N-Cadherin Antibody [Janelia Fluor® 646]

Name: N-Cadherin Antibody [Janelia Fluor® 646]
Brand: Novus Biologicals
SKU: AF1388J
Price: 609 USD
Availability: InStock

Novus Biologicals | Catalog # AF1388J

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Product Specifications
Applications
Preparation & Storage
Background
Product Documents
Specific Notices
Research Areas

Key Product Details

Species Reactivity

Human

Applications

Immunohistochemistry, Western Blot

Label

Janelia Fluor 646

Antibody Source

Polyclonal Sheep IgG

View all N-Cadherin Primary Antibodies »

Product Specifications

Immunogen

E. coli-derived recombinant human N-Cadherin Propeptide
Ser26-Arg159
Accession # P19022

Specificity

Detects human N-Cadherin Propeptide in direct ELISAs and Western blots. In direct ELISAs, less than 5% cross-reactivity with recombinant human (rh) Cadherin-8, rhCadherin-11, and rhR-Cadherin is observed.

Clonality

Polyclonal

Host

Sheep

Isotype

IgG

Applications for N-Cadherin Antibody [Janelia Fluor® 646]

Application

Recommended Usage

Immunohistochemistry

Optimal dilutions of this antibody should be experimentally determined.

Western Blot

Optimal dilutions of this antibody should be experimentally determined.

Application Notes

Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Purification

Antigen Affinity-purified

Formulation

50mM Sodium Borate

Preservative

0.05% Sodium Azide

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C in the dark.

Background: N-Cadherin

N-Cadherin, also referred to as Neural Cadherin (NCAD) or Cadherin-2 (CHD2), is a 130 kDa protein that is a member of the calcium-dependent adhesion molecule family of classical (type I) cadherins (1-4). Under the CDH2 gene, human N-cadherin is synthesized as a 906 amino acid protein with a theoretical molecular weight of 99.8 kDa (5). The N-cadherin protein structure is similar to other classical type I cadherins including epithelial (E-) cadherin and placental (P-) cadherin (1,2). N-cadherin consists of a 25 amino acid (aa) N-terminal signal peptide and 134 aa pro-peptide, a 565 aa extracellular domain (ECD) with five cadherin repeats, a 21 aa transmembrane segment, and a 161 aa cytoplasmic domain (1-3,5). The ECD of N-cadherin monomers is responsible for homotypic binding through either cis or trans adhesion (2,3).

N-cadherin is expressed on multiple cell types but is most highly expressed by mesenchymal cells and neural tissue (2). Functionally, N-cadherin has a number of roles including maintaining structural integrity and adhesion, cell signaling, and formation of neuronal synapses and the vascular wall (2). The cytoplasmic tail interacts with beta-catenin which then binds with alpha-catenin, forming the cadherin-catenin adhesion complex, an important component of adhesions junctions (1-3). Given its role in adhesion, N-cadherin serves as an indicator of epithelial-to-mesenchymal transition (EMT) (1-4). The loss of E-cadherin during EMT corresponds with an increase in N-cadherin expression (1-4). This "cadherin-switch" is associated with increased migratory and invasive behavior observed in tumor progress (1-4). Proteases including activity of a disintegrin and metalloprotease 10 (ADAM10), matrix metalloproteinases (MMPs), caspase 3, presenilin, and calpain can cleave N-cadherin as a mechanism for regulating Wnt/beta-catenin signaling and inducing oncogenic signals (3,4). In addition to its expression in solid tumors, N-cadherin has been indicated in hematological disorders such as leukemia and multiple myeloma (1). N-cadherin antagonists are currently being studied as potential therapeutics for a variety of cancer studies (1-2).

References

1. Mrozik, K. M., Blaschuk, O. W., Cheong, C. M., Zannettino, A., & Vandyke, K. (2018). N-cadherin in cancer metastasis, its emerging role in haematological malignancies and potential as a therapeutic target in cancer. BMC Cancer. https://doi.org/10.1186/s12885-018-4845-0

2. Loh, C. Y., Chai, J. Y., Tang, T. F., Wong, W. F., Sethi, G., Shanmugam, M. K., Chong, P. P., & Looi, C. Y. (2019). The E-Cadherin and N-Cadherin Switch in Epithelial-to-Mesenchymal Transition: Signaling, Therapeutic Implications, and Challenges. Cells. https://doi.org/10.3390/cells8101118

3. Derycke, L. D., & Bracke, M. E. (2004). N-cadherin in the spotlight of cell-cell adhesion, differentiation, embryogenesis, invasion and signalling. The International Journal of Developmental Biology. https://doi.org/10.1387/ijdb.041793ld

4. Yu, W., Yang, L., Li, T., & Zhang, Y. (2019). Cadherin Signaling in Cancer: Its Functions and Role as a Therapeutic Target. Frontiers in Oncology. https://doi.org/10.3389/fonc.2019.00989

5. Unitprot (P1903)

Long Name

Neural Cadherin

Alternate Names

Cadherin-2, CD325, CDH2, NCadherin

Gene Symbol

CDH2

Additional N-Cadherin Products

Product Documents for N-Cadherin Antibody [Janelia Fluor® 646]

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Product Specific Notices for N-Cadherin Antibody [Janelia Fluor® 646]

Sold under license from the Howard Hughes Medical Institute, Janelia Research Campus.

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.