MMP14 empowers tumor-initiating breast cancer cells under hypoxic nutrient-depleted conditions: L.E. Hillebrand, et al.; FASEB J. 33, 4124 (2019), Abstract;
Hydroxy‐Safflower Yellow A inhibits the TNFR1‐Mediated Classical NF‐κB Pathway by Inducing Shedding of TNFR1: H. Wang, et al.; Phytother. Res. 30, 790 (2016), Abstract;
A comparative study on inhibition of total astragalus saponins and astragaloside IV on TNFR1-mediated signaling pathways in arterial endothelial cells: S.Q. Liu, et al.; PLoS One. 9, e101504 (2014), Abstract; Full Text
Accelerated receptor shedding inhibits kidney injury molecule-1 (KIM-1)-mediated efferocytosis: R. Gandhi, et al.; Am. J. Physiol. Renal. Physiol. 307, F205 (2014), Abstract;
Matrix metalloproteinase-8 plays a pivotal role in neuroinflammation by modulating TNF-α activation: E.J. Lee, et al.; J. Immunol. 193, 2384 (2014), Abstract;
Overexpression of TNF-α-converting enzyme in fibroblasts augments dermal fibrosis after inflammation: S. Fukaya, et al.; Lab. Invest. 93, 72 (2013), Abstract;
Produced in E. coli. Active Matrix Metalloproteinase-1 (MMP-1, interstitial collagenase, fibroblast collagenase) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-1 (Phe100-Gln268) with a C-terminal purification tag., ≥95% (SDS-PAGE) | Print as PDF
Produced in E. coli. Active recombinant matrix metalloproteinase-9 (MMP-9, gelatinase B, 92 kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Phe107-Pro449 (NM_004994), which comprises the catalytic/fibronectin domain of human MMP-9, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-9 which lacks the C-terminal hemopexin domain. Activity toward its targets, such as gelatin, casein, or peptide substrates, is unaffected., ≥95% (SDS-PAGE) | Print as PDF
Produced in E. coli. Active Matrix Metalloproteinase-3 (MMP-3, stromelysin-1, transin) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-3 (Phe100-Thr272, NM_002422) with a C-terminal purification tag., ≥95% (SDS-PAGE) | Print as PDF
Produced in insect cells. Primarily full length latent MMP-13, with some active forms present. Produced in a baculovirus expression system. | Print as PDF
Produced in E. coli. Active Matrix Metalloproteinase-13 (MMP-13, collagenase-3) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-13 (Tyr104-Asn274, NM_002427) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-13 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected., ≥95% (SDS-PAGE) | Print as PDF
