N-Cadherin Antibody (CL3716) Summary
Immunogen |
This N-Cadherin Antibody (CL3716) was developed against a recombinant protein corresponding to amino acids: NSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDP. |
Epitope |
ENPYFAPNPK |
Predicted Species |
Mouse (99%), Rat (99%). Backed by our 100% Guarantee. |
Isotype |
IgG1 |
Clonality |
Monoclonal |
Host |
Mouse |
Gene |
CDH2 |
Purity |
Protein A purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Immunocytochemistry/Immunofluorescence 2-10 ug/ml
- Immunohistochemistry 1:500 - 1:1000
- Immunohistochemistry-Paraffin 1:500 - 1:1000
- Knockdown Validated
- Western Blot 1 ug/ml
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Application Notes |
For IHC-Paraffin, HIER pH 6 retrieval is recommended. For ICC/IF, PFA/Triton X-100 is recommended for fixation/permeabilization. |
Theoretical MW |
100 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. |
Control Peptide |
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Reactivity Notes
Please note that this antibody is reactive to Mouse and derived from the same host, Mouse. Mouse-On-Mouse blocking reagent may be needed for IHC and ICC experiments to reduce high background signal. You can find these reagents under catalog numbers PK-2200-NB and MP-2400-NB. Please contact Technical Support if you have any questions.
Packaging, Storage & Formulations
Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
Buffer |
PBS (pH 7.2) and 40% Glycerol |
Preservative |
0.02% Sodium Azide |
Purity |
Protein A purified |
Alternate Names for N-Cadherin Antibody (CL3716)
Background
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)
Limitations
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.
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Product General Protocols
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FAQs for N-Cadherin Antibody (NBP2-61632) (0)
Secondary Antibodies
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