Recombinant Mouse Cadherin-4/R-Cadherin Protein, CF

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6677-CA-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Mouse Cadherin-4/R-Cadherin Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured by the ability of the immobilized protein to support the adhesion of A172 human glioblastoma cells (ATCC: CRL-1620). When 5 x 104 cells/well are added to Recombinant Mouse Cadherin‑4/R‑Cadherin coated plates, cell adhesion is enhanced in a dose dependent manner after 90 minutes at 37 °C. The ED50 for this effect is 0.4-2.0 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Cadherin-4/R-Cadherin protein
Met1-Ala731 with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
His21 & Asp167
Predicted Molecular Mass
78.5 & 62.5 kDa
SDS-PAGE
99 & 84 kDa, reducing conditions

Product Datasheets

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6677-CA

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

6677-CA

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 400 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: Cadherin-4/R-Cadherin

Cadherin‑4, also known as R‑Cadherin, is a 120‑140 kDa type I transmembrane 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). Mouse Cadherin‑4 is synthesized with a 20 amino acid (aa) signal peptide and a 146 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 22 aa transmembrane segment, and a 160 aa cytoplasmic domain (3, 4). Within the propeptide and ECD, mouse Cadherin‑4 shares 92% and 98% aa sequence identity with human and rat Cadherin‑4, respectively. Cadherin‑4 is expressed in epithelial cells, vascular smooth muscle cells, glial and neuronal cells, pancreatic beta ‑cells, thyroid follicular cells, and bone marrow Lin hematopoietic stem cells (4 ‑ 10). It interacts in cis to form homodimers as well as heterodimers with N‑Cadherin which function as adhesion multimers in trans-configuration (3, 11, 12). It is down‑regulated in invasive breast cancer but up‑regulated in rhabdomyosarcoma and has been shown to exert both positive and negative effects on cell migration and tumor cell invasiveness (5, 13, 14). Cadherin‑4 is involved in a variety of homing processes including guidance of the optic nerve and pioneer axons in early brain development, branching and guidance of the retinal vasculature, and targeting of hematopoietic stem cells to sites of ischemia (7, 10, 15, 16). Cadherin‑4 additionally binds to KLRG1, an inhibitory receptor expressed on NK cells (17).

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. Matsunami, H. et al. (1993) J. Cell Sci. 106:401.
  4. Hutton, J.C. et al. (1993) Mol. Endocrinol. 7:1151.
  5. Agiostratidou, G. et al. (2009) Cancer Res. 69:5030.
  6. Slater, S.C. et al. (2004) Arterioscler. Thromb. Vasc. Biol. 24:1204.
  7. Gerhardt, H. et al. (2000) Glia 31:131.
  8. Shibuya, Y. et al. (2005) Kobe J. Med. Sci. 51:35.
  9. Fagman, H. et al. (2003) Endocrinology 144:3618.
  10. Dorrell, M.I. et al. (2004) Blood 103:3420.
  11. Shan, W-S. et al. (2000) J. Cell Biol. 148:579.
  12. Murase, S. et al. (2000) Biochem. Biophys. Res. Commun. 276:1191.
  13. Kucharczak, J. et al. (2008) Cancer Res. 68:6559.
  14. Johnson, E. et al. (2004) J. Biol. Chem. 279:31041.
  15. Andrews, G.L. and G.S. Mastick (2003) J. Neurosci. 23:9873.
  16. Dorrell, M.I. et al. (2002) Invest. Ophthalmol. Vis. Sci. 43:3500.
  17. Ito, M. et al. (2006) J. Exp. Med. 203:289.
Entrez Gene IDs
1002 (Human); 12561 (Mouse); 311710 (Rat)
Alternate Names
CAD4; cadherin 4, type 1, preproprotein; cadherin 4, type 1, R-cadherin (retinal); Cadherin4; Cadherin-4; CDH4; FLJ22202; FLJ40547; MGC126700; MGC138355; RCAD; R-CAD; R-Cadherin; Retinal cadherin

Citation for Recombinant Mouse Cadherin-4/R-Cadherin Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. Secretomics reveals gelatinase substrates at the blood-brain barrier that are implicated in astroglial barrier function
    Authors: Burmeister, M;Fraunenstein, A;Kahms, M;Arends, L;Gerwien, H;Deshpande, T;Kuhlmann, T;Gross, CC;Naik, VN;Wiendl, H;Klingauf, J;Meissner, F;Sorokin, L;
    Science advances
    Species: Mouse
    Sample Types: Recombinant Protein
    Applications: Bioassay

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