Esta buscando: Ácido+hexacloroiridico+(IV)

Numero del catalogo: (BOSSBS-1856R-HRP)

Proveedor: Bioss

Descripción: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-1856R-FITC)

Proveedor: Bioss

Descripción: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-1564R-CY3)

Proveedor: Bioss

Descripción: The Annexins are a family of structurally similar proteins. Annexins bind to phospholipids and may be involved in regulation of membrane transport, membrane channel activity, and interaction of the cell membrane with the extracellular matrix. Annexin A4 (ANXA4) belongs to the annexin family of calcium dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have been implicated in membrane related events along exocytotic and endocytotic pathways. ANXA4 has 45 to 59% identity with other members of its family and shares a similar size and exon intron organization. Isolated from human placenta, ANXA4 encodes a protein that has possible interactions with ATP, and has in vitro anticoagulant activity and also inhibits phospholipase A2 activity. ANXA4 is almost exclusively expressed in epithelial cells.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-1564R-CY7)

Proveedor: Bioss

Descripción: The Annexins are a family of structurally similar proteins. Annexins bind to phospholipids and may be involved in regulation of membrane transport, membrane channel activity, and interaction of the cell membrane with the extracellular matrix. Annexin A4 (ANXA4) belongs to the annexin family of calcium dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have been implicated in membrane related events along exocytotic and endocytotic pathways. ANXA4 has 45 to 59% identity with other members of its family and shares a similar size and exon intron organization. Isolated from human placenta, ANXA4 encodes a protein that has possible interactions with ATP, and has in vitro anticoagulant activity and also inhibits phospholipase A2 activity. ANXA4 is almost exclusively expressed in epithelial cells.

UOM: 1 * 100 µl

Promoción

Proveedor: Merck

Descripción: Ácido sulfúrico 2.5 mol/l (5 N) en solución acuosa, Titripur® solución volumétrica, Supelco®

FDS

Proveedor: Merck

Descripción: Ácido fórmico ≥99.0% (by acidimetry) para síntesis, Sigma-Aldrich®

FDS

Proveedor: Merck

Descripción: Ácido tricloroacético (cristalizable) para síntesis, Sigma-Aldrich®

FDS

Numero del catalogo: (1.00684.0005)

Proveedor: Merck

Descripción: Ácido sulfanílico, Supelco®

UOM: 1 * 5 g

FDS Certificados Promoción

Proveedor: PROLABO CMP

Descripción: Ácido ortofosfórico 150 ml/l

Numero del catalogo: (1.17048.1000)

Proveedor: Merck

Descripción: Ácido sulfúrico 95-97% for COD determination, Supelco®

UOM: 1 * 1 L

FDS Certificados Promoción

Numero del catalogo: (PRLS89269.360)

Proveedor: PROLABO CMP

Descripción: Ácido ortofosfórico 0.667 mol/l (2 N)

UOM: 1 * 5 L

Promoción

Numero del catalogo: (PRLS85104.360)

Proveedor: PROLABO CMP

Descripción: Ácido ortofosfórico 120 ml/l

UOM: 1 * 5 L

Promoción

Numero del catalogo: (BOSSBS-1377R)

Proveedor: Bioss

Descripción: 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 remodeling, 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.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-1377R-A488)

Proveedor: Bioss

Descripción: 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.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-1377R-A647)

Proveedor: Bioss

Descripción: 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.

UOM: 1 * 100 µl

Promoción

Proveedor: PROLABO CMP

Descripción: Ácido sulfúrico 1 mol/l (2 N) en solución acuosa

FDS Certificados