11171 Results for: "Welch+by+Gardner+Denver&pageNo=17"

Supplier: Sartorius Balances

The Cubis® II laboratory balances are modular, providing choice between applications and configurations that best suit the users' needs. These balances can be configured at the level of display, draftshields, software applications and hardware functions. The Cubis® II range of high-capacity micro balances with a maximum load between 32 and 111 g and a readability between 0,001 mg and 0,002 mg provide the ideal choice for a broad range of applications.

Supplier: Merck

Fast method development of complex samples across the pH range from 1,5 to 10,5 with different mobile phases and temperature conditions.
Purospher® STAR RP-18 endcapped HPLC columns are designed for universal use. Basic, neutral and metal-chelating compounds can easily be separated with simple mobile phases – naturally without peak tailing. Thanks to its outstanding performance and stability, Purospher® STAR RP-18 endcapped offers maximum flexibility in method development. Robust methods can be developed over the entire pH range from 1,5 to 10,5. High pH-stability allows the separation of strongly basic compounds with alkaline eluents. The combination of high purity silica, best all-round retention characteristics, outstanding pH stability up to pH 10,5, and suitability for up to 100% aqueous mobile phases, make Purospher® STAR RP-18 endcapped an all-round top performance column, almost universal in its range of applications.

Supplier: NEUBERT VOLUME GLASSWAERE

Kurzschliff, Flachboden 1 * 1 items

Supplier: Lovibond Tintometer

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

Supplier: SARSTEDT

2ml Autoanalyser Sample Cups for Hitachi Analysers (Polystyrene) 38x17mm 1 * 5.000 items

Supplier: VWR Chemicals

VWR® dehydrated culture media that has been granulated offers both convenience and safety benefits. The correct dissolution of culture media is critical to achieving the best performance. Granulated culture media saves time in the preparation of ready to use culture media. In addition, granulation reduces dust generation, so handling the product is more pleasant and safer for the user, making it a much cleaner and safer working environment.

Supplier: WATERS

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

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: 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

Supplier: OriGene

Recombinant human HSD17B11 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. 1 * 100 µG

Supplier: DEUTSCH NEUMANN

HOLLOW STOPPERS NAT. RUBB. RED 19/17MM 1 * 100 items

Supplier: WATERS

Column AccQ-Tag Ultra C18 1.7um 2.1 x 100mm 1 * 1 items

Supplier: NEUBERT VOLUME GLASSWAERE

mit Kurzschliff Rundboden 24 x 2,5 100 mm 36,80 + - 0,10g 1 * 1 items

Supplier: DWK Life Sciences

Tube 50ml, round, 34x100mm, borosilicate3.3. 1 * 200 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: 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: LGC Standards PROMOCHEM

11-DEOXYCORTISOL (17,21-DIHYDROXYPREGN-4-ENE-3,20-DIONE) 1 * 10 mg

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: 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, stainless steel frame and a stainless steel (single range models) or aluminium load cell (dual range models). The front mounted 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: HWS LABORTECHNIK

O-RING 1 * 1 items

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: 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.
Please complete the quote request to enable us to assist you in finding the right unit for your application.
https://uk.cmd2.vwr.com/bin/public/fc/main?f=Y5&pimid=17028583

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.