12089 Results for: "VARLP041720ELTN00001&pageNo=17&view=easy"

Supplier: RENTEX

Lined jacket made from 55% modacrylic, 43% cotton and 2% Nega-Stat® with PTFE coating. The lining is made from 100% cotton with flame-resistant Proban® coating. Filling is made from 100% viscose FR.

Supplier: Thermo Orion

Use the Orion Star T940 all-in-one titrator for flexible pH, redox and ion concentration titrations including equivalence point titrations, preset pH or mV endpoint titrations plus multiple known addition (MKA) mode for automated known addition of various ions.

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: Ansell

Hand-specific, ergonomically designed gloves with a beaded cuff. Ideal for use in laboratories, pharmaceutical, biotech and medical device manufacturing.

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: 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: 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: 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: Corning

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

Supplier: Antibodies.com

Human LI Cadherin ELISA Kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human LI Cadherin in serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Supplier: Antibodies.com

Rat IL-17A ELISA Kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of rat IL-17A in serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

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: 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: Antibodies.com

Mouse pTau ELISA kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of mouse pTau in serum, plasma, cell culture supernatant, cell or tissue lysate, and other liquid samples.

Supplier: Antibodies.com

Human Tau (phospho T231) ELISA Kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human Tau (phospho T231) in serum, plasma, cell culture supernatant, cell or tissue lysate, and other liquid samples.

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: 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: 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: Ansell

These overalls consisting of two layers of fabric (non woven inner layer and microporous PE film) provide both protection and comfort with exceptional liquid and particulate protection. Ideal for industrial applications.

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: Antibodies.com

Human IL-17A ELISA kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human IL-17A in serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

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: Portwest

A classic style with a full update, made from a sustainable polyester/cotton fabric.

Supplier: Portwest

Rugged trouser made from durable Kingsmill polyester/cotton 300 g fabric with a modern fit and adjustable leg length. Pockets have oxford reinforcement for extra durability.