11082 Results for: "P\\\\\\\\\\\\\\\\u0142ytki+do+TLC&pageNo=17&view=easy"

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: Thermo Fisher Scientific

Hypercarb porous graphitic carbon (PGC, Hypercarb) is a unique stationary phase composed of flat sheets of hexagonally arranged carbon atoms with a satisfied valence, as in a very large polynuclear aromatic molecule, it provides extended separation capabilities, enhanced retention of polar compounds and separtion of structurally related analytes with stability at extreme pH and high temperature.

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: VWR Collection

Designed to hold multiple test tubes, test tube racks, vials or cylinders. Vortexing action is created by securing the top of the vessel in place while allowing the bottom to move freely in a defined orbit. Two stainless steel posts hold the support plate securely in place for quiet, rattle-free mixing. The support plate is easily adjustable by loosening knobs and moving the support plate up and down. The circular groove around the top of the taller post allows the support plate to be swung away from the tray for easy removal of samples. The suction cup feet dampen motion and prevent the unit from moving along the work bench. Made from stainless steel with corrosion resistant paint. Equipped with a powerful, permanent magnet motor with sealed ball bearings. Motor is rated for continuous duty.

Supplier: Avantor Fluid Handling

Versatile piston pump drives for high-accuracy fluid dispensing and delivery – with an intuitive touch-screen interface.

Supplier: Avantor Fluid Handling

High-flow pump for process applications – with an intuitive touch-screen interface and advanced connectivity.

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: 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: 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: 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 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: 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: 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: THERMO MATRIX TECHNOLOGIES

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

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: 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

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: 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: 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: 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.