12105 Results for: "Pyridine+hydrofluoride&pageNo=17&view=list"

Supplier: HAMILTON BONADUZ

These syringes are the Gastight® version of the original 700 series syringes and are ideal for dispensing volumes from 1 µl up to 500 µl.

Supplier: Biotium

Label your antibody with one of our superior CF® Dyes in 30 minutes without a purification step. Labelling tolerates many common buffer components including BSA and ascites.

Supplier: Ahlstrom-Munksjö

Ahlstrom-Munksjö’s qualitative grades of filter paper are recommended for use in analytical methods which determine or identify particulate constituents of a mixture irrespective of the amount present. Qualitative filter papers are often used in routine separation work that still requires high purity and consistent performance. These filter papers covers a wide range of laboratory applications, as liquids clarification, qualitative analytical separations for precipitates and buffers filtration, and are also used for soil analysis and in food and beverage testing. Wet-strengthened grades contain a reinforcement agent that increases their resistance to rupture when wet, such as in vacuum filtration, and their resistance when filtering acidic solutions.

Supplier: Thermo Fisher Scientific

The Pierce™ NAb™ Spin Kits are convenient for rapid, small-scale affinity purification of antibodies from a variety of sample types. Each pre-filled microcentrifuge spin column of the immobilised protein resin enables quick purification of 100 to 1000 µg of IgG from 25 to 500 µl of serum or other sample. The actual amount of IgG purified varies depending upon the sample type and the specific spin column used.

Supplier: G-Biosciences

Plasmid Screening ToothPick™ allows the rapid screening of bacteria for transformed plasmids. Simply pick a colony, add to Plasmid Screening ToothPick™ reagents and then analyse using restriction enzymes.

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: EPPENDORF

Eppendorf's twin.tec® 96-well, 150 µl PCR Plates feature a polycarbonate frame and thin-walled polypropylene wells ensuring optimal heat transfer and high rigidity. The SafeCode variants enhance sample identification, while the BioBased options, manufactured using renewable resources, provide an eco-friendly alternative without compromising performance.

Supplier: Sartorius Balances

The Cubis® II laboratory balances are modular, providing choice between applications and configurations that best suit the users' needs. These balances can be configured at the level of display, draftshields, software applications and hardware functions. The Cubis® II range of high-capacity micro balances with a maximum load between 32 and 111 g and a readability between 0,001 mg and 0,002 mg provide the ideal choice for a broad range of applications.

Supplier: VWR Chemicals

VWR® dehydrated culture media that has been granulated offers both convenience and safety benefits. The correct dissolution of culture media is critical to achieving the best performance. Granulated culture media saves time in the preparation of ready to use culture media. In addition, granulation reduces dust generation, so handling the product is more pleasant and safer for the user, making it a much cleaner and safer working environment.

Supplier: HAMILTON BONADUZ

The 1000 series is a mid volume Gastight® syringe. Gastight® syringes are ideal for dispensing both liquids and gases. They have a precision machined PTFE plunger tip which creates a leak-free seal. With the tight fit, the tip essentially wipes the interior of the syringe barrel free of sample. This feature is particularly useful with heterogeneous samples as it reduces the chance that a deposit will occur and cause the plunger to freeze.

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: CPACHEM

TRIBROMOMETHANE CRM ISO/IEC 17025/17034 1 * 1 mL

Supplier: CPACHEM

SODIUM CHLORIDE 99.995% ISO 17035 17025 1 * 50 g

Supplier: Binder

The VD series of vacuum drying chambers provide fast gentle drying of non flammable solvents, delivering impressive performance through their precise temperature control and gentle drying. Expansion rack technology also ensures optimal heat transfer, shelves provide flexible placement, and the interior of the chamber is easy to clean. The VDL series of safety vacuum drying chambers ensures maximum safety when drying flammable organic solvents, and have been safety tested by a state recognised test institute (GS mark). VD/VDL units can also be purchased as modular options with vacuum pump and pump chamber to form a complete system.

Supplier: LMS

LMS Series 4 cooled incubators are temperature controlled cabinets with fan assisted air circulation via a pre-mixing chamber. The units have a stainless steel exterior, stainless steel lined interior with polyurethane foam insulation, and feature a door lock and magnetic door gasket. Corrosion resistant inner chamber is easy to clean, disinfection procedures are detailed in the user manual.

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: DWK Life Sciences

TISSUE GRINDER 0.3ML MICRO DUAL ALLGLASS 1 * 1 items

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: KOEHLER TECHNISCHE PRODUKTEN

transparente Dose, blauer Deckel 1 * 1 items

Supplier: CUSTOM MADE CHEMICALS LAB

10mg/l each of Ag As Ba Cd Co Cr Cu Hg Li Ni Pb Sb Se Sn Tl V Mo 1 * 100 mL

Supplier: HORIBA

These waterproof meters can measure and display up to 11 parameters simultaneously with one single probe. Thanks to their rugged design and their field replaceable sensors they are ideal for outdoor use, for example, when testing ground or surface water. Their compact size and the hand strap enable one-handed operation.

Supplier: EPPENDORF

Eppendorf epT.I.P.S.® Reloads offer high-precision pipette tips in 'Eppendorf Quality' and 'PCR clean' purity grades. Eco-friendly, cost-effective, and designed for seamless compatibility with Eppendorf Box 2.0, they ensure accuracy and sustainability in labs.

Supplier: Lovibond Tintometer

Filter Set 3000 Comp. Gardner (TINT 342000 ) 1 * 1 items

Supplier: Thermo Fisher Scientific

Thermo Scientific Slide-A-Lyzer™ G3 Dialysis Cassettes facilitate the rapid and trouble-free dialysis of sample volumes from 0,5 to 125 ml. Unlike standard flat tubing, these innovative devices do not require knots or clips that can lead to leaking and sample loss.

Supplier: FRISTADS KANSAS

These high visibility trousers are made of 54% modacrylic, 44% cotton and 2% anti-static fibre. Reinforced with 79% cotton FR, 20% polyamide, 1% anti-static fibre. They provide protection against chemicals, heat, flames and electric arcs.