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Description:
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesised as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodelling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.
Description:
Transcription factor required for formation of positional identity in the developing retina, regionalization of the optic chiasm and morphogenesis of the kidney. Can neuralize ectodermal cells directly By similarity. Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and acts as a transcriptional repressor. Also acts as a transcriptional activator. Promotes development of neural crest cells from neural tube progenitors. Restricts neural progenitor cells to the neural crest lineage while suppressing interneuron differentiation. Required for maintenance of pluripotent cells in the pre-implantation and peri-implantation stages of embryogenesis. Probable transcription factor involved in embryogenesis and somatogenesis. FOXD1 is involved in regulating inflammation as well as kidney and retinal development. FOXD1 regulates the activity of NFAT and NFkB. Deficiency of FOXD1 results in multiorgan systemic inflammation, exaggerated Th cell-derived cytokine production, and T cell proliferation in autogolgous MLRs. In kidneys, FOXD1 controls the production of signals required for the normal transition of induced mesenchyme into tubular epithelium and full growth and branching of the collecting system. Deletion of FOXD1 results in renal abnormalities. FOXD2 acts as a modulator of T cell activation.
Description:
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.
Description:
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.
Description:
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.
Description:
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.
Description:
Required for S phase entry of the cell cycle.The eukaryotic cell division cycle consists of a number of gene-controlled sequences that involve cyclin dependent kinases (Cdks) and cell division control (Cdc) proteins. Cdc123 (Cell division cycle protein 123), also known as D123, is a 336 amino acid cytoplasmic protein that is involved in cell cycle control. Widely expressed with high expression in thymus, spleen, ovary, testis, small intestine and leukocytes, Cdc123 functions to destabilize Chfr (checkpoint with forkhead and ring finger domain) proteins which, when accumulated, block the G to S phase transition. Cdc123 prevents the Chfr proteins from collecting in the cell, thereby allowing the cell to enter the S phase. Due to its role in cell cycle control, Cdc123 is thought to be a basal marker for luminal breast cancers.
Description:
Required for S phase entry of the cell cycle.The eukaryotic cell division cycle consists of a number of gene-controlled sequences that involve cyclin dependent kinases (Cdks) and cell division control (Cdc) proteins. Cdc123 (Cell division cycle protein 123), also known as D123, is a 336 amino acid cytoplasmic protein that is involved in cell cycle control. Widely expressed with high expression in thymus, spleen, ovary, testis, small intestine and leukocytes, Cdc123 functions to destabilize Chfr (checkpoint with forkhead and ring finger domain) proteins which, when accumulated, block the G to S phase transition. Cdc123 prevents the Chfr proteins from collecting in the cell, thereby allowing the cell to enter the S phase. Due to its role in cell cycle control, Cdc123 is thought to be a basal marker for luminal breast cancers.
Description:
Required for S phase entry of the cell cycle.The eukaryotic cell division cycle consists of a number of gene-controlled sequences that involve cyclin dependent kinases (Cdks) and cell division control (Cdc) proteins. Cdc123 (Cell division cycle protein 123), also known as D123, is a 336 amino acid cytoplasmic protein that is involved in cell cycle control. Widely expressed with high expression in thymus, spleen, ovary, testis, small intestine and leukocytes, Cdc123 functions to destabilize Chfr (checkpoint with forkhead and ring finger domain) proteins which, when accumulated, block the G to S phase transition. Cdc123 prevents the Chfr proteins from collecting in the cell, thereby allowing the cell to enter the S phase. Due to its role in cell cycle control, Cdc123 is thought to be a basal marker for luminal breast cancers.
Description:
Myo-inositol is involved in many important aspects of cellular regulation including membrane structure, signal transduction and osmoregulation. It is taken up into cells by the sodium/myo-inositol cotransporter (SMIT). SMIT activity maintains intracellular concentrations of myo-inositol; it is upregulated in response to hypertonic stress. The human SMIT protein is encoded by the SLC5A3 gene, which maps to chromosome 21q22.12. It is expressed in many human tissues, such as brain, kidney and placenta. Specifically, SMIT is abundantly expressed throughout the whole brain and spinal cord in fetal rat, but is downregulated in adult rat brain with the exception of the choroid plexus, where SMIT expression remains high. In kidney, SMIT localizes to the baso-lateral membranes of the thick ascending limb of Henle (TAL) and the inner medullary collecting duct (IMCD). Impaired SMIT activity is implicated in the pathogenesis of diabetes and Down syndrome.
UOM:
1 * 100 µl
Promotion
,BOSSBS-11954R-HRPEA
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