Recombinant Mouse Matriptase/ST14 Catalytic Domain, CF

Catalog # Availability Size / Price Qty
4735-SE-010
R&D Systems Recombinant Proteins and Enzymes
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Citations (4)
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Recombinant Mouse Matriptase/ST14 Catalytic Domain, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to cleave the fluorogenic peptide substrate Boc-QAR-AMC (Catalog # ES014). The specific activity is >4,000 pmol/min/µg, as measured under the described conditions.
Source
E. coli-derived mouse Matriptase/ST14 protein
Gly596-Val855, with an N-terminal Met and 6-His tag
The protein was auto-activated and further purified.
Accession #
N-terminal Sequence
Analysis
Met & Val615
Predicted Molecular Mass
3 kDa & 26 kDa
SDS-PAGE
27 kDa (major) and minor auto-activation fragments, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

4735-SE

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.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Assay Procedure

Materials
  • 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
  1. Dilute rmMatriptase to 0.2 ng/µL in Assay Buffer.
  2. Dilute Substrate to 50 µM in Assay Buffer.
  3. 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.
  4. Read at excitation and emission wavelengths of 380 nm and 460 nm, respectively, in kinetic mode for 5 minutes.
  5. 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
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Matriptase/ST14

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).

References
  1. Cho, E. et al. (2001) J. Biol. Chem. 276:44581.
  2. List, K. et al. (2006) Mol. Med. 12:1.
  3. Uhland, K. (2006) Cell Mol. Life Sci. 63:2968.
Entrez Gene IDs
6768 (Human); 19143 (Mouse); 114093 (Rat)
Alternate Names
EC 3.4.21; Epithin; HAI; Matriptase; Membrane-type serine protease 1; MTSP1; MT-SP1EC 3.4.21.109; prostamin; PRSS14; Serine protease 14; Serine protease TADG-15; SNC19; SNC19MTSP1; ST14; suppression of tumorigenicity 14 (colon carcinoma); suppression of tumorigenicity 14 (colon carcinoma, matriptase, epithin); suppressor of tumorigenicity 14 protein; TADG15; TADG-15; TMPRSS14; tumor associated differentially expressed gene 15 protein; Tumor-associated differentially-expressed gene 15 protein

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.

4 Citations: Showing 1 - 4
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  1. Matriptase Cleaves EpCAM and TROP2 in Keratinocytes, Destabilizing Both Proteins and Associated Claudins
    Authors: CJ Wu, M Lu, X Feng, G Nakato, MC Udey
    Cells, 2020;9(4):.
    Species: N/A
    Sample Types: Recombinant Protein
    Applications: Bioassay
  2. 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):.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  3. 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.
    Species: Mouse
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay
  4. 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.
    Species: N/A
    Sample Types: N/A
    Applications: Western Blot

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Fluorogenic Peptide Substrates

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Recombinant Mouse Matriptase/ST14 Catalytic Domain, CF
By Anonymous on 11/03/2016
Application: In vitro bioactivity in cell culture