11785 Results for: "Microbiology+Test+Systems&pageNo=17&view=list"

Supplier: DuPont

These Tyvek® overalls are composed of flash spun high density polyethylene, providing an ideal balance of protection, durability and comfort. Tyvek® is permeable to both air and water vapour, yet repels water-based liquids and aerosols. It offers an excellent barrier against fine particles and fibres (down to 1 µm in size).

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: FRISTADS KANSAS

Thanks to its durability and high degree of comfort, the PR54 jacket is perfectly suited to workshops and industrial and service enterprises. The material is made from 65% polyester and 35% cotton. The inside is brushed and as a result conveys a pleasantly comfortably cotton feeling. The outside is also resistant to the roughest demands and will not fade even after countless washes.

Supplier: SIOEN

Waterproof and windproof jacket either made of Flexothane® Essential (100% polyester knitting with PU coating) or Flexothane® Classic (polyamide knitting with PU coating). All versions feature a fixed quilted lining for cold protection and high frequency welded seams.

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: Sartorius Balances

Cubis® II MCE analytical balances with essential user interface offer a maximum weighing capacity between 120 and 520 g in combination with readability of 0.1 mg.

Supplier: Sartorius Balances

Cubis® II MCE high-capacity toploading balances with essential user interface offer a maximum load between 11,2 and 70,2 kg and readability between 0,1 and 1 g provide the ideal model for every application.

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: SI Analytics

The number of samples to be processed is growing constantly while at the same time the demands on reliability are increasing in accordance with GLP and ISO standards. The SI Analytics sample changer (TW 7200) helps you meet these increased requirements and free up highly qualified employees from routine work. TW 7200 basic unit with two integrated magnetic stirrers, including external power supply 100 to 240 V with adapters for EU, US and UK, USB cable for direct PC connection and connection cable for rod stirrer.

Supplier: VWR Collection

Experience the next level of high-performance liquid chromatography with the Chromaster Plus HPLC system. This latest version boasts a sleek new design and enhanced performance features, including the upgraded CM5310 column oven and CM5410 UV detector. The new design offers a modern and user-friendly interface, while the enhanced performance of the CM5310 column oven and CM5410 UV detector ensures superior results. Additionally, users can enjoy peace of mind with an extended warranty coverage.

Supplier: Q BIOANALYTIC

OneCup it‘s so easy! The OneCup assay comes along with a minimum of pipetting steps. Everything is included in the mix. You only need to combine 20 μl of the mix with 2 μl of your DNA sample and everything is ready. You have a minimum of hands-on time and avoid mistakes during pipetting. You can run the test on all common block cyclers. Application: Detection of Salmonella in food samples and environmental samples subsequent to a pre-enrichment step according to DIN EN ISO 20837 and 20838. In combination with an appropriate pre-enrichment and DNA preparation the test complies with the official method of the German food and feed law §64. ASU L00.00-98. Test principle: The test is dedicated to detect DNA of Salmonella in a sample using Real-Time PCR in compliance with the ISO method mentioned below. The kit uses the TaqMan® principle. Thus the requirements of the ISO standard, that an amplification product has to be confirmed by a hybridization step, is fulfilled. Each reactions contains an internal amplification control. Therefore, false negative results due to inhibition of the reaction can be excluded. The test included the UNG enzyme to prevent re-amplification of contaminating amplicons.

Supplier: THERMO MATRIX TECHNOLOGIES

Matrix™ tri-coded tubes combine the 2D matrix code with an improved linear and human-readable barcode.

Supplier: Thermo Fisher Scientific

Integral filter made from water-repellent PE which does not swell on accidental penetration by liquid, allowing recovery of the sample. Protect pipettes and the samples from contamination with Thermo Scientific™ Finntip™ Filtered Pipette Tips. These sterile, disposable pipette tips keep pipettes clean, and are perfect for PCR amplification applications and for pipetting radioactive, infectious, and aerosol-emitting samples. Available in racks with a wide volume range of 0,2 μl to 10 ml.

Supplier: Sartorius Balances

Cubis® II MCE precision balances with essential user interface offer a maximum load between 320 and 14200 g and a readability of 1 to 100 mg provide, ideal model for every application.

Supplier: Portwest

This hardwearing contrast colour jacket is made of 60% cotton and 40% polyester. The soft handle cotton rich fabric is built to last and will look and feel great. Cotton ensures it washes well at 60 °C whilst the polyester gives a ruggedness essential for daily use.

Supplier: Portwest

Stylish, functional, and durable, the PW2 winter jacket offers protection and warmth in extreme weather conditions. Key features include contrast coloured panels for added style, an adjustable detachable hood, and plenty of pockets for storage.

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: Corning

Filtered, maxymum recovery, and sterile pipette tips in a truly sustainable packaging format that reduces plastic by 70% per case.

Supplier: ProSci Inc.

The gene encodes the DMRT1 protein is found in a cluster with two other members of the gene family, having in common a zinc finger-like DNA-binding motif (DM domain). The DM domain is an ancient, conserved component of the vertebrate sex-determining pathway that is also a key regulator of male development in flies and nematodes. This gene exhibits a gonad-specific and sexually dimorphic expression pattern. Defective testicular development and XY feminization occur when this gene is hemizygous. This suggested that DMRT1 may be required for testis development.This gene is found in a cluster with two other members of the gene family, having in common a zinc finger-like DNA-binding motif (DM domain). The DM domain is an ancient, conserved component of the vertebrate sex-determining pathway that is also a key regulator of male development in flies and nematodes. This gene exhibits a gonad-specific and sexually dimorphic expression pattern. Defective testicular development and XY feminization occur when this gene is hemizygous. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: OHAUS

The Scout® SKX series has been designed for education applications. The overload protection and large backlit LCD, backed by education software makes the Scout® the ideal balance for the classroom. The integrated transportation lock protects the load cell from damage during stacking storage and transportation. Can be used either in battery-powered mode (4× AA batteries, not included) or via the AC adapter, with power saving auto shut-off function and low battery indicator. The SKX123 has an ingenious draught shield with an easy to remove top cover piece.

Supplier: ANTIBODIES.COM

Mouse ISG15 ELISA Kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of mouse ISG15 in serum, plasma, tissue homogenates, and other biological fluids.

Supplier: HUBER

Huber Unichillers offer better efficiency, stable pressure and delivery performance with a constant cooling water temperature compared to traditional tap water cooling.

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.

Supplier: ANTIBODIES.COM

Mouse IL-17A ELISA kit is a high sensitivity sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of mouse IL-17A in serum, plasma, and other biological fluids.

Supplier: 3M

The 3M Speedglas Heavy-Duty Welding Helmet G5-01 builds on the 9100 series. Having more adjustable features than ever - from the colour as seen through the welding filter to the direction of the airflow and the level of coverage.

Supplier: EPPENDORF

The robust Reference® 2 is the successor to the Reference® pipette and features a new design, reduced weight and unique one-button operation.

Supplier: HELLMA

The Hellma® calibration standards comply with all necessary standards and regulations and thus offer the highest quality for recalibrating your spectrometer.

Supplier: Thermo Fisher Scientific

Based on Core Enhanced Technology, using 4 µm solid core particles, these columns allow users of conventional HPLC methods to enjoy performance far beyond that of columns packed with 5, 4 or even 3 μm fully porous particles. Very high separation efficiencies, using standard HPLC instruments and conditions, provide increased peak resolution and lower limits of detection. An ultra-stable packed bed results in exceptionally robust columns that demonstrate excellent retention and response reproducibility.