Recombinant Human TIMP-3 Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Inhibition Activity

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Recombinant Human TIMP-3 Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit human MMP-2 cleavage of a fluorogenic peptide substrate Mca-PLGL-Dpa-AR-NH2 (Catalog # ES001). The IC50 value is approximately 3 nM, under conditions the described conditions.
Recombinant Human TIMP-3 is also an excellent inhibitor of human TACE (ADAM-17), with IC50 values measured in the low nM range.
Mouse myeloma cell line, NS0-derived human TIMP-3 protein
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Enzymes
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


Theoretical MW
22 kDa.
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.
26 kDa, reducing conditions
Read Publications using
973-TM in the following applications:

Packaging, Storage & Formulations

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 reconstitution.
Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile, deionized water.
Assay Procedure
  • Assay Buffer: 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% Brij-35 (v/v), pH 7.5 (TCNB)
  • Recombinant Human TIMP-3 (rhTIMP-3) (Catalog # 973-TM)
  • Recombinant Human MMP‑2 (rhMMP‑2) (Catalog # 902-MP)
  • 4-Aminophenylmercuric acetate (APMA), 100 mM stock in DMSO
  • Substrate: MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 ((Catalog # ES001) ), 2 mM stock in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhMMP-2 to 100 µg/mL in Assay Buffer.
  2. Activate 100 µg/mL rhMMP-2 with 1 mM APMA.
  3. Incubate at 37 °C for 1 hour.
  4. Prepare a curve of rhTIMP-3 (MW: 21,700 Da) in Assay Buffer. Make serial dilutions of: 5,000, 2,000, 1,000, 500, 300, 200, 150, 100, 20, and 2 nM.
  5. After activation, dilute 100 µg/mL rhMMP-2 to 12.5 µg/mL in Assay Buffer.
  6. Mix 16 µL of rhTIMP-3 curve dilutions, 25.6 µL of diluted rhMMP-2, and 118.4 µL of Assay Buffer.
  7. Include a control (in duplicate) containing Assay Buffer and the diluted rhMMP-2.
  8. Incubate reactions for 2 hours at 37 °C.
  9. After incubation, dilute the mixtures 5 fold in Assay Buffer.
  10. Dilute Substrate to 10 µM in Assay Buffer.
  11. Load 50 µL of the diluted incubated mixtures in a plate, and start the reaction by adding 50 µL of 10 µM Substrate.
  12. Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively in kinetic mode for 5 minutes.
  13. Derive the IC50 value for rhTIMP-3 from the curve.
  14. Calculate specific activity for each point using the following formula (if needed):

     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 MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).

Per Well:
  • rhMMP-2: 0.020 µg
  • Substrate: 5 µM


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human TIMP-3 Protein, CF

  • HSMRK222
  • K222
  • K222TA2
  • metalloproteinase inhibitor 3
  • MIG-5 protein
  • Protein MIG-5
  • pseudoinflammatory)
  • SFD
  • TIMP metallopeptidase inhibitor 3
  • TIMP3
  • TIMP-3
  • tissue inhibitor of metalloproteinase 3 (Sorsby fundus dystrophy
  • Tissue inhibitor of metalloproteinases 3


Tissue inhibitors of metalloproteinases (TIMPs) are a family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). There are four members of the family, TIMP-1, TIMP-2, TIMP-3 and TIMP-4. TIMP-3 is a glycoprotein with a molecular mass of 30 kDa produced by a wide range of cell types. TIMP-3 inhibits active MMP-mediated proteolysis by forming a non-covalent binary complex with the MMP active site through its N-terminal domain. In addition, TIMP-3 is the only known member of the TIMP family that is an effective inhibitor of ADAMs such as TACE (1).

TIMP-3 is unique among the TIMPs because of its high affinity for binding to the extracellular matrix (2). Point mutations in the TIMP-3 C-terminal domain have been reported to result in Sorsby's fundus dystrophy, a disease leading to macular degeneration and loss of vision.

  1. Amour, A. et al. (1998) FEBS Lett. 435:39.
  2. Leco, K.J. et al. (1994) J. Biol. Chem. 269:9352.

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Publications for TIMP-3 (973-TM)(20)

We have publications tested in 6 confirmed species: Human, Mouse, Rat, Chicken, Primate - Chlorocebus pygerythrus (Vervet Monkey), Rabbit.

We have publications tested in 4 applications: Bioassay, Cell Culture, Enzyme Assay, In Vivo.

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Cell Culture
Enzyme Assay
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Primate - Chlorocebus pygerythrus (Vervet Monkey)
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Showing Publications 1 - 10 of 20. Show All 20 Publications.
Publications using 973-TM Applications Species
J Mitlöhner, R Kaushik, H Niekisch, A Blondiaux, CE Gee, MFK Happel, E Gundelfing, A Dityatev, R Frischknec, C Seidenbech Dopamine Receptor Activation Modulates the Integrity of the Perisynaptic Extracellular Matrix at Excitatory Synapses Cells, 2020;9(2):. 2020 [PMID: 31972963] (Cell Culture, Rat) Cell Culture Rat
CW Su, YC Chang, MH Chien, YH Hsieh, MK Chen, CW Lin, SF Yang Loss of TIMP3 by promoter methylation of Sp1 binding site promotes oral cancer metastasis Cell Death Dis, 2019;10(11):793. 2019 [PMID: 31624299] (Cell Culture, Human) Cell Culture Human
MC Nielsen, MN Andersen, N Rittig, S Rødgaard-H, H Grønbaek, SK Moestrup, HJ Møller, A Etzerodt The macrophage-related biomarkers sCD163 and sCD206 are released by different shedding mechanisms J. Leukoc. Biol., 2019;0(0):. 2019 [PMID: 31242338] (Bioassay, Human) Bioassay Human
G Ruiz-Gómez, S Vogel, S Möller, MT Pisabarro, U Hempel Glycosaminoglycans influence enzyme activity of MMP2 and MMP2/TIMP3 complex formation - Insights at cellular and molecular level Sci Rep, 2019;9(1):4905. 2019 [PMID: 30894640] (Enzyme Assay, Human) Enzyme Assay Human
H Zhai, X Qi, Z Li, W Zhang, C Li, L Ji, K Xu, H Zhong TIMP?3 suppresses the proliferation and migration of SMCs from the aortic neck of atherosclerotic AAA in rabbits, via decreased MMP?2 and MMP?9 activity, and reduced TNF?? expression Mol Med Rep, 2018;18(2):2061-2067. 2018 [PMID: 29956789] (Bioassay, Rabbit) Bioassay Rabbit
JM Dave, T Mirabella, SD Weatherbee, DM Greif Pericyte ALK5/TIMP3 Axis Contributes to Endothelial Morphogenesis in the Developing Brain Dev. Cell, 2018;0(0):. 2018 [PMID: 29456135] (In Vivo, Mouse) In Vivo Mouse
Cathepsin Protease Controls Copper and Cisplatin Accumulation via Cleavage of the Ctr1 Metal-binding Ecto-domain J Biol Chem, 2016;0(0):. 2016 [PMID: 27143361] (Bioassay, Mouse) Bioassay Mouse
KK Wong, F Zhu, I Khatri, Q Huo, DE Spaner, RM Gorczynski Characterization of CD200 Ectodomain Shedding PLoS ONE, 2016;11(4):e0152073. 2016 [PMID: 27111430] (Bioassay, Human) Bioassay Human
Sanz R, Ferraro G, Fournier A IgLON cell adhesion molecules are shed from the cell surface of cortical neurons to promote neuronal growth. J Biol Chem, 2015;290(7):4330-42. 2015 [PMID: 25538237]
Uchikawa S, Yoda M, Tohmonda T, Kanaji A, Matsumoto M, Toyama Y, Horiuchi K ADAM17 regulates IL-1 signaling by selectively releasing IL-1 receptor type 2 from the cell surface. Cytokine, 2015;71(2):238-45. 2015 [PMID: 25461404] (Bioassay, Primate - Chlorocebus pygerythrus (Vervet Monkey)) Bioassay Primate - Chlorocebus pygerythrus (Vervet Monkey)
Show All 20 Publications.

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Gene Symbol TIMP3