11446 Results for: "6-(Aminomethyl)benzoxazole+hydrochloride&pageNo=17"

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: CPACHEM

TRIBROMOMETHANE CRM ISO/IEC 17025/17034 1 * 1 mL

Supplier: CPACHEM

SODIUM CHLORIDE 99.995% ISO 17035 17025 1 * 50 g

Supplier: WATER ID PRIMELAB

25 TUBETESTS COD HR (0 - 15000 MG/L) 1 * 25 Vial

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: ERLAB CAPTAIRE

The Captair® Smart filtering chemical storage cabinets are designed with a simple and innovative way of communication. Smart Technology uses simple light to show that the unit is operating safely so the user can focus his attention on what is most important: his work. Smart Technology enables visual light to indicate the hood status. A simple light pattern indicates if the air flow is compromised, if there is a fan failure, a filter breakthrough or if the doors are open.
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https://uk.cmd2.vwr.com/bin/public/fc/main?f=Y5&pimid=17028583

Supplier: DWK Life Sciences

TISSUE GRINDER 0.3ML MICRO DUAL ALLGLASS 1 * 1 items

Supplier: KOEHLER TECHNISCHE PRODUKTEN

transparente Dose, blauer Deckel 1 * 1 items

Supplier: RPB SAFETY

The RPB PX5 is a battery powered air purifying respirator fan unit which draws in contaminated air from the wearer’s immediate vicinity, passing it through internal filters, and supplying the filtered air to an approved RPB loose fitting respirator head top.

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: EPPENDORF

This centrifuge features a superior capacity of up to 4×1000 ml which makes it the ideal instrument for high-throughput and large volume applications. It has a powerful refrigeration system with advanced temperature management to keep samples safe.

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: CPACHEM

POTASSIUM NITRATE (V) 1 MOL/L ISO 17034 1 * 1 L

Supplier: Lovibond Tintometer

Filter Set 3000 Comp. Gardner (TINT 342000 ) 1 * 1 items

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: NEUBERT VOLUME GLASSWAERE

Kurzschliff, Flachboden 1 * 1 items

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: 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: CUSTOM MADE CHEMICALS LAB

10mg/l each of Ag As Ba Cd Co Cr Cu Hg Li Ni Pb Sb Se Sn Tl V Mo 1 * 100 mL

Supplier: EPPENDORF

Eppendorf epT.I.P.S.® Reloads offer high-precision pipette tips in 'Eppendorf Quality' and 'PCR clean' purity grades. Eco-friendly, cost-effective, and designed for seamless compatibility with Eppendorf Box 2.0, they ensure accuracy and sustainability in labs.

Supplier: HORIBA

These waterproof meters can measure and display up to 11 parameters simultaneously with one single probe. Thanks to their rugged design and their field replaceable sensors they are ideal for outdoor use, for example, when testing ground or surface water. Their compact size and the hand strap enable one-handed operation.

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: WATERS

Column Acquity BEH C18 VanGuard Pre-column 1.7um 2.1 x 5mm 1 * 3 items

Supplier: Lovibond Tintometer

4/49 I.F.U. Disc (TINT 244900 ) 1 * 1 items

Supplier: Lovibond Tintometer

4/50 I.F.U. Disc (TINT 244700 ) 1 * 1 items