Human N-Cadherin Alexa Fluor® 700-conjugated Antibody

Catalog #: FAB13881N Datasheet / COA / SDS
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FAB13881N-100UG
R&D Systems Antibodies
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Human N-Cadherin Alexa Fluor® 700-conjugated Antibody Summary

Species Reactivity
Human
Specificity
Detects mouse N-Cadherin in direct ELISAs and Western blots. In direct ELISAs approximately 50% cross-reactivity with recombinant mouse N-Cadherin is observed, and no cross-reactivity with recombinant human (rh) E-Cadherin, rhP-Cadherin, rhVE-Cadherin, rhCadherin-4, -8, -11, -12, or -13 is observed.
Source
Monoclonal Mouse IgM Clone # 691723
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse N-Cadherin
Asp160-Ala724
Accession # P19022.4
Formulation
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
Label
Alexa Fluor 700 (Excitation= 675-700 nm, Emission= 723 nm)

Applications

Recommended Concentration
Sample
Flow Cytometry
0.25-1 µg/106 cells
HeLa human cervical epithelial carcinoma cell line

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

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Preparation and Storage

Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.

Background: N-Cadherin

Neuronal Cadherin (N-Cadherin or NCAD), also known as Cadherin-2 (CDH2), is a 130 kDa type I membrane protein belonging to the Cadherin superfamily of calcium-dependent adhesion molecules. Cadherins are involved in multiple processes including embryonic development, cell migration, and maintenance of epithelial integrity (1, 2). Human N‑Cadherin is synthesized with a 25 amino acid (aa) signal peptide and a 134 aa N‑terminal propeptide. The mature cell surface‑expressed protein consists of a 565 amino acid (aa) extracellular domain (ECD) that contains five Cadherin repeats, a 21 aa transmembrane segment, and a 161 aa cytoplasmic domain (3). Within the ECD, human N-Cadherin shares 98% aa sequence identity with mouse and rat N-Cadherin. In the nervous system, N-Cadherin mediates adhesion between the opposing faces of developing neuronal synapses and between Schwann cells and neuronal axons (4, 5). It interacts in cis or in trans homophilically and with the GluR2 subunit of neuronal AMPA receptors (1, 6). During synaptic maturation, its expression is lost from inhibitory terminals but maintained at excitatory terminals (5). ADAM10-mediated shedding of the N-Cadherin ECD alters cell-cell adhesion, synaptic development, and AMPA receptor activity (7, 8). N-Cadherin can also be cleaved at multiple additional sites within the intracellular or extracellular domains by Calpain, gamma ‑Secretase, and several MMPs (9 - 13). Cleavage of N‑Cadherin in atherosclerotic plaques contributes alternatively to vascular smooth muscle cell proliferation (MMP-9 and -12) or apoptosis (MMP‑7) (12, 13). Aberrant cell surface expression of the pro and mature forms of N-Cadherin in cancer results in increased tumor progression and invasiveness (14, 15). N-Cadherin also mediates the adhesion between hematopoeitic progenitor cells and mesenchymal stromal cells of the bone marrow (16).

References
  1. Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
  2. Gumbiner, B.M. (2005) Nat. Rev. Mol. Cell Biol. 6:622.
  3. Reid, R.A. and J.J. Hemperly (1990) Nucleic Acids Res. 18:5896.
  4. Wanner, I.B. and P.M. Wood (2002) J. Neurosci. 22:4066.
  5. Benson, D.L. and H. Tanaka (1998) J. Neurosci. 18:6892.
  6. Saglietti, L. et al. (2007) Neuron 54:461.
  7. Reiss, K. et al. (2005) EMBO J. 24:742.
  8. Malinverno, M. et al. (2010) J. Neurosci. 30:16343.
  9. Jang, Y.-N. et al. (2009) J. Neurosci. 29:5974.
  10. Uemura, K. et al. (2006) Neurosci. Lett. 402:278.
  11. Hartland, S.N. et al. (2009) Liver Int. 29:966.
  12. Williams, H. et al. (2010) Cardiovasc. Res. 87:137.
  13. Dwivedi, A. et al. (2009) Cardiovasc. Res. 81:178.
  14. Maret, D. et al. (2010) Neoplasia 12:1066.
  15. Tanaka, H. et al. (2010) Nat. Med. 16:1414.
  16. Wein, F. et al. (2010) Stem Cell Res. 4:129.
Long Name
Neural Cadherin
Entrez Gene IDs
1000 (Human); 12558 (Mouse); 83501 (Rat)
Alternate Names
ACOGS; ARVD14; cadherin 2, type 1, N-cadherin (neuronal); Cadherin-2; calcium-dependent adhesion protein, neuronal; CD325 antigen; CD325; CDH2; CDHN; CDw325; NCAD; N-cadherin 1; NCadherin; N-Cadherin; Neural cadherin; neural-cadherin

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Product Specific Notices


This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.

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