Feb 16, 2017 · Cleavage of PAR1 by MMP-2 was significantly enhanced in CHO cells expressing both PAR1 and α IIb β 3, while MMP-2 was unable to potentiate the activation of platelets of GT patients, confirming that α IIb β 3 is a crucial cofactor for PAR1 activation by MMP-2.

MMP-2 (a type of gelatinase A, 72 kDa) and MMP-9 (a type of gelatinase B, 92 kDa) are composed of 3 domains, distinguished by the presence of type II additional fibronectin domain inserted into the catalytic domain.

The conservation of an inefficient signal sequence in MMP-2 orthologs suggests the presence of selective pressure to retain a significant fraction of this protease within the cytoplasm. This could support the notion that MMP-2 has important, but unknown, physiological functions within cells.

Matrix metalloproteinase 2 (MMP2) is a well-characterized protein that is indispensable for extracellular matrix remodeling and other pathological processes, such as tumor progression and skeletal dysplasia.

Jul 16, 2013 · Transcription from this site generates an N-terminal truncated 65 kDa isoform of MMP-2 (NTT-MMP-2) that lacks the secretory sequence and the inhibitory prodomain region. The NTT-MMP-2 isoform is intracellular, enzymatically active and localizes in part to mitochondria.

The Recombinant Human MMP-2 Protein from R&D Systems is derived from CHO. The Recombinant Human MMP-2 Protein has been validated for the following applications: Enzyme Activity.

Jun 1, 2017 · Human glioblastomas express higher levels of matrix metalloprotease-2 (MMP-2) than low-grade brain tumors and normal brain tissues. Ascochlorin (ASC) has anti-metastatic, …

Nov 19, 2013 · To better understand the subcellular distribution of MMP-2, we expressed HaloTagged MMP-2 in HL-1 cardiomyocytes and used fluorescence confocal microscopy to compare their distribution with markers for ER (PDI) and mitochondria (Mitotracker red).

Jun 17, 2016 · In this study, we hypothesized that proteolytic enzymes including MMP-2 have a specific expression pattern depending on the differentiation state (adipogenic, chondrogenic, and osteogenic differentiation) and that ECM (Col II) increases MMP-2 …

Feb 16, 2017 · Cleavage of PAR1 by MMP-2 was significantly enhanced in CHO cells expressing both PAR1 and α IIb β 3, while MMP-2 was unable to potentiate the activation of platelets of GT patients, confirming that α IIb β 3 is a crucial cofactor for PAR1 activation by MMP-2.