Stromelysin-1/MMP-3 Protein, Human

The Stromelysin-1/MMP-3 protein is a multifunctional metalloprotease that degrades a variety of extracellular matrix components and activates molecules such as growth factors, plasminogen, and MMP9. It is released into the ECM and is activated through the plasmin cascade. Stromelysin-1/MMP-3 Protein, Human is the recombinant human-derived Stromelysin-1/MMP-3 protein, expressed by E. coli , with tag free. The total length of Stromelysin-1/MMP-3 Protein, Human is 255 a.a., with molecular weight of ~34 kDa.

Stromelysin-1/MMP-3, a metalloproteinase, exhibits a broad substrate specificity, capable of degrading various components of the extracellular matrix (ECM) such as fibronectin, laminin, gelatins (type I, III, IV, and V), collagens (III, IV, X, and IX), and cartilage proteoglycans. This enzyme plays a pivotal role in activating different molecules, including growth factors, plasminogen, or other matrix metalloproteinases like MMP9. Upon release into the ECM, the inactive pro-enzyme undergoes activation through the plasmin cascade signaling pathway. Stromelysin-1/MMP-3 also functions intracellularly, as observed in dopaminergic neurons where it becomes activated by the serine protease HTRA2 during stress, contributing to dopamine neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage. Additionally, this metalloproteinase plays a role in immune response and exhibits antiviral activity against various viruses, including vesicular stomatitis virus, influenza A virus (H1N1), and human herpes virus 1. Mechanistically, it translocates from the cytoplasm into the cell nucleus upon virus infection to modulate NF-kappa-B activities.

Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nva-WR-K(Dnp)-NH2 and the specific activity is >300 pmoles/min/μg. (Activation description: The proenzyme needs to be activated by Chymotrypsin for an activated form).

Human

E. coli

Tag Free

P08254 (Y18-T272)

4314  [NCBI]

YPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPET

Approximately 34 kDa

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris, 10 mM CaCL₂, 1uM ZnCL₂, 50 mM NaCl, 0.5% Brij35, pH 7.0. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Less than 1 EU/µg as determined by LAL test.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.