Human Cadherin-4/R-Cadherin Antibody

Catalog # Availability Size / Price Qty
AF2217
AF2217-SP
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Human Cadherin-4/R-Cadherin Antibody Summary

Species Reactivity
Human
Specificity
Detects human Cadherin‑4/R‑Cadherin in direct ELISAs and Western blots. In direct ELISAs and Western blots, less than 5% cross-reactivity with recombinant human (rh) N-Cadherin is observed and less than 1% cross-reactivity with rhCadherin-8, rhCadherin-11, rhCadherin-12, rhCadherin-17, rhE-Cadherin, rhP-Cadherin, and rhVE-Cadherin is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human Cadherin‑4/R‑Cadherin
His21-Ala734 (Lys347Trp)
Accession # P55283
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human Cadherin‑4/R-Cadherin Fc Chimera (Catalog # 2217-CA)

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

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store 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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Cadherin-4/R-Cadherin

The cadherin superfamily is a large family of membrane-associated glycoproteins that engage in both homo- and heterotypic, calcium-dependent, cell-cell adhesion events. The superfamily can be divided into at least four subfamilies based on its member’s extracellular (EC) regions and cytoplasmic domains (1, 2). These include classical cadherins, desmosomal cadherins, protocadherins, and cadherin-like molecules that contain a variable number of EC and transmembrane (TM) domains (1). Cadherin-4, also known as R-Cadherin, is a classical cadherin of 120‑140 kDa (3, 4). Human Cadherin-4 is synthesized as a 916 amino acid (aa) type I transmembrane glycoprotein that contains a 20 aa signal peptide, a 149 aa prosequence, a 565 aa extracellular region (EC), a 22 aa transmembrane segment, and a 160 aa cytoplasmic domain (5, 6). There are five EC cadherin domains that are approximately 110 aa in length. This pattern is consistent with classical cadherin family molecules that are modular in their extracellular region and mediate calcium-dependent cell-cell adhesion through their Ca++-binding repeats (2). One potential Cadherin-4 splice variant involves the preprosegment and shows 32 aa substitution for the N-terminal 124 amino of the full-length precursor (7). The extracellular region of human Cadherin-4 is 96% aa identical to mouse Cadherin-4 extracellular region (3). Cadherin-4 is expressed in vascular smooth muscle (8), pancreatic beta -cells (9), thyroid follicular cells (10), bone marrow Lin- HSCs (11), sensory neurons of the dorsal root ganglia (12), and, possibly, astrocytes and endothelium of the retina (13). As a classic cadherin, Cadherin-4 will form both homodimers and heterodimers with N-cadherin (4, 14). These complexes translate into adhesion multimers in cis‑ and trans-configurations. Such structures serve to both unite adjacent cells, and provide guidance for migrating cells/processes (13). Additionally, R-Cadherin is associated with cell quiescence, as a loss of cell Cadherin-4 expression is correlated with cell proliferation (8). Finally, R-Cadherin is reported to bind to KLRG1 (killer cell lectin-like receptor G1). This inactivates NK cell cytotoxicity, and provides protection for R-Cadherin expressing cells (15).

References
  1. Koch, A.W. et al. (2004) Cell. Mol. Life Sci. 61:1884.
  2. Angst, B.D. et al. (2001) J. Cell Sci. 114:629.
  3. Matsunami, H. et al. (1993) J. Cell Sci. 106:401.
  4. Shan, W-S. et al. (2000) J. Cell Biol. 148:579.
  5. Tanihara, H. et al. (1994) Cell Adhes. Commun. 2:15.
  6. Suzuki, S. et al. (1991) Cell Regul. 2:261.
  7. GenBank Accession # BAC03677.
  8. Slater, S.C. et al. (2004) Arterioscler. Thromb. Vasc. Biol. 24:1204.
  9. Hutton, J.C. et al. (1993) Mol. Endocrinol. 7:1151.
  10. Fagman, H. et al. (2003) Endocrinology 144:3618.
  11. Dorrell, M.I. et al. (2004) Blood 103:3420.
  12. Shibuya, Y. et al. (2005) Kobe J. Med. Sci. 51:35.
  13. Dorrell, M.I. et al. (2002) Invest. Ophthalmol. Vis. Sci. 43:3500.
  14. Murase, S. et al. (2000) Biochem. Biophys. Res. Commun. 276:1191.
  15. 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

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