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 |
|
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
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).
- Zelensky, A.N. and J.E. Gready (2005) FEBS J. 272:6179.
- Jaquinod, M. et al. (1999) Biol. Chem. 380:1307.
- Wewer, U.M. and R. Albrechtsen (1992) Lab. Invest. 67:253.
- Nielsen, B.B. et al. (1997) FEBS Lett. 412:388.
- Clemmensen, I. et al. (1986) Eur. J. Biochem. 156:327.
- Christensen, L. and I. Clemmensen (1989) Histochemistry 92:29.
- Christensen, L. et al. (1987) Histochemistry 87:195.
- Clemmensen, I. (1989) Scand. J. Lab. Invest. 49:719.
- Westergaard, U.B. et al. (2003) Eur. J. Biochem. 270:1850.
- Mogues, T. et al. (2004) J. Biomed. Biotechnol. 2:73.
- Wewer, U. M. et al. (1998) Dev. Biol. 200:247.
- Iba, K. et al. (2001) Mol. Cell. Biol. 21:7817.
- Iba, K. et al. (2009) Wound Repair Regen. 17:108.
- Obrist, P. et al. (2004) J. Clin. Pathol. 57:417.
- Brunner, A. et al. (2007) Virchows Arch. 450:659.
- De Vries, T.J. et al. (1996) J. Pathol. 179:260.
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