NCAM Protein Overview: Sequence, Structure, Function and Protein Interaction

NCAM Protein Overview

Great structural diversity in NCAM is due to transcriptional variations of a single gene and posttranslational mechanisms which are under exquisite developmental control (Rutishauser and Goridis, 1986). The neural cell adhesion molecule appears on early embryonic cells and is important in the formation of cell collectives and their boundaries at sites of morphogenesis. Later in development it is found on various differentiated tissues and is a major CAM mediating adhesion among neurons and between neurons and muscle.NCAM shares many features with immunoglobulins and is considered a member of the immunoglobulin superfamily. Cunningham et al. (1987) determined the structure of the 3 polypeptides of chicken NCAM; the chains are called ld, sd, and ssd. Lin et al. (1994) stated that there are cell adhesion molecules in invertebrates related to NCAM. Fasciclin II has been cloned in grasshoppers and Drosophila; apCAM has been identified in Aplysia. In these species, the NCAM analogs are members of the immunoglobulin superfamily both in structure (5 C2-type immunoglobulin domains followed by 2 fibronectin type 3 domains) and sequence. All of these molecules can mediate homophilic cell aggregation in vitro. Lin et al. (1994) used loss-of-function and gain-of-function mutants of fasciclin II in Drosophila to study the protein's function during growth cone guidance. The fasciclin II mutants had impaired fasciculation, but other aspects of outgrowth and directional guidance were intact, and thus genetically separate. NCAM is a membrane-bound glycoprotein that plays a role in cell-cell and cell-matrix adhesion through both its homophilic and heterophilic binding activity. To investigate the significance of this binding, Rabinowitz et al. (1996) used a gene targeting strategy in embryonic stem (ES) cells to replace the membrane-associated form of NCAM with a soluble, secreted form of its extracellular domain. Although the heterozygous mutant ES cells were able to generate low coat color chimeric mice, only the wildtype allele was transmitted, suggesting the possibility of dominant lethality. Analysis of chimeric embryos with a high level of ES cell contribution revealed severe growth retardation and morphologic defects by embryonic days 8.5-9.5. The second allele was also targeted and embryos derived almost entirely from the homozygous mutant ES cells exhibited the same lethal phenotype as observed with heterozygous chimeras. Rubinek et al. (2003) studied the role of pituicyte cell-cell contact mediated by CDH2 (114020) and NCAM1 in the regulation of GH (139250) secretion. RT-PCR showed CDH2 mRNA expression in 8 of 12 GH-secreting adenomas compared with 1 of 7 prolactin-cell adenomas. CDH2 and NCAM1 were similarly expressed in adenomas and in adult and fetal normal pituitary tissues. Cell adhesion molecule (CAM) stimulation increased GH secretion from pituitary fetal cultures by 40 to 60% and also from cultured GH adenoma cells by 40 to 75%. Disrupting CDH2 homophilic binding by anti-CDH2 antibody decreased fetal, but not tumorous, GH secretion by 40%. This study indicated that pituitary cell-cell contact mediated by homophilic interactions between adhesion molecules regulates human GH secretion.

NCAM protein name

Recommended name
Neural cell adhesion molecule 1
Short name
N-CAM-1||NCAM-1
Aliases
CD56, NCAM
Alternative name
CD_antigen: CD56

NCAM Gene family protein

NCAM Protein Sequence

Species Human NCAM protein
Length 858
Mass (Da) 94574
Sequence Human NCAM protein sequence
Species Mouse NCAM protein
Length 1115
Mass (Da) 119427
Sequence Mouse NCAM protein sequence
Species Rat NCAM protein
Length 858
Mass (Da) 94658
Sequence Rat NCAM protein sequence

NCAM Protein Molecular Weight & PI

Neural cell adhesion molecule 1 precursor (N-CAM-1) (NCAM-1) (CD56 antigen) Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 20-858 Neural cell adhesion molecule 1.

Molecular weight (Da)

92407.56

Theoretical pI

4.79

NCAM Protein Structure

Human NCAM, FN3 domains 1 and 2, M610R mutant
Deposited
2008-01-04   Released:  2008-02-26
Deposition Author(s)
Carafoli, F., Saffell, J.L., Hohenester, E.
Organism(s)
Homo sapiens
Expression System
Homo sapiens
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
2.7000 Å
R-Value Free
0.268
R-Value Work
0.223
2VKX From PDB

Human NCAM protein Secondary structure

NCAM Protein Interaction

Recombinant NCAM Protein Feature

NCAM Protein, Human, Recombinant (ECD, His Tag)

High Purity
> 95 % as determined by SDS-PAGE.
Low Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.

Recombinant NCAM protein citations

Title
Mobilization of human mesenchymal stem cells through different cytokines and growth factors after their immobilization by sulfur mustard
Year
2018
Author
Schreier, C;Rothmiller, S;Scherer, MA;Rummel, C;Steinritz, D;Thiermann, H;Schmidt, A;
Journal
Toxicol. Lett.
Title
Chemical proteomics tracks virus entry and uncovers NCAM1 as Zika virus receptor
Year
2020
Author
Srivastava, M;Zhang, Y;Chen, J;Sirohi, D;Miller, A;Zhang, Y;Chen, Z;Lu, H;Xu, J;Kuhn, RJ;Andy Tao, W;
Journal
Nat Commun

Bulk Order of Recombinant NCAM Protein

Please Leave Us a Message if you have any questions regarding bulk price quote of our products on the website, our customer specialist will get back to you in 24 hours by email.

Custom Recombinant Protein Production Service Features

  • Over 10 years' experience for 6000+ recombinant proteins production.
  • One-stop service from gene synthesis and vector construction to protein expression and purification.
  • Multiple protein expression systems: bacterial, yeast, baculovirus-insect and mammalian expression system.
  • Multiple purification systems (30+) to choose.
  • High R & D ability with over 1000 new proteins per year and quick problem-solving ability.
  • Close to 100 bioreactors with various volume between 2-1000 L to guarantee high-throughput and large-scale production.

Custom Recombinant Protein Production Service Advantages

  • High-efficiency expression vectors
  • High cell density culturing
  • Proprietary medium formulation
  • >6000 proteins expression and purification experience
  • High-efficiency expression vectors
  • High cell density culturing

Recombinant Protein Production Service Description

We offer one-stop services for recombinant protein production using our advanced protein expression platform technologies. Our full services include protein gene synthesis, protein codon optimization, protein expression vector design, large scale cell culture and fermentation, protein purification, and protein quality control testing. We offer significant cost saving advantages and record speed in protein expression and bulk production. We also have extensive experiences and expertise in handling various types of recombinant protein purification projects, with or without purification tags.