MMP2

Epithelial-Mesenchymal Transition (EMT) is the trans-differentiation of stationary epithelial cells into motile mesenchymal cells. During EMT, epithelial cells lose their junctions and apical-basal polarity, reorganize their cytoskeleton, undergo a change in the signaling cascade that defines cell shape and reprograms gene expression. Collectively, these changes increase the motility of individual cells and enables the development of an invasive phenotype.

MMP2 is a 72 kDa enzymatic protein and it belongs to matrix metalloproteinases (MMPs), a heterogenous family of zinc/calcium-dependent TIMPs (tissue inhibitors of matrix metalloproteinases) regulated matrix-degrading endopeptidases which are classified into collagenases (MMP-1, -8, -13, -18), gelatinases (MMP-2, -9), stromelysins (MMP-3, -7, -10, -11), elastase (MMP-12), and membrane-type matrix metalloproteinases (MT-MMP-1 through -5) (1). MMP2 involves in extracellular matrix metabolism and cleaves type IV collagen along with degrading the already denatured collagens.

MMP24 is an extracellular matrix (ECM) degradative peptidase enzyme that is a member of the large family of matrix metalloproteinases (MMP). Each MMP has a different substrate specificity, and the aberrant or derailed expression of these is strongly correlated with unregulated events such as tumor invasion, metastasis, angiogenesis, and arthritis. This is in contrast to the tightly controlled normal physiological processes such as tissue remodeling, reproduction, rebuilding, and embryonic development. Deregulation often occurs through the loss of negative checks.

GPNMB is a type I transmembrane glycoprotein with homology to the PMEL17 precursor, a melanocyte-specific protein. Two transcript variants encoding different isoforms exist.GPNMB is expressed in minimally (but not highly) metastatic human melanoma cell lines and xenografts and may be involved in the delay and reduction of metastatic potential and growth.

MMP2 is a peptidase enzyme that belongs to the large family of matrix metalloproteinases (MMPs) which degrade the extracellular matrix (ECM) with different substrate specificities. Aberrant and unregulated expression of MMPs via deregulation of key negative check controls is strongly associated with increased tumor invasiveness, metastasis potential, and angiogenesis. This uncontrolled behavior is in direct contrast to the tightly controlled physiological systems of embryonic development, tissue remodeling, and rebuilding.

MMP2 is an extracellular matrix degradative peptidase enzyme that belongs to the large family of matrix metalloproteinases (MMPs) which each have different substrate specificities. Aberrant or derailed expression of various MMPs through loss of negative checks is strongly associated with tumor invasion, metastasis, and angiogenesis, as compared to tightly controlled physiological processes such as tissue remodeling, rebuilding, and embryonic development.

Calreticulin is a Calcium binding chaperone that has multiple functions both inside and outside the endoplasmic reticulum. Calreticulin is involved in the quality control of newly synthesized proteins and glycoproteins, interacting with various other ER chaperones, specifically Calnexin.

The matrix metalloproteinases are zinc-dependent protease enzymes which interact with a range of ECM (extracellular matrix) proteins, and are activated by proteolytic cleavage. We at Novus Biologicals offer a wide range of top quality MMP reagents, including MMP3, MMP7, MMP9, MMP13 and MMP2 specific antibodies.

The main function of the matrix metalloproteinase (MMP) family was originally thought to be restricted to degradation of extracellular matrix (ECM) proteins. However, studies with their antibodies have identified several other functions. We at Novus Biologicals have an extensive range of MMP antibodies for research.

The enzymes of the Matrix Metalloproteinase (MMP) family assist in the degradation of the extracellular matrix, under both normal and pathological conditions. MMP antibodies have identified roles in a number of physiological processes, such as embryonic development and tissue remodelling. They also regulate enzyme cascades, expression of various proteins and the migration of both normal and malignant cells.