Catalog # 10154-CM) was resolved with SDS-PAGE under reducing (R) andnon-reducing (NR) conditions and visualized by Coomassie®Blue staining, showing bands at 95-110 kDa.

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse OCAM/NCAM2 His-tag Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of T47D human breast cancer cells. The ED₅₀ for this effect is 0.6-3.6 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse OCAM/NCAM2 protein
  Met1-Asn697, with a C-terminal 6-His tag
• Accession #: O35136
• N-terminal Sequence: Leu20
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 76.8 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 95-110 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse OCAM/NCAM2 His-tag Protein, CF

• NCAM2
• N-CAM-2
• NCAM-2
• NCAM21MGC51008
• neural cell adhesion molecule 2 precursor10
• neural cell adhesion molecule 2
• OCAM
• Rb-8
• RNCAM

Background

OCAM (olfactory cell adhesion molecule), also known as NCAM2 (neural cell adhesion molecule 2) and RNCAM (Rb‑8 neural cell adhesion molecule) is an approximately 100 kDa type I transmembrane glycoprotein belonging to the NCAM family within the immunoglobulin superfamily (1‑5). OCAM dimerizes and participates in homophilic adhesion, but unlike NCAM1/CD56, it is not polysialic acid‑glycosylated, and does not participate in heparin sulfate binding or heterophilic adhesion (2). The 837 amino acid (aa) form of human or mouse OCAM contains a 19 aa signal sequence, a 678 aa extracellular domain (ECD) with five Ig‑like C2‑type domains and two fibronectin type III domains, a transmembrane domain and a 119 aa cytoplasmic domain (2‑4). The first two Ig‑like domains mediate homodimer formation in trans (6). In mouse, a glycosyl phosphatidylinositol‑linked form may show differential expression and function on olfactory axons (1‑3, 7). The ECD of mouse OCAM shares 93%, 98% and 92% aa sequence identity with human, rat, and bovine OCAM, respectively. OCAM is expressed by a subset of axons in the olfactory, vomeronasal, and retrosplenial cortex in a zone‑specific manner (1‑3, 7‑9). It is thought to be important for organization of axons and dendrites and segregation of axodendritic and dendrodendritic synapses within glomeruli (1, 7, 10, 11). Because OCAM is encoded on chromosome 21 in humans, it is implicated in neurological abnormalities in Down Syndrome (trisomy 21) (1, 3, 4). It may also be implicated in development of autism and Alzheimer's disease, and over‑expressed in some breast and prostate cancers (1, 5).

1. Winther, M. et al. (2012) Int. J. Biochem. Cell Biol. 44:441.
2. Yoshihara, Y. et al. (1997) J. Neurosci. 17:5930.
3. Alenius, M. and S. Bohm (1997) J. Biol. Chem. 272:26083.
4. Paoloni-Giacobino, A. et al. (1997) Genomics 43:43.
5. Takahashi, S. et al. (2011) Cancer Sci. 102:808.
6. Kulahin, N. et al. (2011) Structure 19:203.
7. Alenius, M. and S. Bohm (2003) Development 130:917.
8. von Campenhausen, H. et al. (1997) Neuroreport 8:2607.
9. Ichinohe, N. et al. (2003) Eur. J. Neurosci. 18:1764.
10. Walz, A. et al. (2006) Mol. Cell. Neurosci. 32:1.
11. Borisovska, M. et al. (2011) J. Physiol. 589:1927.

Bioinformatics

• Uniprot:
  • O35136()