53075 Results for: "Magnesium+trisilicate,+hydrate&pageNo=36"

Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors.

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Methyl (2Z)-3-(2,6-dichlorophenyl)-2-acetamidoprop-2-enoate 97%

Supplier: Apollo Scientific

Methyl (2Z)-3-(2,6-dichlorophenyl)-2-acetamidoprop-2-enoate 97%

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Anti-ITGAX Mouse Monoclonal Antibody [clone: 3.9]

Supplier: Tonbo Biosciences

The 3.9 antibody reacts with human CD11c, also known as integrin alpha X. This 150 kDa cell surface glycoprotein is part of a family of integrin receptors that mediate adhesion between cells (cell-cell) and components of the extracellular matrix, e.g. fibrinogen (cell-matrix). In addition, integrins are active signaling receptors which recruit leukocytes to inflammatory sites and promote cell activation. Complete, functional integrin receptors consist of distinct combinations of integrin chains which are differentially expressed. Integrin alpha X (CD11c) assembles with Integrin beta-2 (CD18) into a receptor known as CR4 which can bind and induce signaling through ICAMs and VCAM-1 on endothelial cells and can also facilitate removal of iC3b bearing foreign cells.

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Anti-MMP-26 Rabbit Polyclonal Antibody (Cy5.5®)

Supplier: Bioss

Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.