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Recombinant Mouse Syndecan-4 Protein, CF

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Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Syndecan-4 Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of A431 human epithelial carcinoma cells. When 5 x 104 cells/well are added to mouse Syndecan-4 and human Fibronectin (0.5 μg/mL, Catalog # 1918-FN) coated plates, cell adhesion is enhanced in a dose dependent manner after 45 minutes at 37 °C. The ED50 for this effect is
1‑4 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Syndecan-4 protein
Glu24-Val146, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Glu24
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
14.3 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.
Publications
Read Publication using
6267-SD in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Syndecan-4 Protein, CF

  • Amphiglycan
  • MGC22217
  • Ryudocan core protein
  • Ryudocan
  • SDC4
  • SYND4ryudocan amphiglycan
  • syndecan 4 (amphiglycan, ryudocan)
  • syndecan 4
  • syndecan proteoglycan 4
  • Syndecan4
  • Syndecan-4

Background

Syndecan-4, previously known as amphiglycan or ryudocan, is a member of the syndecan family of type 1 transmembrane proteins capable of carrying heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans (1 ‑ 4). The four vertebrate syndecans have two conserved cytoplasmic domains and divergent extracellular portions, except for HS attachment sites. Syndecan-4 is the most similar to Syndecan-2, but is more universally expressed and is found in virtually every cell type. Expression can be up‑regulated by TGF-beta 2 and in response to mechanical stress in smooth muscle, wound healing, arterial injury or acute myocardial infarction, probably in response to at least one inflammatory mediator (1, 2). Mouse Syndecan-4 is synthesized as a 198 amino acid (aa) core protein with a 22 aa signal sequence, a 123 aa extracellular domain containing three consensus Ser-Gly sequences for the attachment of HS side chains and a conserved NXIP (X = any aa) cell adhesion site, a 25 aa transmembrane region and a 28 aa cytoplasmic tail (3 - 5). Mouse Syndecan-4 ECD shares approximately 79%, 91%, 79%, 77%, 77% and 75% aa identity with human, rat, canine, bovine, equine and porcine Syndecan-4 ECD, respectively. Addition of 20 - 80 disaccharides per side chain adds considerably to the size of the 20 kDa core protein. Non-covalent homodimerization of Syndecan-4 is dependent on the transmembrane domain (6). The HS chains can bind fibronectin, SDF-1, antithrombin, FGF-2, midkine and tissue factor pathway inhibitor and can present FGF-2 to its receptors (1, 2, 7). The NXIP site is critical for integrin-dependent binding of mesenchymal cells or vascular endothelium (5). Proteolytic cleavage by plasmin, thrombin or a metalloproteinase may create a functional ectodomain (8 - 10). Genetic disruption of the Syndecan-4 gene causes a mild phenotype, presumably due to compensation by other syndecans, but mice have an increase in placental thrombi as well as defects in wound healing and response to endotoxin shock (11, 12).

  1. Tkachenko, E. et al. (2005) Circ. Res. 96:488. 
  2. Oh, E.-S, and J. R. Couchman (2004) Mol. Cells 17:181.
  3. David, G. et al. (1992) J. Cell Biol. 118:961. 
  4. Tsuzuki, S. et al. (1997) J. Biochem. 122:17.
  5. Whiteford, J.R. and J.R. Couchman (2006) J. Biol. Chem. 281:32156.
  6. Choi, S. et al. (2005) J. Biol. Chem. 280:42573. 
  7. Charnaux, N. et al. (2005) FEBS J. 272:1937.  
  8. Schmidt, A. et al. (2005) J. Biol. Chem. 280:34441.
  9. Rauch, B. H. et al. (2005) J. Biol. Chem. 280:17507.
  10. Fitzgerald, M. L. et al. (2000) J. Cell Biol. 148:811.
  11. Ishiguro, K. et al. (2003) Glycoconj. J. 19:315.
  12. Echtermeyer, F. et al. (2001) J. Clin. Invest. 107:R9.

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