Recombinant Human Cadherin-4/R-Cadherin Fc Chimera, CF
Recombinant Human Cadherin-4/R-Cadherin Fc Chimera, CF Summary
Product Specifications
Human Cadherin-4 His21 - Ala734 (Leu347Trp) Accession # P55283.2 | IEGRMD | Human IgG1 (Pro100 - Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
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.
2217-CA
Formulation | Lyophilized from a 0.2 μm filtered solution in Tris-Citrate and NaCl. |
Reconstitution | Reconstitute at 100 μg/mL in sterile 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.
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Reconstitution Calculator
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 theN-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).
- Koch, A.W. et al. (2004) Cell. Mol. Life Sci. 61:1884.
- Angst, B.D. et al. (2001) J. Cell Sci. 114:629.
- Matsunami, H. et al. (1993) J. Cell Sci. 106:401.
- Shan, W-S. et al. (2000) J. Cell Biol. 148:579.
- Tanihara, H. et al. (1994) Cell Adhes. Commun. 2:15.
- Suzuki, S. et al. (1991) Cell Regul. 2:261.
- GenBank Accession # BAC03677.
- Slater, S.C. et al. (2004) Arterioscler. Thromb. Vasc. Biol. 24:1204.
- Hutton, J.C. et al. (1993) Mol. Endocrinol. 7:1151.
- Fagman, H. et al. (2003) Endocrinology 144:3618.
- Dorrell, M.I. et al. (2004) Blood 103:3420.
- Shibuya, Y. et al. (2005) Kobe J. Med. Sci. 51:35.
- Dorrell, M.I. et al. (2002) Invest. Ophthalmol. Vis. Sci. 43:3500.
- Murase, S. et al. (2000) Biochem. Biophys. Res. Commun. 276:1191.
- Ito, M. et al. (2006) J. Exp. Med. 203:289.
Citation for Recombinant Human Cadherin-4/R-Cadherin Fc Chimera, 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
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Distinct PTPmu-associated signaling molecules differentially regulate neurite outgrowth on E-, N-, and R-cadherin.
Authors: Oblander SA, Brady-Kalnay SM
Mol. Cell. Neurosci., 2010-03-01;44(1):78-93.
Species: Chicken
Sample Types: Whole Tissue
Applications: Bioassay
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