11180 Results for: "Methylenov\u00E1+mod\u0159&pageNo=17"

Supplier: Bioss

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.

Supplier: OHAUS

The Defender 5000 Series multifunctional bench scales are ideal for numerous applications including production, packaging, inventory and shipping. Durably constructed to withstand harsh environments and equipped with a stainless steel platform, powder-coated steel frame and an aluminium load cell. Choice of indicator: D52P unit is ABS plastic and the D52XW indicator is 304 stainless steel with sand blasted surface treatment, which offers protection to IP 68.

Supplier: OriGene

IL17RD ANTIBODY 1 * 100 µl

Supplier: NEUBERT VOLUME GLASSWAERE

[EN]TUBE CENTRIFUGE 10ML GRINDING NS 1 * 1 KS

Supplier: A.KRÜSS Optronic

[EN]FLOW-THROUGH TUBE STAINLESS STEEL 1 * 1 KS

Supplier: Merck

7ALPHA-METHYL-5┐-ESTRAN-3ALPHA-OL- 1 * 1 mg

Supplier: LGC Standards PROMOCHEM

9-CHLORO-11BETA-HYDROXY-16BETA-METHYL-3, 1 * 100 mg

Supplier: ANTIBODIES.COM

[EN]APOLIPOPROTEIN B ANTIBODY 1 * 1 mg

Supplier: Abnova

ESTRADIOL ELISA KIT 1 * 1 KIT

Supplier: Merck

DEHYDROISOANDROSTERONE 3-ACETATE, 97% 1 * 5 g

Supplier: WTW

OxiTop®-IDS (inteligentní digitální snímače) je moderní měřicí přístroj vhodný k použití ve všech typech respirometrických měření. Univerzální OxiTop®-IDS je vhodný pro aerobní i anaerobní vyšetření. Všechny hlavy lze používat nezávisle z libovolného měřidla pro normální měření BSK mezi 1 a 7 dny.

Supplier: Dräger

The powered air-purifying respirator (PAPR) X-plore 8000 offers a number of user friendly standard and specialised carrying systems for standard and decontamination applications. Dräger has also developed a wide range of tight- and loose-fitting headgear such as half and full-face masks, short and long hoods and helmets with visor and protective visor. Standard and enhanced flexibility hoses are available and compatibility is ensured. Modular components: A wide range of components for every application.

Supplier: RPB SAFETY

The RPB T200 is a lightweight multi-purpose respirator designed specifically for the healthcare and life science industries, relieving workers of breathing difficulties and fatigue experienced with N95 use. Available with either a head harness or bump cap for head protection and multiple hood options, the T200 has the ability to adapt to different environments that need face protection and respiratory protection.

Supplier: GILSON

PIPETMAN®, recognized as the pipetting standard for its reliability and proven durability, is a fully adjustable, air-displacement pipette that uses disposable tips. PIPETMAN combines legendary accuracy, precision, and durability with easy pipetting and handling.

Supplier: MACHEREY-NAGEL

The high purity CHROMABOND® adsorbents can be used for a self-filling of SPE columns or further analytical applications.

Supplier: Merck

GLASSAEULE 1,83M X 1,4INCH GEF. MIT 10% 1 * 1 KS

Supplier: schuett-biotec GmbH

[EN]QUARTZ TUBE 1 * 2 KS

Supplier: Biorbyt

BOVINE FGF ACIDIC PROTEIN 1 * 1 µG

Supplier: Merck

[EN]MERLIN MICROSEAL SEPTUM HOLDER FOR S 1 * 1 KS

Supplier: FRITSCH

[EN]SIEVE TEST 400/65MM MESH 12 ASTM (1. 1 * 1 KS

Supplier: BUCHI

Set adaptérů PETP pro přír.trubice Ø<=17mm 1 * 1 SET

Supplier: UNEX METALLGESELLSCHAFT

[EN]Safety hose clamp - Stainless Steel 1 * 1 KS

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: BUCHI

Set těsnění PTFE pro17mm falkon zkumavky 1 * 1 SET

Supplier: LGC Standards PROMOCHEM

DEXTRORPHAN TARTRATE (O-DESMETHYLDEXTROM 1 * 1 mL

Supplier: ANTIBODIES.COM

[EN]APOLIPOPROTEIN B ANTIBODY 1 * 250 µG

Supplier: SI Analytics

O-kroužek - těsnící sada 9921/77 1 * 1 KS