Print…

You Searched For: Heat+Stress+Meters


12,459  results were found

Refine Results Sort by
SearchResultCount:"12459"

Sort Results

List View Easy View

Rate These Search Results

Product Image-95043-782

Anti-HSP90B1 Rat Monoclonal Antibody [clone: 9G10]

Catalog Number: (95043-782)
Supplier: Enzo Life Sciences
Description: Glucose-regulated protein 94 (Grp94, gp96), an abundant resident endoplasmic reticulum (ER) lumenal stress protein, belongs to the Hsp90 family of molecular chaperones along with cytosolic Hsp90. Grp94 and such other resident soluble proteins of the ER as the Ca 2+ binding protein subfamily (CaBP, CaBPI, CaBP2 and calreticulin) possess the C-terminal tetrapeptide Lys-Asp-Glu-Leu (KDEL), a sorting signal considered responsible for the retention of these proteins in the pre-Golgi compartments. Stress conditions such as glucose starvation and heat shock which promote protein misfolding or unfolding increase Grp94 expression. In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. Grp94 and Hsp90 share high sequence identity and apparently identical adenosine nucleotide dependent modes of regulation, although previous data suggests that Hsp90 and Grp94 may differ in their nucleotide binding properties. The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket which also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol. However, the molecular basis for adenosine nucleotide-dependent regulation of Grp94 remains unclear. Data supports a ligand dependent regulation of Grp94 function, and suggests a model whereby Grp94 function is regulated through a ligand -dependent conversion of Grp94 from an inactive to an active conformation.
Product Image-95042-198

Anti-HSP90 Rabbit Polyclonal Antibody

Catalog Number: (95042-198)
Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

SDS


Image Unavailable-76083-602

Anti-HSP27 Ser82 Rabbit Polyclonal Antibody (Alexa Fluor® 750)

Catalog Number: (76083-602)
Supplier: Bioss
Description: The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined.
Product Image-89106-716

Anti-HSP90 Mouse Monoclonal Antibody (DyLight® 488)

Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

SDS

Product Image-10049-542

Anti-TRAP1 Mouse Monoclonal Antibody [clone: 9B6]

Catalog Number: (10049-542)
Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress. It includes cytoplasmic (Hsp90-alpha/beta), ER (Grp94) and mitochondrial (TRAP1) localized members. Hsp90 is structurally composed of an N-terminal ATP binding domain, a medial substrate-binding region, and a C-terminal dimerization motif.  Hsp90 dimers function in cooperation with cochaperones to stabilize a multitude of client protein substrates. TRAP1 (aka Hsp75) was originally identified as a chaperone binding partner for retinoblastoma protein. TRAP1 was later found by immunofluorescence to be localized to the mitochondria. TRAP1 is significantly more active as an ATPase due in part to the lack of regulatory elements in the C-terminus, but retains the ability to dimerize. However, it does not form stable complexes with typical cochaperones of Hsp90 like p23 and HOP4. Recently TRAP1 has been identified as a protective element for cell survival, and has been suggested as a novel target for anti-cancer therapeutics.
Product Image-89135-328

Anti-HSP90B Rabbit Polyclonal Antibody

Supplier: Enzo Life Sciences
Description: The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells express inducible Hsp90 alpha and constitutive Hsp90 beta isoforms that are encoded by separate genes. The amino acid sequences of human and yeast Hsp90 alpha are 85% and 90% homologous to those of Hsp90 beta, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular protein in most cells. Hsp90 functions as part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control by serving as a chaperone for many key signaling molecules including steroid receptors, cell cycle kinases involved in signal transduction, and p53. As many of these client proteins are known oncogenes, Hsp90 inhibitors such as 17-AAG, a geldanamycin analog, have been of benefit in the treatment of many cancers.

Product Image-95043-824

Anti-HSP60 Rabbit Polyclonal Antibody

Supplier: Enzo Life Sciences
Description: The Hsp60 of Heliothis viescens belongs to a highly conserved family of molecular chaperones from several species, including plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60, and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix, and in plants Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria share a common ancestry (>1 billion years), and this coupled with the high degree of homology between the divergent Hsp60s suggests that these proteins perform a primitive but vital function similar to all the different species. The common characteristics shared by the Hsp60s from the divergent species include high abundance; induction with environmental stress such as heat shock; homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP; ATPase activity; and a role in folding and assembly of oligomeric protein structures. Studies support these similarities, showing expression of the single-ring human mitochondrial homolog Hsp60 with its co-chaperonin Hsp10, in a E. coli strain engineered so that the groE operon remained under strict regulatory control. The findings demonstrate that expression of Hsp60-Hsp10 enabled successful performance of all essential in vivo functions of GroEL and its co-chaperonin, GroES. Consistent with their functions as chaperones, Hsp60 and Hsp10 may act as docking molecules with a passive role in the maturation of caspase processing. Data incidates that recombinant Hsp60 and Hsp10 accelerate the activation of procaspase-3 by cytochrome c and dATP in an ATP-dependent manner. Hsps are intracellular proteins thought to serve protective functions against infection and cellular stress; however, several studies reveal a possible link between members of the Hsp60 and a number of autoimmune diseases, atherosclerosis, and chlamydial disease.

SDS

Image Unavailable-10233-892

Anti-HSPA1A Rabbit Polyclonal Antibody (Cy5.5®)

Catalog Number: (10233-892)
Supplier: Bioss
Description: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
Product Image-10049-514

Anti-HSP90A Mouse Monoclonal Antibody [clone: K41009]

Catalog Number: (10049-514)
Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90α/β), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.
Product Image-10861-736

MB120 Halogen Moisture Analyzer, OHAUS

Catalog Number: (10861-736)
Supplier: Ohaus
Description: The MB120 delivers functionality and precision that you can rely on, and is easy to operate and clean—you can test more samples in less time! Advanced features such as a temperature guide help to analyze optimum drying temperature, and methods and results storage allows statistical analysis of measurements. Three levels of user management ensure data safety—set up and lock temperature settings and method parameters with administrator access.

UL Listed cUL Listed CSA Certified


Product Image-10049-548

Anti-HSP90A Rabbit Polyclonal Antibody

Catalog Number: (10049-548)
Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.
Image Unavailable-100243-740

Anti-BiP Rat Monoclonal Antibody [clone: 76-E6]

Catalog Number: (100243-740)
Supplier: Southern Biotechnology
Description: The immunoglobulin heavy chain binding protein BiP is a member of the hsp70 family of heat shock proteins and is identical to the glucose regulated protein GRP78. While BiP was originally described for its function in B cells, it is now known to be distributed in a variety of tissues, if not ubiquitous. The highly conserved hsp70 proteins have an essential physiological role in stress responses and as “molecular chaperones” which are responsible for a variety of functions such as protein transport, prevention of protein toxicity and direction of protein folding. With regard to its immunological role, BiP is a component of the endoplasmic reticulum and binds free intracellular heavy chains in nonsecreting pre-B cell lines (μ+,L-) or incompletely assembled Ig precursors in H+L+ secreting hybridomas and myelomas. In the absence of light chain synthesis, heavy chains remain associated with BiP and are not secreted. BiP is an ATP binding protein and the dissociation of the BiP-heavy chain complex is probably driven by the ATPase activity attributed to BiP. The monoclonal antibody 76-E6 recognizes a conserved epitope localized within the region of amino acids 497 to 581 of BiP.
Image Unavailable-76083-600

Anti-HSP27 Ser82 Rabbit Polyclonal Antibody (Alexa Fluor® 680)

Catalog Number: (76083-600)
Supplier: Bioss
Description: The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined.
Image Unavailable-89359-690

Anti-HSP90 Mouse Monoclonal Antibody [clone: AC88]

Catalog Number: (89359-690)
Supplier: Genetex
Description: The 90kDa molecular chaperone family comprises several proteins including the 90kDa heat shock protein, Hsp90 and the 94kDa glucose regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90a and hsp90s which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90a is 85% and 90% homologous to that of Hsp90s respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N terminal and C terminal regions which have been shown to contain independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 is part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by nonphysiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context several key regulatory proteins such as steriod receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90. It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways.
Product Image-89009-519

ErgoSCRUB® Scrubbing Handles and ScrubDISK® Pads, Foamtec International

Supplier: Foamtec International
Description: Ergonomically correct, disposable, and reusable scrubbing handles and pads for cleaning critical surfaces on process equipment in the semiconductor, flat-panel display, optical component, and hard disk drive industries.

Certificates

Product Image-76402-686

Laboratory Glassware Washers, PLW 8616, Miele

Supplier: Miele
Description: The PLW 8616 laboratory washer can accommodate 216 laboratory flasks, 588 vials, or 294 pipettes. The large glassware washer is flexible and simple to use, it has modular load carriers and SimpleLoad system. This efficient unit has a double door, 900 mm wide, a usable capacity of 351 litres. PLW 8616 provides reliable results, high pump performance with a variable-speed pump and features spray arm monitoring and a conductivity meter.

Inquire for Price
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 at 1-800-932-5000.
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 at 1-800-932-5000.
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 Regulatory_Affairs@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 organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
241 - 256 of 12,459
no targeter for Bottom