11826 Results for: "Western+Blotting+Reagents&pageNo=17&view=easy"

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: Lovibond Tintometer

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

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: 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: LMS

LMS Series 2 cooled incubators are temperature controlled cabinets with fan assisted air circulation via a pre-mixing chamber. The units have a white enamelled sheet steel exterior, high impact plastic interior and polyurethane foam insulation, and feature a door lock and magnetic door gasket. The corrosion resistant inner chamber is easy to clean, disinfection procedures are detailed in the user manual.

Supplier: GRANT INSTRUMENTS

The Grant Optima™ range consists of both general purpose and advanced performance thermostats combined with premium stainless steel baths (drain tap on 12, 18, 26 and 38 litre baths). Stirred circulation within the bath ensures excellent temperature stability and uniformity. Units can also be used with accessory C1G and C2G immersion coolers for operation below ambient temperatures.

Supplier: MOTIC

Microscopes for basic work in biology life science. Fixed Koehler set-up gives adequate power resources for upgrading the microscope with contrast methods like phase contrast, polarisation or darkfield. The Motic BA 210 is a robust, ready to use with pre-installed set-up of optics and 3 W LED illumination.

Supplier: WATERS

Column Acquity BEH C18 VanGuard Pre-column 1.7um 2.1 x 5mm 1 * 3 items

Supplier: Lovibond Tintometer

4/49 I.F.U. Disc (TINT 244900 ) 1 * 1 items

Supplier: Lovibond Tintometer

4/50 I.F.U. Disc (TINT 244700 ) 1 * 1 items

Supplier: OriGene

Recombinant human HSD17B11 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. 1 * 100 µG

Supplier: LEICA MICROSYSTEMS

The Leica DM IL is a fluorescence-ready digital imaging solution designed for use in a variety of laboratory settings including cell culture, micromanipulation, immuno staining and routine live imaging.

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: DEUTSCH NEUMANN

HOLLOW STOPPERS NAT. RUBB. RED 19/17MM 1 * 100 items

Supplier: WATERS

Column AccQ-Tag Ultra C18 1.7um 2.1 x 100mm 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

mit Kurzschliff Rundboden 24 x 2,5 100 mm 36,80 + - 0,10g 1 * 1 items

Supplier: DWK Life Sciences

Tube 50ml, round, 34x100mm, borosilicate3.3. 1 * 200 items

Supplier: LGC Standards PROMOCHEM

11-DEOXYCORTISOL (17,21-DIHYDROXYPREGN-4-ENE-3,20-DIONE) 1 * 10 mg

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: 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: 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: HWS LABORTECHNIK

O-RING 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: 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: 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, stainless steel frame and a stainless steel (single range models) or aluminium load cell (dual range models). The front mounted D52XW indicator is 304 stainless steel with sand blasted surface treatment, which offers protection to IP 68.