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Recombinant Human CLEC3B/Tetranectin Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human CLEC3B/Tetranectin Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA.

When rhHGF (Catalog # 294-HGN) is immobilized at 5 µg/mL, the concentration of rhCLEC3B that produces 50% of the optimal binding response is found to be approximately 1‑5 μg/mL.

Source
Mouse myeloma cell line, NS0-derived human CLEC3B/Tetranectin protein
Glu22-Val202, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Glu22
Protein/Peptide Type
Recombinant Proteins
Gene
CLEC3B
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
21.0 kDa (monomer).
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
25 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 100 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 CLEC3B/Tetranectin Protein, CF

  • CLEC3B
  • C-type lectin domain family 3 member B
  • C-type lectin domain family 3, member B
  • DKFZp686H17246
  • Plasminogen kringle 4-binding protein
  • TETN
  • tetranectin (plasminogen binding protein)
  • Tetranectin
  • TNA
  • TNAtetranectin (plasminogen-binding protein)
  • TNtetranectin

Background

CLEC3B (C‑type lectin domain family 3 member B), also known as Tetranectin, is a 17 kDa O‑glycosylated member of the C‑type lectin superfamily (1, 2). Mature human CLEC3B consists of an alpha -helical coiled-coil region followed by one C‑type lectin domain (CTLD) (3, 4). It shares 81% amino acid sequence identity with mouse and rat CLEC3B. CLEC3B associates into non‑covalent homotrimers, although it was named Tetranectin based on the proposal that it formed tetramers (4, 5). CLEC3B is secreted by endocrine, epithelial, endothelial, and mesenchymal cells including several hematopoietic cell types (6, 7). It shows binding selectivity for heparan sulfate, fucoidan, and chondroitin sulfates A, B, and C (8). CLEC3B binds the Kringle domain-containing proteins Plasminogen, tPA, and HGF, and it enhances the tPA-mediated activation of Plasminogen (5, 9). It also reduces the ability of Angiostatin (a Plasminogen fragment) to inhibit vascular endothelial cell proliferation (10). In mouse, CLEC3B is involved in the development and repair of muscle, spine, and skin (11 - 13). CLEC3B is upregulated in stromal cells surrounding various tumors but not in the tumor cells themselves (3, 14 ‑ 16). It is concentrated in the extracellular matrix at the leading edge of malignant tumors, a pattern that overlaps that of Plasminogen (3, 14, 16).
  1. Zelensky, A.N. and J.E. Gready (2005) FEBS J. 272:6179.
  2. Jaquinod, M. et al. (1999) Biol. Chem. 380:1307.
  3. Wewer, U.M. and R. Albrechtsen (1992) Lab. Invest. 67:253.
  4. Nielsen, B.B. et al. (1997) FEBS Lett. 412:388.
  5. Clemmensen, I. et al. (1986) Eur. J. Biochem. 156:327.
  6. Christensen, L. and I. Clemmensen (1989) Histochemistry 92:29.
  7. Christensen, L. et al. (1987) Histochemistry 87:195.
  8. Clemmensen, I. (1989) Scand. J. Lab. Invest. 49:719.
  9. Westergaard, U.B. et al. (2003) Eur. J. Biochem. 270:1850.
  10. Mogues, T. et al. (2004) J. Biomed. Biotechnol. 2:73.
  11. Wewer, U. M. et al. (1998) Dev. Biol. 200:247.
  12. Iba, K. et al. (2001) Mol. Cell. Biol. 21:7817.
  13. Iba, K. et al. (2009) Wound Repair Regen. 17:108.
  14. Obrist, P. et al. (2004) J. Clin. Pathol. 57:417.
  15. Brunner, A. et al. (2007) Virchows Arch. 450:659.
  16. De Vries, T.J. et al. (1996) J. Pathol. 179:260.

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Bioinformatics

Gene Symbol CLEC3B
Uniprot