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Ammonium+cerium(IV)+sulphate
Artikel-Nr:
(ORIGBCRT104)
Lieferant:
OriGene
Hersteller-Artikelnummer::
BCRT104
Lokale Artikelnummer::
ORIGBCRT104
Beschreibung:
TissueScan Breast Cancer cDNA Array IV, containing two identical sets of 48 samples covering 4-normal, 2-Stage I, 15-IIA, 9-IIB, 7-IIIA, 4-IIIB, 6-IIIC, 1-IV. 1 * 1 KIT
VE:
1 * 1 KIT
Artikel-Nr:
(BSBTPB9233)
Lieferant:
BosterBio
Hersteller-Artikelnummer::
PB9233
Lokale Artikelnummer::
BSBTPB9233
Beschreibung:
Polyclonal antibody for TRANSFERRIN RECEPTOR/TFRC detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. TRANSFERRIN RECEPTOR/TFRC information: Molecular Weight: 84871 MW; Subcellular Localization: Cell membrane ; Single-pass type II membrane protein . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
VE:
1 * 100 µG
Lieferant:
Corning
Beschreibung:
PS, beschichtet mit Laminin (von der Maus). Laminin ist ein wichtiger Strukturbaustein der Basalmembran und hat viele verschiedene Funktionen, welche durch Bindung an die verschiedenen Bauteile der Basalmembran (z. B. Collagen IV) und an die Zelloberflächenrezeptoren vermittelt werden. Mit Laminin überzogene Zellkulturplatten können für verschiedene Anwendungen eingesetzt werden; darunter die Verbesserung der Zelladhäsion sowie die Proliferation und Differenzierung verschiedenster Zelltypen, insbesondere von Neuronen, Epithelzellen, Myozyten und Myoblasten.
Lieferant:
Thermo Scientific
Beschreibung:
Ammoniumsulfat 99.9995% (bezogen auf die Metalle der seltenen Erden)
Lieferant:
Alfa Aesar
Beschreibung:
Ammoniumsulfat ≥98%
Artikel-Nr:
(PRSI33-003)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
33-003
Lokale Artikelnummer::
PRSI33-003
Beschreibung:
Syndecans are a family of four transmembrane proteoglycans divided into two subfamilies based on transmembrane and cytoplasmic domain similarity: Syndecan 1/3 and 2/4. Via their covalently attached heparan sulphate chains, they bind a variety of ligands and play a role in a number of cell functions including adhesion, proliferation and migration. Syndecan 4 is highly expressed on the cell surface of epithelial cells and fibroblasts and plays an important role in tissue repair. Integrin-mediated binding of fibronectin to Syndecan-4 induces focal adhesions and formation of cytoskeletal stress fibers, facilitating wound healing.
VE:
1 * 100 µG
Lieferant:
Alfa Aesar
Beschreibung:
Vanadylsulfat Hydrat ≥99,9% (Metall-Basis)
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-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
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-CY7)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1377R-CY7
Lokale Artikelnummer::
BOSSBS-1377R-CY7
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
Lieferant:
Thermo Scientific
Beschreibung:
Aluminiumammoniumsulfat Dodecahydrat 99%, rein
Artikel-Nr:
(ABCAAB204034-100)
Lieferant:
Abcam
Hersteller-Artikelnummer::
AB204034-100
Lokale Artikelnummer::
ABCAAB204034-100
Beschreibung:
Anti-beta IV Tubulin Rabbit Monoclonal Antibody [clone: EPR16775] (Alexa Fluor® 647)
VE:
1 * 100 µl
 This is a MarketSource item. Additional charges may apply
Lieferant:
Alfa Aesar
Beschreibung:
Ammoniumsulfat ≥99,999% (Metall-Basis), Puratronic®
Artikel-Nr:
(ACRO193250050)
Lieferant:
Thermo Scientific
Hersteller-Artikelnummer::
193250050
Lokale Artikelnummer::
ACRO193250050
Beschreibung:
Ammoniumeisen(II)sulfat Hexahydrat 98%, reinst
VE:
1 * 5 kg
Preis auf Anfrage
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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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