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Catalog Number: (MICRBKL993521IRB)
Supplier: MICRONOVA
Description: The unique LDPE/nylon laminate is a superb barrier material for lining totes to transport raw materials or to line buckets containing disinfectants or other cleaning solutions.
UOM: 1 * 24 items


Supplier: Ansell
Description: Cotton liner with teal nitrile coating for a better resistance to snags, punctures, abrasions and cuts when compared to ordinary cotton and string-knit gloves.

Supplier: NITRITEX
Description: These ambidextrous cleanroom gloves with beaded cuffs can be used in medical as well as in laboratory environments.

Supplier: HULME MARTIN HEAT SEALERS
Description: Heat sealer, bags, HM 2950

Supplier: Ansell
Description: This industrial work nylon glove with nitrile palm coating provides light mechanical protection with dexterity. Designed specifically for use in moderately oily manufacturing and maintenance environments.

Catalog Number: (115-3035)
Supplier: CONTEC
Description: The StatZorb wipe is made from polyester fabric combined with a conductive fibre knitted in a specially designed grid pattern that minimises 'hot spots'.
UOM: 1 * 1.800 items


Supplier: SEMADENI
Description: Clip, Clips for bags, polyamide, For: 220 mm wide bags

Supplier: Ansell
Description: Ambidextrous, light and stretchy gloves made from cotton.

Supplier: Ansell
Description: These cotton jersey gloves with nitrile coating effectively repel grease, oil and dirt and supersede the classic leather general purpose glove in medium-duty applications.

Supplier: Ansell
Description: These heavy duty gloves consist of two layers: The soft inner layer is made of acrylic terry and the 3/4 nitrile coating provides comfort and dexterity.

Supplier: ENZO LIFE SCIENCES
Description: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

Catalog Number: (ENZOADISPA8136D)
Supplier: ENZO LIFE SCIENCES
Description: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.
UOM: 1 * 50 µG


Supplier: Bel-Art Products, a Part of SP
Description: Autoclavable bags, in PP, 50 µm thick, transparent useful for discarding used Petri dishes, membrane filters, multi-well cell culture plates, cell culture flasks, culture plates, pipettes and more.

Supplier: Ansell
Description: This knitted spandex/nylon/Dyneema® glove with thin PU palm coating provides a high level of dexterity and tactility for applications with cut risks.

Supplier: ENZO LIFE SCIENCES
Description: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate binding domain of Hsd70 cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

Catalog Number: (129-0222)
Supplier: VWR Collection
Description: These high strength bags, made from PP, are ideal for hazardous waste collection and decontamination in an autoclave. Bags are formulated to withstand stress at the side seams and are strong enough to hold items in the laboratory. They are red and printed with a black biohazard symbol: 'Infectious Waste' and feature a temperature indicator patch.
UOM: 1 * 400 items


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organisation. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
Product(s) marked with this symbol are discontinued - sold till end of stock. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service on +353 1 8822222.
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