Latent protein • Host: HEK293 cells • AA: 20-469 • Tag: C-terminal His • MW: 50-55 kDa
Technical Support & Resources

Visit our FAQ

Contact Us

Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888

Request Technical Support

Technical Support Request

To streamline the process attach the appropriate questionnaire to your inquiry.

Download IHC QuestionnaireDownload WB Questionnaire

View Our Privacy Statement for details on how we use and protect your data. In addition, this site is protected by hCaptcha and its Privacy Policy and Terms of Service apply.

MMP-1 (human, recombinant)

Item No. 35438

Technical Information
Synonyms
  • Collagenase-1
  • Fibroblast Collagenase
  • Interstitial Collagenase
  • Matrix Metalloproteinase-1
Purity
≥95% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/µg determined by the LAL endotoxin assay
Source
Recombinant human C-terminal His-tagged MMP-1 expressed in HEK293 cells
Amino Acids
20-469
MW
50-55 kDa
Lyophilized from sterile 25 mM MES, pH 6.0, with 1 mM calcium chloride, 150 mM sodium chloride, 0.5% Brij 35, 5% trehalose, 5% mannitol, and 0.01% Tween 80
UniProt Accession №
P03956
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
Recommended Products

Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

    Add

    Add

    Kinase Resource Center
    Discover Products & Resources for Kinase Research
    • Kinase inhibitors, screening libraries, assay kits, & more
    • Tools to study kinase signaling pathways:
      • Growth factor signaling
      • PI3K/Akt/mTOR
      • MAPKs (ERK, p38, & JNK)
      • JAK/STAT signaling
    • Articles, resources, & advice
    EXPLORE NOW
    Product Description

    Matrix metalloproteinase-1 (MMP-1) is an endopeptidase that has a major role in tissue remodeling.1,2 It is composed of an N-terminal extracellular signal peptide, a prodomain containing a cysteine switch that interacts with the catalytic domain to regulate the proteolytic activity of MMP-1, a catalytic domain, and a C-terminal domain containing four hemopexin-like repeats which confer specificity for collagen.1 MMP-1 is ubiquitously expressed at low levels under normal physiological conditions and localizes to the extracellular space.2 It is primarily involved in the degradation of the extracellular matrix with type I collagen being its main substrate, but also degrades types II, III, V, IX, and X fibrillar collagens. MMP-1 also cleaves cell surface molecules such as insulin-like growth factor 1 (IGF-1) binding protein 3 (IGFBP3) and TNF-α.1 Knockdown of MMP1 inhibits the proliferation, migration, and invasion of colorectal cancer cells.3 MMP1 transgenic mice exhibit increased alveolar damage following exposure to M. tuberculosis.4 Polymorphisms of MMP1 are associated with several diseases, including various cancers, periodontitis, and coronary artery disease.2 Cayman’s MMP-1 (human, recombinant) protein provided as the latent zymogen form. After activation with p-aminophenylmercuric acetate (APMA), it can be used for enzyme activity applications. This protein consists of 461 amino acids and has a predicted N-terminus of Phe20 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 50-55 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Pardo, A., and Selman, M. MMP-1: The elder of the family. Int. J. Biochem. Cell Biol. 37(2), 283-288 (2005).

    2. Arakaki, P.A., Marques, M.R., and Santos, M.C.L.G. MMP-1 polymorphism and its relationship to pathological processes. J. Biosci. 34(2), 313-320 (2009).

    3. Wang, K., Zheng, J., Yu, J., et alKnockdown of MMP‑1 inhibits the progression of colorectal cancer by suppressing the PI3K/Akt/c‑myc signaling pathway and EMT. Oncol. Rep. 43(4), 1103-1112 (2020).

    4. Elkington, P., Shiomi, T., Breen, R., et alMMP-1 drives immunopathology in human tuberculosis and transgenic mice. J. Clin. Invest. 121(5), 1827-1833 (2011).