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Recombinant Human N-Cadherin His Protein

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-59927

Novus Biologicals, part of Bio-Techne
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NBP2-59927-250ug
NBP2-59927-50ug

Key Product Details

Source

Baculovirus

Tag

His

Conjugate

Unconjugated

Applications

SDS-PAGE

Product Specifications

Description

A recombinant protein with a C-Terminal His-tag and corresponding to the amino acids 160-724 of Human N-Cadherin

Source: Baculovirus

Amino Acid Sequence: ADPDWVIPPI NLPENSRGPF PQELVRIRSD RDKNLSLRYS VTGPGADQPP TGIFIINPIS GQLSVTKPLD REQIARFHLR AHAVDINGNQ VENPIDIVIN VIDMNDNRPE FLHQVWNGTV PEGSKPGTYV MTVTAIDADD PNALNGMLRY RIVSQAPSTP SPNMFTINNE TGDIITVAAG LDREKVQQYT LIIQATDMEG NPTYGLSNTA TAVITVTDVN DNPPEFTAMT FYGEVPENRV DIIVANLTVT DKDQPHTPAW NAVYRISGGD PTGRFAIQTD PNSNDGLVTV VKPIDFETNR MFVLTVAAEN QVPLAKGIQH PPQSTATVSV TVIDVNENPY FAPNPKIIRQ EEGLHAGTML TTFTAQDPDR YMQQNIRYTK LSDPANWLKI DPVNGQITTI AVLDRESPNV KNNIYNATFL ASDNGIPPMS GTGTLQIYLL DINDNAPQVL PQEAETCETP DPNSINITAL DYDIDPNAGP FAFDLPLSPV TIKRNWTITR LNGDFAQLNL KIKFLEAGIY EVPIIITDSG NPPKSNISIL RVKVCQCDSN GDCTDVDRIV GAGLGTGAHH HHHH

Purity

>90%, by SDS-PAGE

Endotoxin Level

< 1.0 EU per 1ug of protein (determined by LAL method)

Predicted Molecular Mass

62.9 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.

Protein / Peptide Type

Recombinant Protein

Scientific Data Images for Recombinant Human N-Cadherin His Protein

SDS-PAGE: Recombinant Human N-Cadherin His Protein [NBP2-59927]

SDS-PAGE: Recombinant Human N-Cadherin His Protein [NBP2-59927]

SDS-Page: Recombinant Human N-Cadherin Protein [NBP2-59927] - 15% SDS-PAGE

Formulation, Preparation and Storage

NBP2-59927
Formulation PBS (pH 7.4), 20% glycerol
Preservative No Preservative
Concentration 0.5 mg/ml
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.

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 Recombinant Human N-Cadherin His Protein

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Product Specific Notices for Recombinant Human N-Cadherin His Protein

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

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