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Product Image-CA95057-938

Anti-HSP90 Rabbit Polyclonal Antibody

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-CA95045-172

Anti-HSPA8 Mouse Monoclonal Antibody

Supplier: Enzo Life Sciences
Description: The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

SDS

Product Image-CA200062-728

Anti-HSPA8 Mouse Monoclonal Antibody

Supplier: Enzo Life Sciences
Description: The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Product Image-76443-186

Forced Convection Cleanroom Ovens, DES and DTS Series, Yamato

Supplier: Yamato Scientific
Description: These forced convection cleanroom ovens feature space saving, large volume class 100 clean oven.

Irregular Voltage

Image Unavailable-89359-682

Anti-HSP90 Rat Monoclonal Antibody [clone: 2D12]

Catalog Number: (89359-682)
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.
Image Unavailable-10354-044

Anti-HSPB1 Rabbit Polyclonal Antibody (Cy3®)

Catalog Number: (10354-044)
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. [provided by RefSeq]. Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.
Image Unavailable-10354-530

Anti-HSPB1 Rabbit Polyclonal Antibody (Cy7®)

Catalog Number: (10354-530)
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. [provided by RefSeq]. Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.
Image Unavailable-10094-114

Anti-SAFB Rabbit Polyclonal Antibody

Catalog Number: (10094-114)
Supplier: Proteintech
Description: Heterogeneous nuclear ribonucleoproteins (hnRNPs) constitute a set of polypeptides that contribute to pre-mRNA processing and transport. hnRNPs also bind heterogeneous nuclear RNA (hnRNA), the transcripts produced by RNA polymerase II. SAFB (scaffold attachment factor B) is a nuclear matrix-associated protein that binds to matrix- or scaffold-associating regions (MARs or SARs) on DNA and interacts with RNA polymerase II and serine-/arginine-rich RNA processing factors (SR proteins). SAFB, also designated HAP (hnRNP A1 associated protein) and HET (HSP 27-ERE-TATA-binding protein) is a proven hnRNP protein that has a speckled distribution in the nucleus and, in response to stress agents such as heat shock, is recruited to a few, large nuclear granules, called perichromatin granules. SAFB also binds to the estrogen receptor (ER) and is expressed in several breast cancer cell lines at varying levels. Subsequently, SAFB may play a role in breast cancer by mediating cellular proliferation and division. This antibody specifically reacts whith the isoform 1 of human SAFB protein.
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-89142-092

Anti-HSP90 Mouse Monoclonal Antibody (PE (Phycoerythrin))

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.

Product Image-CA200062-752

Anti-HSP90 Mouse Monoclonal Antibody

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.

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-CA76472-490

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.

Product Image-CA76472-510

Laboratory Glassware Washers, Model PLW 8617, Miele

Supplier: Miele
Description: The PLW 8617 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 single door, 1150 mm (3' 91/4") wide, a usable capacity of 351 litres. PLW 8617 provides reliable results, high pump performance with a variable-speed pump and features spray arm monitoring and a conductivity meter.

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.
Product Image-CA76472-482

Laboratory Glassware Washers, PLW 8615, Miele

Supplier: Miele
Description: The PLW 8615 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 single door, 900 mm wide, a usable capacity of 351 litres. PLW 8615 provides reliable results, high pump performance with a variable-speed pump and features spray arm monitoring and a conductivity meter.

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