Recombinant Mouse Syndecan-3 Protein, CF Summary
Product Specifications
Ala45-Glu384, 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.
2734-SD
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 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-3
Syndecan-3, also called N-syndecan, is one of four vertebrate syndecans that are principal carriers of heparan sulfate and chondroitin sulfate glycosaminoglycans (GAGs) (1 - 3). These type 1 transmembrane proteins show conserved cytoplasmic domains and divergent extracellular domains (1 - 3). Human Syndecan-3 is synthesized as a 442 amino acid (aa) core protein with a 44 aa signal sequence, a 343 aa extracellular domain (ECD), a 21 aa transmembrane (TM) region and a 34 aa cytoplasmic tail with a binding site for PDZ domains (1). The ECD of mouse Syndecan-3 shares 95%, 83%, 82% and 81% aa identity with of rat, human, canine and bovine Syndecan-3, respectively. Syndecan-3 contains four conserved closely-spaced GAG attachment sites near the N‑terminus and unique threonine-rich and mucin-like sequences near the membrane (4). Addition of glycan side chains results in an apparent size of 120 ‑ 150 kDa. Non-covalent homodimerization of Syndecan-3 or, potentially, heterodimerization with Syndecan-2 or -4, is dependent on the transmembrane domain (5). A cleavage site near the TM domain allows shedding of soluble ECD; the remainder of the molecule undergoes regulated intramembrane proteolysis (6). Syndecan-3 is expressed in the nervous system and at limb buds during development (1, 2). It is expressed on neuronal axons and Schwann cell perinodal processes, promoting nerve cell migration and synapse formation (7, 8). Roles in memory and body weight regulation have been described (2, 9, 10). Through localization of growth factors such as FGF2, HGF and TGF-beta, it regulates expression of molecules important for differentiation of muscle and bone, such as myogenin, BMP-2 and hedgehog family members (1, 2, 11 ‑ 13). In adults, it is up‑regulated during regeneration, such as following myocardial infarction (14).
- Xian, X. et al. (2010) Cell Tissue Res. 339:31.
- Reizes, O. et al. (2008) Int. J. Biochem. Cell Biol. 40:28.
- Carey, D.J. et al. (1997) J. Biol. Chem. 272:2873.
- ENTREZ protein Accession # Q64519.
- Dews, I.C. and K.R. MacKenzie (2007) Proc. Natl. Acad. Sci. USA 104:20782.
- Schultz, J.G. et al. (2003) J. Biol. Chem. 278:48651.
- Hienola, A. et al. (2006) J. Cell Biol. 174:569.
- Goutebroze, L. et al. (2003) BMC Neurosci. 4:29.
- Kaksonen, M. et al. (2002) Mol. Cell. Neurosci. 21:158.
- Strader. A.D. et al. (2004) J. Clin. Invest. 114:1354.
- Cornelison, D.D.W. et al. (2004) Genes Dev. 18:2231.
- Fisher, M.C. et al. (2006) Matrix Biol. 25:27.
- Pacifici, M. et al. (2005) J. Bone Miner. Metab. 23:191.
- Finsen, A.V. et al. (2004) Physiol. Genomics 16:301.
Citation for Recombinant Mouse Syndecan-3 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: Mouse
Sample Types: Whole Cells
Applications: Bioassay
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