Recombinant Mouse TIMP-4 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7667-TM

R&D Systems, part of Bio-Techne
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7667-TM-010
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Key Product Details

Source

NS0

Accession #

Q9JHB3

Conjugate

Unconjugated

Applications

Enzyme Activity

View all TIMP-4 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived mouse TIMP-4 protein
Met1-Pro224

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Cys30

Predicted Molecular Mass

23 kDa

SDS-PAGE

25-26 kDa, reducing conditions

Activity

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 <3 nM, as measured under the described conditions.

Formulation, Preparation and Storage

7667-TM
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
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.

Background: TIMP-4

Tissue inhibitors of metalloproteinases (TIMPs) are a family of secreted proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). There are four known members of the family, TIMP-1, -2, -3, and -4. TIMP-4 is produced by a wide range of tissues, particularly brain, heart, ovary and skeletal muscle (1, 2). Limited studies have shown that TIMP-4 has a tumor suppressive effect against Wilm’s tumor, exhibits negative correlation with glioma maligancy and is found in breast carcinoma cells (3, 5). TIMP-4 inhibits MMP-mediated proteolysis by forming a noncovalent binary complex with the MMP active site through its N-terminal domain. In addition, it binds to the hemopexin-like domain of proMMP-2 through its C-terminal domain in a manner similar to TIMP-2 (6). However, unlike TIMP-2, TIMP-4 does not promote proMMP-2 activation by MT1-MMP (MMP-14) (7). Although TIMP-4 is a potent inhibitor of most MMPs, it is not an effective inhibitor of ADAMs, such as TACE (8, 9).

References

  1. Greene et al. (1996) J. Biol. Chem. 271:30375.
  2. Leco et al. (1997) FEBS Lett. 401:213.
  3. Geliker et al. (2001) Oncogene 20:4337.
  4. Groft et al. (2001) Br. J. Cancer 85:55.
  5. Hurst et al. (2001) Biochem. Biophys. Res. Comm. 281:166.
  6. Bigg et al. (1997) J. Biol. Chem. 272:15496.
  7. Hernandez-Barrantes et al. (2001) Biochem. Biophys. Res. Comm. 281:126.
  8. Amour et al. (1998) FEBS Lett. 435:39.
  9. Liu et al. (1997) J. Biol. Chem. 272:20479.

Long Name

Tissue Inhibitors of Metalloproteinases 4

Alternate Names

TIMP4

Entrez Gene IDs

7079 (Human); 110595 (Mouse)

Gene Symbol

TIMP4

UniProt

Q9JHB3

Additional TIMP-4 Products

Product Documents for Recombinant Mouse TIMP-4 Protein, CF

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Recombinant Mouse TIMP-4 Protein, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

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