Recombinant Human TIMP-1 Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human TIMP-1 Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
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 2.5 nM as measured under the described conditions. 
Mouse myeloma cell line, NS0-derived human TIMP-1 protein
Accession #
N-terminal Sequence
Predicted Molecular Mass
21 kDa
28-30 kDa, reducing conditions

Product Datasheets

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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.


Formulation Lyophilized from a 0.2 μm filtered solution in Sodium Acetate and NaCl.
Reconstitution Reconstitute at 100 μg/mL in sterile, deionized water.
Shipping The product is shipped at ambient temperature. 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 reconstitution.

Assay Procedure

  • Assay Buffer: 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% Brij-35 (w/v), pH 7.5 (TCNB)
  • Recombinant Human TIMP-1 (rhTIMP-1) (Catalog # 970-TM)
  • Recombinant Human MMP‑2 (rhMMP‑2) (Catalog # 902-MP)
  • p-aminophenylmercuric acetate (APMA), (Sigma, Catalog # A-9563), 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. Activate rhMMP-2 at 100 µg/mL with 1 mM of APMA at final concentration respectively, in Assay Buffer.
  2. Incubate activation of rhMMP-2 at 37°C for 1 hour.
  3. Prepare a curve of rhTIMP-1 (MW: 20,695 Da). Make the following serial dilutions in Assay Buffer: 2000 nM, 1,000 nM, 500 nM, 300 nM, 200 nM, 150 nM, 100 nM, 20 nM, and 2 nM.
  4. Dilute activated 100 µg/mL rhMMP-2 to 12.8 µg/mL in Assay Buffer.
  5. Mix 25 µL of 12.8 µg/mL rhMMP-2, 16 µL of rhTIMP-1 serial curve dilutions, and 119 µL of Assay Buffer in micro-tubes.
  6. Include two enzyme controls of 25 µL of 12.8 µg/mL rhMMP-2 and 135 mL Assay Buffer in micro-tubes.
  7. Incubate reaction mixtures at 37 °C for 2 hours.
  8. Dilute incubated reaction mixtures by a 5-fold dilution in Assay Buffer.
  9. Dilute Substrate to 10 µM in Assay Buffer.
  10. In a plate load 50 µL of 5-fold diluted incubated reaction mixtures to wells.
  11. Start the reaction by adding 50 µL of 10 µM Substrate to wells.
  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 of rhTIMP-1 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: 0.02 µg
  • rhTIMP-1 curve: 20 nM, 10 nM, 5 nM, 3 nM, 2 nM, 1.5 nM, 1.0 nM, 0.2 nM, 0.02 nM, and 0 nM
  • Substrate: 5 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.


Background: TIMP-1

Tissue inhibitors of metalloproteinases or 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-1 is a glycoprotein with a molecular mass of 28 kDa produced by a wide range of cell types. TIMP-1 inhibits active MMP-mediated proteolysis by forming an N-terminal, non-covalent binary complex with the MMP active site. TIMP-1 also associates C-terminally with Pro-MMP-9 in a complex which may play a role in regulating activation. Independent of MMPs, TIMP-1 has been shown to have a role in tissue homeostasis.

Long Name
Tissue Inhibitors of Metalloproteinases 1
Entrez Gene IDs
7076 (Human); 21857 (Mouse); 116510 (Rat)
Alternate Names
CLGI; Collagenase inhibitor; collagenase inhibitor); EPATIMP-1; EPO; erythroid potentiating activity; Erythroid-potentiating activity; Fibroblast collagenase inhibitor; FLJ90373; HCI; metalloproteinase inhibitor 1; TIMP metallopeptidase inhibitor 1; TIMP1; TIMP-1; TIMPtissue inhibitor of metalloproteinase 1 (erythroid potentiating activity; Tissue inhibitor of metalloproteinases 1

Citations for Recombinant Human TIMP-1 Protein, 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.

16 Citations: Showing 1 - 10
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  1. Loss of mutual protection between human osteoclasts and chondrocytes in damaged joints initiates osteoclast-mediated cartilage degradation by MMPs
    Authors: QC Larrouture, AP Cribbs, SR Rao, M Philpott, SJ Snelling, HJ Knowles
    Scientific Reports, 2021;11(1):22708.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Post-Translational Regulation And Proteolytic Activity Of The Metalloproteinase Adamts8
    Authors: S Santamaria, DR Martin, X Dong, K Yamamoto, SS Apte, J Ahnström
    The Journal of Biological Chemistry, 2021;0(0):101323.
    Species: Human
    Sample Types: Protein
    Applications: enzyme activity
  3. Matrix Metalloproteinase-3 is Key Effector of TNF-alpha-Induced Collagen Degradation in Skin
    Authors: U Mirastschi, B Lupše, K Maedler, B Sarma, A Radtke, G Belge, M Dorsch, D Wedekind, LJ McCawley, G Boehm, U Zier, K Yamamoto, S Kelm, MS Ågren
    Int J Mol Sci, 2019;20(20):.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: Bioassay
  4. Chemerin acts via CMKLR1 and GPR1 to stimulate migration and invasion of gastric cancer cells: putative role of decreased TIMP-1 and TIMP-2
    Authors: JD Kumar, I Aolymat, L Tiszlavicz, Z Reisz, HM Garalla, R Beynon, D Simpson, GJ Dockray, A Varro
    Oncotarget, 2019;10(2):98-112.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Characterization of CD200 Ectodomain Shedding
    Authors: KK Wong, F Zhu, I Khatri, Q Huo, DE Spaner, RM Gorczynski
    PLoS ONE, 2016;11(4):e0152073.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Circular trimers of gelatinase B/matrix metalloproteinase-9 constitute a distinct population of functional enzyme molecules differentially regulated by tissue inhibitor of metalloproteinases-1.
    Authors: Vandooren J, Born B, Solomonov I, Zajac E, Saldova R, Senske M, Ugarte-Berzal E, Martens E, Van den Steen P, Van Damme J, Garcia-Pardo A, Froeyen M, Deryugina E, Quigley J, Moestrup S, Rudd P, Sagi I, Opdenakker G
    Biochem J, 2015;465(2):259-70.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  7. ADAM17 regulates IL-1 signaling by selectively releasing IL-1 receptor type 2 from the cell surface.
    Authors: Uchikawa S, Yoda M, Tohmonda T, Kanaji A, Matsumoto M, Toyama Y, Horiuchi K
    Cytokine, 2015;71(2):238-45.
    Species: Primate - Chlorocebus pygerythrus (Vervet Monkey)
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Purification and characterization of bioactive his6-tagged recombinant human tissue inhibitor of metalloproteinases-1 (TIMP-1) protein expressed at high yields in mammalian cells.
    Authors: Vinther L, Lademann U, Andersen E, Hojrup P, Thaysen-Andersen M, Krogh B, Viuff B, Brunner N, Stenvang J, Moreira J
    Protein Expr Purif, 2014;101(0):157-64.
  9. TIMP-1 inhibits the proteolytic processing of Reelin in experimental epilepsy.
    Authors: Tinnes, Stefanie, Ringwald, Julia, Haas, Carola A
    FASEB J, 2013;27(7):2542-52.
    Species: Rat
    Sample Types: Whole Tissue
    Applications: Bioassay
  10. Tissue inhibitor of matrix metalloproteinase 1 (TIMP1) controls adipogenesis in obesity in mice and in humans.
    Authors: Meissburger B, Stachorski L, Roder E, Rudofsky G, Wolfrum C
    Diabetologia, 2011;54(6):1468-79.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Inhibition
  11. A multiplex immunoassay for human adipokine profiling.
    Authors: Schipper HS, De Jager W, van Dijk ME, Meerding J, Zelissen PM, Adan RA, Prakken BJ, Kalkhoven E
    Clin. Chem., 2010;56(0):1320.
  12. Decorin is a novel antagonistic ligand of the Met receptor.
    Authors: Goldoni S, Humphries A, Nystrom A, Sattar S, Owens RT, McQuillan DJ, Ireton K, Iozzo RV
    J. Cell Biol., 2009;185(4):743-54.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  13. Use of an immunoaffinity-mass spectrometry-based approach for the quantification of protein biomarkers from serum samples of lung cancer patients.
    Authors: Nicol GR, Han M, Kim J, Birse CE, Brand E, Nguyen A, Mesri M, FitzHugh W, Kaminker P, Moore PA, Ruben SM, He T
    Mol. Cell Proteomics, 2008;7(10):1974-82.
    Species: N/A
    Sample Types: N/A
    Applications: Standard
  14. Monocytes/macrophages cooperate with progenitor cells during neovascularization and tissue repair: conversion of cell columns into fibrovascular bundles.
    Authors: Anghelina M, Krishnan P, Moldovan L, Moldovan NI
    Am. J. Pathol., 2006;168(2):529-41.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  15. Depletion of cellular cholesterol and lipid rafts increases shedding of CD30.
    Authors: von Tresckow B, Kallen KJ, von Strandmann EP, Borchmann P, Lange H, Engert A, Hansen HP
    J. Immunol., 2004;172(7):4324-31.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  16. Tumor necrosis factor-alpha-accelerated degradation of type I collagen in human skin is associated with elevated matrix metalloproteinase (MMP)-1 and MMP-3 ex vivo.
    Authors: Agren M, Schnabel R, Christensen L, Mirastschijski U
    Eur J Cell Biol, 0;94(1):12-21.
    Species: Human
    Sample Types: Whole Tissue
    Applications: Tissue Culture


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Reviews for Recombinant Human TIMP-1 Protein, CF

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Recombinant Human TIMP-1 Protein, CF
By Anonymous on 07/12/2018
Application: IP for LC/MS analysis.
Reason for Rating: Great control for IPs.

By Balaji Mahender on 12/20/2017
Application: Immunoassay Standard

Recombinant Human TIMP-1 Protein, CF
By Anonymous on 11/16/2017
Application: Immunoassay Standard

This recombinant protein was used to build an ELISA standard while using MAB970 and BAF970 as the matched pair antibodies.

Recombinant Human TIMP-1 Protein, CF
By Anonymous on 05/25/2017
Application: Immunoassay Standard