Recombinant Mouse Matriptase/ST14 Catalytic Domain, CF Summary
Gly596-Val855, with an N-terminal Met and 6-His tag
The protein was auto-activated and further purified.
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Supplied as a 0.2 μm filtered solution in Tris and Glycerol.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- Assay Buffer: 50 mM Tris, 50 mM NaCl, 0.01% (v/v) Tween® 20, pH 9.0
- Recombinant Mouse Matriptase/ST14 Catalytic Domain (rmMatriptase) (Catalog # 4735-SE)
- Substrate: BOC-Gln-Ala-Arg-AMC (Catalog # ES014)
- F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
- Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
- Dilute rmMatriptase to 0.2 ng/µL in Assay Buffer.
- Dilute Substrate to 50 µM in Assay Buffer.
- Load into a plate 50 µL of 0.2 ng/µL rmMatriptase, and start the reaction by adding 50 µL of 50 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 50 µM Substrate.
- Read at excitation and emission wavelengths of 380 nm and 460 nm, respectively, in kinetic mode for 5 minutes.
- Calculate specific activity:
Specific Activity (pmol/min/µg) =
|Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)|
|amount of enzyme (µg)|
*Adjusted for Substrate Blank
**Derived using calibration standard 7-Amino, 4-Methyl Coumarin (Sigma, Catalog # A9891).Per Well:
- rmMatriptase: 0.010 µg
- Substrate: 25 µM
Matriptase, a mouse type II membrane serine protease encoded by the ST14 (suppression of tumorigenicity 14) gene, is also known as epithin, and membrane-type serine protease 1/MT-SP1 (1-2). Its human ortholog MT-SP1/Matriptase (Catalog # 3946-SE), which shares 81% amino acid identity with epithin, has been thought to play an important role in tumor biology and is a potential target for anti-cancer therapy (3). Matriptase has a multidomain structure containing a putative N-terminal transmembrane region, two CUB domains, four LDLRA repeats, and a C-terminal serine protease domain (1). The protease domain of epithin starts with Val615. R&D Systems recombinant mouse Matriptase is an active protease and consists of the catalytic domain (Val615 to Val855) and a short peptide (Gly596 to Arg614).
- Cho, E. et al. (2001) J. Biol. Chem. 276:44581.
- List, K. et al. (2006) Mol. Med. 12:1.
- Uhland, K. (2006) Cell Mol. Life Sci. 63:2968.
Citations for Recombinant Mouse Matriptase/ST14 Catalytic Domain, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 5
Filter your results:
Matriptase Cleaves EpCAM and TROP2 in Keratinocytes, Destabilizing Both Proteins and Associated Claudins
Authors: CJ Wu, M Lu, X Feng, G Nakato, MC Udey
Sample Types: Recombinant Protein
Proteolytic Cleavage of Podocin by Matriptase Exacerbates Podocyte Injury
Authors: S Ozawa, M Matsubayas, H Nanaura, M Yanagita, K Mori, K Asanuma, N Kajiwara, K Hayashi, H Ohashi, M Kasahara, H Yokoi, H Kataoka, E Mori, T Nakagawa
J. Biol. Chem., 2020;0(0):.
Sample Types: Cell Lysates
Structure-activity relationship studies of dipeptide-based hepsin inhibitors with Arg bioisosteres
Authors: H Kwon, H Ha, H Jeon, J Jang, SH Son, K Lee, SK Park, Y Byun
Bioorganic chemistry, 2020;0(0):104521.
Sample Types: Peptide
Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type I serine proteases from transmembrane anchors.
Authors: Raman K, Trivedi N, Raymond W, Ganesan R, Kirchhofer D, Verghese G, Craik C, Schneider E, Nimishakavi S, Caughey G
J Biol Chem, 2013;288(15):10588-98.
Sample Types: Recombinant Protein
Applications: Enzyme Assay
Loss of matriptase suppression underlies spint1 mutation-associated ichthyosis and postnatal lethality.
Authors: Szabo R, Kosa P, List K, Bugge TH
Am. J. Pathol., 2009;174(6):2015-22.
Sample Types: N/A
Applications: Western Blot
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Fluorogenic Peptide Substrates
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