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Supplier: NITRITEX
Description: These cleanroom gloves with beaded cuffs can be used in medical as well as in laboratory environments. Suitable for double-donning.
Supplier: VWR Collection
Description: Polyester 2×8 strip films are identical to polyester films in material and adhesive, but designed for sealing only one or two 8-well rows at a time on either strip-well plates or standard plates whenever rows must be selectively protected or accessed. Sterile product is packed in tamper-evident bags of 50/bag.

Supplier: Greiner Bio-One
Description: PP with HDPE screw cap.
Supplier: CAMPING GAZ
Description: The Fold'N Cool™ soft foldable coolers are comfortable to carry and are available in various sizes and could be folded to store after use.

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: (112-9990)
Supplier: INSTRUMENTS FOR RESEARCH
Description: PE glove bag with inflatable glove chamber, Handy-Lok closure, turned in gloves and one equipment opening.
UOM: 1 * 1 items


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: VWR Collection
Description: 100% polyester string mops. Double clear poly bagged for cleanroom use. Good chemical sorbancy. Ideal for application of cleaning solutions on floors in critical environments.

Catalog Number: (BELAF132360000)
Supplier: Bel-Art Products, a Part of SP
Description: Safety pouch upright stand, bright orange, epoxy-coated steel wire, 100×130×200 mm
UOM: 1 * 1 items


Catalog Number: (BELAH132340000)
Supplier: Bel-Art Products, a Part of SP
Description: Hard to pierce pouch offering protection against the danger of being cut by contaminated sharp objects. Convenient for labs, clinics and medical offices. Used with the Poxygrid® safety pouch stand for easy benchtop collection.
UOM: 1 * 200 items


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: DAKLAPACK
Description: These pouches are intended for use as a one time use pouch for food and even non food products. The pouch is designed with an opening bottom gusset which means the pouch will stand up on its own.

Supplier: S▄DPACK MEDICA
Description: Tubular LDPE 80 µ pouches - pharma quality.
Supplier: DEUTSCH NEUMANN
Description: These are red natural rubber latex balloon suitable for rotary evaporators for mixing or collecting gas and for controlling air or gas flows at suitable equipment. It also features a tubing with length 140 mm and diameter 12 mm.

Supplier: NITRITEX
Description: BioClean Ultimate™ sterile cleanroom gloves are manufactured from polychloroprene and are hand-specific with a beaded cuff. They offer excellent cytotoxic protection with sensitivity.
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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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