Mouse Testican 3/SPOCK3 Biotinylated Antibody Summary
Ala26-Ile436
Accession # Q8BKV0
Applications
Mouse Testican 3/SPOCK Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Testican 3/SPOCK3
Testican 3 encoded by the SPOCK3 gene is a proteoglycan expressed in brain (1). The human and mouse cDNAs predict 90% identity between the deduced amino acid sequences from the two species, indicating a conserved function (2, 3). Only the human protein, but not the mouse protein, has been characterized in the literature. Testican 3 contains Ca2+-binding domain and the C-terminal acidic domain with putative glycosaminoglycan attachment sites. In addition, it contains three potential inhibitory domains targeted toward three different classes of proteases, metallo, cysteine and serine proteases. The N-terminal region, which is unique to testicans, is responsible for the inhibition of Testican 3 towards MMP-14 (MT1-MMP, a metalloprotease) activation of MMP-2 (1). The thyropin domain and the follistatin-like domain with a six cysteine Kazal-like motif may inhibit cysteine and serine proteases, respectively (4). A spliced variant designated as N-Tes contains the N-terminal unique region, the follistatin-like domain and the Ca2+-binding domain, but lacks the C-terminal thyropin domain and the acidic domain (1). The purified rmTestican 3 is capable of inhibiting rhMMP-14 and rhCathepsin L (R&D Systems, Catalog # 918-MP and 952-CY) in assays using the fluorogenic peptide substrates (R&D Systems, Catalog # ES001 and ES008). As compared to rhTestican 1 (R&D Systems, Catalog # 2327-PI), the IC50 of rmTestican 3 is weaker toward rhCathepsin L and rhMMP-14 activity.
- Nakada, M. et al. (2001) Cancer Res. 61:8896.
- Strausberg, R.L. et al. (2002) Proc. Natl. Acad. Sci. USA 99:16899.
- Okazaki, Y. et al. (2002) Nature 420:563.
- Alliel, P.M. et al. (1993) Eur. J. Biochem. 214:347.
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