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Recombinant Human MMP-3 protein (His Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

His Tag

Activity

not tested

Cat no : Eg0382

Validation Data Gallery

  • Purity of Recombinant Human MMP-3 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

    Purity of Recombinant Human MMP-3 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Human MMP-3 protein Tyr18-Cys477 (Accession# P08254) with a His tag at the C-terminus.
GeneID 4314
Accession P08254
PredictedSize 56 kDa
SDS-PAGE 55-65 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

MMP-3 (matrix metallopeptidase 3), also named as Stromelysin 1 or STR1, is a member of matrix metalloproteinase (MMP) family. The MMP family of enzymes is comprised of critically important extracellular matrix remodeling proteases whose activity has been implicated in normal embryogenesis and tissue remodelling and in many diseases such as arthritis, cancer, periodontitis, glomerulonephritis, encephalomyelitis, atherosclerosis and tissue ulceration. These proteases have come to represent important therapeutic and diagnostic targets for the treatment and detection of human cancers. MMP-3 is secreted from the cells as a proenzyme. The proenzyme has been shown to stimulate plasminogen activation. The active MMP-3 is capable of cleaving types III, IV, IX and X collagen, aggrecan, fbronectin, laminin, IGFBP-3, serpins, and IL-1β.

References:

1. Roy R. et al. (2009) Journal of Clinical Oncology. 27(31):5287-5297.
2. Nagase H. et al. (1994) Contributions to Nephrology. 107:85.
3. Stamenkovic I. et al. (2003) The Journal of Pathology. 200(4):448-464.
4. Pytliak M. et al. (2012) Onkologie. 35(1-2):49-53.
5. Begoña Arza. et al. (2000). Febs Journal. 267(21):6378.
6. Fan. et al. (2011) International Journal of Molecular Medicine. 27(4).