Recombinant Mouse Collagen XIII alpha 1 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Collagen XIII alpha 1 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 1 x 105 cells per well are added to rmCOL-13A1 coated plate (2 μg/mL, 100 μL/well), approximately 45%-75% will adhere after 1 hour at 37 °C. 

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

Source
Mouse myeloma cell line, NS0-derived mouse Collagen XIII alpha 1 protein
Glu107-Gln565, with an N-terminal 6-His tag
Accession #
N-terminal Sequence
His
Protein/Peptide Type
Recombinant Proteins
Gene
Col13a1
Purity
>80%, 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
46.0 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
50-60 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
>80%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 300 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 Collagen XIII alpha 1 Protein, CF

  • COL13A1
  • collagen alpha-1(XIII) chain
  • Collagen XIII alpha 1
  • collagen, type XIII, alpha 1
  • FLJ42485

Background

Collagen XIII alpha 1 is an 85 kDa - 95 kDa protein in the type 2 transmembrane collagen family (1). Mature mouse Collagen XIII alpha 1 consists of a 40 amino acid (aa) cytoplasmic domain, a 19 aa transmembrane segment, and a 692 aa extracellular domain (ECD). The ECD contains three collagenous regions separated by shorter non‑collagenous regions (2, 3). Within comparable regions of the ECD, mouse Collagen XIII alpha 1 shares 85% and 88% aa sequence identity with human and rat Collagen XIII alpha 1, respectively. Mouse Collagen XIII alpha 1 is extensively spliced, with some isoforms showing a tissue specific distribution (2, 4). Collagen XIII alpha 1 is widely expressed during development and in the adult (4, 5). It localizes to intercellular adherens junctions and cell-matrix focal adhesions (6, 7). Collagen XIII  alpha 1 assembles into disulfide-linked trimers, a process that is enhanced by proline hydroxylation (2, 8). Trimerization involves triple helix formation within the collagenous domains, although portions of the non‑collagenous regions can also form coiled coils (8 ‑ 10). The ECD of trimeric Collagen XIII alpha 1 is an extended rod-like structure with two flexible hinges that correspond to non‑collagenous regions (11). Collagen XIII alpha 1 clusters in cholesterol-rich domains on the plasma membrane (2, 12), and it can be cleaved from the cell surface or intracellularly by a furin-like protease (12). Collagen XIII alpha 1 binds the extracellular matrix molecules fibronectin, heparin, integrin  alpha 1, nidogen‑2, and perlecan (11, 13). The shed ECD retains its ability to bind fibronectin and can interfere with matrix formation (14).

 

  1. Franzke, C.-W. et al. (2005) J. Biol. Chem. 280:4005.
  2. Hagg, P. et al. (1998) J. Biol. Chem. 273:15590.
  3. Pihlajaniemi, T. and M. Tamminen, 1990, J. Biol. Chem. 265:16922.
  4. Peltonen, S. et al. (1997) DNA Cell Biol. 16:227.
  5. Sund, M. et al. (2001) Matrix Biol. 20:215.
  6. Peltonen, S. et al. (1999) J. Invest. Dermatol. 113:635.
  7. Hagg, P. et al. (2001) Matrix Biol. 19:727.
  8. Snellman, A. et al. (2000) J. Biol. Chem. 275:8936.
  9. Latvanlehto, A. et al. (2003) J. Biol. Chem. 278:37590.
  10. Snellman, A. et al. (2007) J. Biol. Chem. 282:14898.
  11. Tu, H. et al. (2002) J. Biol. Chem. 277:23092.
  12. Vaisanen, T. et al. (2006) J. Biol. Chem. 281:33352.
  13. Nykvist, P. et al. (2000) J. Biol. Chem. 275:8255.
  14. Vaisanen, M.-R. et al. (2006) Biochem. J. 393:43.

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Bioinformatics

Gene Symbol Col13a1
Uniprot