Recombinant Human Tenascin XB2 Protein, CF Summary
The ED50 for this effect is 0.5-2.0 μg/mL.
Optimal dilutions should be determined by each laboratory for each application.
Met1-Gly673, with a C-terminal 6-His tag
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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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 400 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.
Background: Tenascin XB2
Tenascin X (TNX) is a 450 kDa, 4266 amino acid (aa) extracellular matrix glycoprotein belonging to the tenascin family of adhesion proteins (1, 2). Tenascins are modular proteins containing heptad, EGF‑like and fibronectin type III repeats and a C‑terminal fibrinogen‑like domain (1 ‑ 3). The Tenascin XB2 form, also called XB‑S or XB‑short, is transcribed from a separate promoter, producing a 74 kDa protein that consists of the C‑terminal 673 aa of the full‑length TNX (3 ‑ 5). Of the TNX domains, Tenascin XB2 contains only the last 4 of ~32 fibronectin type III (FnIII) repeats and the C‑terminal fibrinogen‑like globular domain, along with some of the N‑glycosylation and serine phosphorylation sites (3 ‑ 5). Human Tenascin XB2 shares 84% aa sequence identity with corresponding regions of mouse and rat TNX. Tenascin XB2 is expressed mainly in the adrenal gland, with minor amounts of mRNA detected in the small intestine, lung and spleen (3, 6). It is also found in some human cell lines, such as MCF7, H1299 and HeLa, and can be induced by hypoxia in MCF‑7 cells (6, 7). In contrast, full‑length TNX is prominent in muscle and connective tissue, and deletion or mutation of TNX is one cause of human joint hypermobility syndromes such as the Ehlers‑Danlos syndrome (1 ‑ 3, 6, 8, 9). Tenascin XB2 lacks an RGD integrin binding site between FnIII 10 and 11, and decorin/collagen‑binding sites that include the EGF‑like repeats, but retains the collagen‑binding fibrinogen‑like domain and could conceivably interfere with collagen crosslinking and fibril formation (4, 9). However, a 75 kDa plasma form that overlaps with the sequence of Tenascin XB2 binds tropoelastin but not collagens (10). At least a portion of Tenascin XB2 is expressed in the cytoplasm and is co‑localized with the mitotic motor kinesin, Eg5, during interphase and mitosis (6, 7).
- Hsia, H. and J.E. Schwarzbauer (2005) J. Biol. Chem. 280:26641.
- Bristow, J. et al. (1993) J. Cell Biol. 122:265.
- Speek, M. et al. (1996) Hum. Mol. Genet. 5:1749.
- Tee, M.K. et al. (1995) Genomics 28:171.
- Swiss-Prot accession P22105.
- Kato, A. et al. (2008) Exp. Cell Res. 314:2661.
- Endo, T. et al. (2009) Mol. Cell. Biochem. 320:53.
- Zweers, M. et al. (2004) Arthritis Rheum. 50:2742.
- Bristow, J. et al. (2005) Am. J. Med. Genet. C Semin. Med. Genet. 139C:24.
- Egging, D.F. et al. (2007) FEBS J. 274:1280.
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