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2-Cyclopropylmethoxy-3-iodopyridine
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2-Cyclopropylmethoxy-3-iodopyridine
Artikel-Nr:
(BOSSBS-1377R-A555)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1377R-A555
Lokale Artikelnummer::
BOSSBS-1377R-A555
Beschreibung:
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.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-0318R)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-0318R
Lokale Artikelnummer::
BOSSBS-0318R
Beschreibung:
PADI4 (peptidyl arginine deiminase, type IV) catalyzes the deimination of arginine residues of proteins. Down-regulates histone H3 and H4 arginine methylation, both by preventing arginine methylation by CARM1 and HRMT1L2/PRMT1 and by converting methylarginine to citrulline. subcellular location at cytoplasmic granules. Belongs to the protein arginine deiminase family. This gene may play a role in granulocyte and macrophage development leading to inflammation and immune response.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-8510R-CY7)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-8510R-CY7
Lokale Artikelnummer::
BOSSBS-8510R-CY7
Beschreibung:
Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-8510R-CY5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-8510R-CY5
Lokale Artikelnummer::
BOSSBS-8510R-CY5
Beschreibung:
Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-8116R-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-8116R-A750
Lokale Artikelnummer::
BOSSBS-8116R-A750
Beschreibung:
Component of some MITRAC complex, a cytochrome c oxidase (COX) assembly intermediate complex that regulates COX assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-1856R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1856R-A647
Lokale Artikelnummer::
BOSSBS-1856R-A647
Beschreibung:
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.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-8116R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-8116R-A647
Lokale Artikelnummer::
BOSSBS-8116R-A647
Beschreibung:
Component of some MITRAC complex, a cytochrome c oxidase (COX) assembly intermediate complex that regulates COX assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-5115R-HRP)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-5115R-HRP
Lokale Artikelnummer::
BOSSBS-5115R-HRP
Beschreibung:
The protein encoded by this gene is a membrane-bound cytochrome that reduces ferric hemoglobin (methemoglobin) to ferrous hemoglobin, which is required for stearyl-CoA-desaturase activity. Defects in this gene are a cause of type IV hereditary methemoglobinemia. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2010]
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11071R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11071R-A647
Lokale Artikelnummer::
BOSSBS-11071R-A647
Beschreibung:
This gene encodes a receptor for anthrax toxin. The protein binds to collagen IV and laminin, suggesting that it may be involved in extracellular matrix adhesion. Mutations in this gene cause juvenile hyaline fibromatosis and infantile systemic hyalinosis. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2009].
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-6728R-A488)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-6728R-A488
Lokale Artikelnummer::
BOSSBS-6728R-A488
Beschreibung:
Ca2+/calmodulin dependent protein kinase type IV (CAMKIV) belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-6728R-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-6728R-A750
Lokale Artikelnummer::
BOSSBS-6728R-A750
Beschreibung:
Ca2+/calmodulin dependent protein kinase type IV (CAMKIV) belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-4593R-A555)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-4593R-A555
Lokale Artikelnummer::
BOSSBS-4593R-A555
Beschreibung:
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-0397R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-0397R-CY3
Lokale Artikelnummer::
BOSSBS-0397R-CY3
Beschreibung:
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-1377R-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1377R-A750
Lokale Artikelnummer::
BOSSBS-1377R-A750
Beschreibung:
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.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-1377R-FITC)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1377R-FITC
Lokale Artikelnummer::
BOSSBS-1377R-FITC
Beschreibung:
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.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-1377R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1377R-CY3
Lokale Artikelnummer::
BOSSBS-1377R-CY3
Beschreibung:
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.
VE:
1 * 100 µl
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 noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das
noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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