Recombinant Mouse Syndecan-4 Protein, CF Summary
Product Specifications
1‑4 μg/mL.
Glu24-Val146, with a C-terminal 6-His tag
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.
6267-SD
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 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.
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Reconstitution Calculator
Background: Syndecan-4
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).
- Tkachenko, E. et al. (2005) Circ. Res. 96:488.
- Oh, E.-S, and J. R. Couchman (2004) Mol. Cells 17:181.
- David, G. et al. (1992) J. Cell Biol. 118:961.
- Tsuzuki, S. et al. (1997) J. Biochem. 122:17.
- Whiteford, J.R. and J.R. Couchman (2006) J. Biol. Chem. 281:32156.
- Choi, S. et al. (2005) J. Biol. Chem. 280:42573.
- Charnaux, N. et al. (2005) FEBS J. 272:1937.
- Schmidt, A. et al. (2005) J. Biol. Chem. 280:34441.
- Rauch, B. H. et al. (2005) J. Biol. Chem. 280:17507.
- Fitzgerald, M. L. et al. (2000) J. Cell Biol. 148:811.
- Ishiguro, K. et al. (2003) Glycoconj. J. 19:315.
- Echtermeyer, F. et al. (2001) J. Clin. Invest. 107:R9.
Citation for Recombinant Mouse Syndecan-4 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
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Identification of the growth cone as a probe and driver of neuronal migration in the injured brain
Authors: Nakajima, C;Sawada, M;Umeda, E;Takagi, Y;Nakashima, N;Kuboyama, K;Kaneko, N;Yamamoto, S;Nakamura, H;Shimada, N;Nakamura, K;Matsuno, K;Uesugi, S;Vep?ek, NA;Küllmer, F;Nasufovi?, V;Uchiyama, H;Nakada, M;Otsuka, Y;Ito, Y;Herranz-Pérez, V;García-Verdugo, JM;Ohno, N;Arndt, HD;Trauner, D;Tabata, Y;Igarashi, M;Sawamoto, K;
Nature communications
Species: Murine polyomavirus strain A3
Sample Types: Whole Cells
Applications: Bioassay
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