Recombinant Human Tenascin XB2 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Tenascin XB2 Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of Saos‑2 human osteosarcoma cells.

The ED50 for this effect is 0.5-2.0 μg/mL.

Optimal dilutions should be determined by each laboratory for each application.

Source
Chinese Hamster Ovary cell line, CHO-derived human Tenascin XB2 protein
Met1-Gly673, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Met1
Structure / Form
Monomer
Protein/Peptide Type
Recombinant Proteins
Gene
TNXB
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
74.8 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.
SDS-PAGE
80-95 kDa, reducing conditions

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 400 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 Human Tenascin XB2 Protein, CF

  • Tenascin XB2
  • TNXB2

Background

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).

  1. Hsia, H. and J.E. Schwarzbauer (2005) J. Biol. Chem. 280:26641.
  2. Bristow, J. et al. (1993) J. Cell Biol. 122:265.
  3. Speek, M. et al. (1996) Hum. Mol. Genet. 5:1749.
  4. Tee, M.K. et al. (1995) Genomics 28:171.
  5. Swiss-Prot accession P22105.
  6. Kato, A. et al. (2008) Exp. Cell Res. 314:2661.
  7. Endo, T. et al. (2009) Mol. Cell. Biochem. 320:53.
  8. Zweers, M. et al. (2004) Arthritis Rheum. 50:2742.
  9. Bristow, J. et al. (2005) Am. J. Med. Genet. C Semin. Med. Genet. 139C:24.
  10. Egging, D.F. et al. (2007) FEBS J. 274:1280.

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Bioinformatics

Gene Symbol TNXB
Uniprot