10831 Results for: "4-Chloro-2-nitrobenzaldehyde&pageNo=17"

Supplier: HELLMA

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

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

These Nunc™ cell culture flasks are designed for culture consistency, cell health, and reproducibility. Choose from a variety of surfaces and sizes with culture areas ranging from 25 to 500 cm² to suit your specific applications and cell types.

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: Rubbermaid Commercial Products

Highly durable waste containers created with the toughest enviroments in mind.

Supplier: Ansell

Nylon supported neoprene gloves that provide broad chemical protection with enhanced comfort and tactility.

Supplier: Merck

All Spectroquant® test kits can be used with the Prove range of spectrophotometers and Nova 60/60A instruments. Tests can be used not only on photometers and spectrophotometer from Merck, but also on photometers and spectrophotometers from other suppliers (programming details available on request). Spectroquant® cell test kits.

Supplier: Merck

The selectivity offered by ZIC®-HILIC is suitable for a wide variety of molecules containing hydrophilic or ionisable functional groups. This includes compounds such as carbohydrates, metabolites, acids and bases, organic and inorganic ions, metal complexes, amino acids, peptides, protein digests, plant and cell extracts, plus much more. Such compounds are normally characterised by a small or negative LogP value and have poor retention on reversed-phase columns.

Supplier: Greiner Bio-One

EDTA tubes are ideal for the examination of whole blood in haematology and are offered as either K2EDTA or K3EDTA tubes.

Supplier: SIOEN

Multifunctional breathable jacket made of Siopor® Ultra (100% polyester fabric with 100% PU coating) that can be used in all weather conditions. The outer fabric is water-repellent and windproof while the coating on the inside is moisture attracting. With fixed lining, knitted wind cuffs in sleeves and taped 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: 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: Greiner Bio-One

MiniCollect® offers a gentle way to collect small blood samples for a wide range of analyses for young children, geriatric patients as well as patients with fragile veins.

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: MILLIPORE

MultiScreenHTS plates are specifically developed for high-throughput use with automated work stations. Rigid sidewalls improve handling and ample surfaces are provided for bar code labels. Wells are individually sealed to prevent incubation crosstalk and the underdrain is removable for access to the filters. Filter plates are available in 96- and 384-well platforms with a broad selection of membranes and plastics.

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: 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: 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: 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: HELLMA

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

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: 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.

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.