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

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.

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: 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: 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: Hettich

ADAPTER FOR 8X15 ML TUBE 1 * 1 items

Supplier: EPPENDORF

Eppendorf Tubes® with screw cap are an ideal choice when working with medium-sized sample volumes (0,5 to 5,0 ml). SafeCode variants enhance sample identification, while the BioBased option, manufactured using renewable resources, provides an eco-friendly alternative without compromising performance.

Supplier: OHAUS

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: Cayman Chemical

17Β-HYDROXY EXEMESTANE-D3 1 * 500 µG

Supplier: AGILENT

XL1 and XL2-Blue Competent Cells are versatile for routine cloning and allow blue-white colour screening for high efficiency cloning of methylated DNA.

Supplier: MACHEREY-NAGEL

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

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: Agilent

Seat Capillary 0.17 Mm Id 110 Mm 1 * 1 items

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: KLAGER PLASTIK

BOTTLE CYLINDER 100-1 NATURAL 1 * 100 items

Supplier: CAPITAL SAFETY

Protecta Viper LT Rope kermantle ø 12.5mm, 10m length with 25kN screw gate carabiner, 17mm opening 1 * 1 items

Supplier: Merck

Monolithic silica technology: A new age in chromatography. Chromolith® columns are based on silica so existing methods can be easily transferred with only minimal investment in new method development work. 'Sol-Gel' technology allows highly porous monolithic rods of silica to be formed. These feature a bimodal pore structure provides a unique combination of macropores and mesopores.

Supplier: Roth Carl

Rotilabo-flask tongs 1 * 1 items

Supplier: KNAUER

P3058 rotor seal 1 channel 1 * 1 items

Supplier: REVCO TECHNOLOGIES

KIT REPLACEMENT UPRIGHT GASKET 13/17CF 1 * 1 items

Supplier: TRESTON

Hook,R-24 D17x65,#17x65 1 * 1 items

Supplier: Hach

STRAINER ASSY SAMPLE LINE 1 * 1 items

Supplier: SARSTEDT

TUBE, REAGENT AND CENTRIFUGE, 13ML, 88X17MM, TRANSPARENT, ROUND BASE, PUSH CAP, POLYETHYLENE 1 * 1.000 items

Supplier: GILSON

Designed for performance and comfort, PIPETMAN® L comes in a comprehensive range of models, adapted to your needs in the lab. PIPETMAN L air-displacement pipettes cover a full volume range. Comfortable, precise, accurate, and reliable, use PIPETMAN L pipettes confidently in your applications.

Supplier: ROTRONIC INSTRUMENTS

SCS CALIBRATION ACCORDING TO ISO 17025 1 * 1 items

Supplier: ProSci Inc.

Ubiquitin-Like Protein ISG15 (ISG15) is a ubiquitin-like protein that becomes conjugated to many cellular proteins upon activation by interferon-alpha and -beta. Several functions have been ascribed to the encoded protein, including chemotactic activity towards neutrophils, direction of ligated target proteins to intermediate filaments, cell-to-cell signalling, and antiviral activity during viral infections. While conjugates of this protein have been found to be noncovalently attached to intermediate filaments, this protein is sometimes secreted. ISG15 becomes conjugated to a diverse set of proteins after IFN-alpha/beta stimulation or microbial challenge. The functions or biochemical consequences ISG15 conjugation to proteins are not yet known, but it appears that this modification does not target proteins for proteasomal degradation. ISG15 shows specific chemotactic activity towards neutrophils and activates them to induce release of eosinophil chemotactic factors. Upon interferon treatment, ISG15 can be detected in both free and conjugated forms and is secreted from monocytes and lymphocytes where it can function as a cytokine. In the cell, ISG15 co-localises with intermediate filaments and ISGylation may modulate the JAK-STAT pathway or certain aspects of neurological disease.