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Catalog Number: (10110-140)
Supplier: Prosci
Description: Protein kinase activation is a frequent response of cells to treatment with growth factors, chemicals, heat shock, or apoptosis-inducing agents. This protein kinase activation presumably allows cells to resist unfavorable environmental conditions. The yeast 'sterile 20' (Ste20) kinase acts upstream of the mitogen-activated protein kinase (MAPK) cascade that is activated under a variety of stress conditions. MST2 was identified as a kinase that is activated by the proapoptotic agents straurosporine and FAS ligand.Protein kinase activation is a frequent response of cells to treatment with growth factors, chemicals, heat shock, or apoptosis-inducing agents. This protein kinase activation presumably allows cells to resist unfavorable environmental conditions. The yeast 'sterile 20' (Ste20) kinase acts upstream of the mitogen-activated protein kinase (MAPK) cascade that is activated under a variety of stress conditions. MST2 was identified as a kinase that is activated by the proapoptotic agents straurosporine and FAS ligand (MIM 134638) (Taylor et al., 1996 [PubMed 8816758]; Lee et al., 2001 [PubMed 11278283]).[supplied by OMIM]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. PRIMARYREFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP 1-11 U26424.1 1-11 12-2826 BC010640.2 1-2815


Catalog Number: (10408-928)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (95043-816)
Supplier: Enzo Life Sciences
Description: Hsp25 is a member of the family of small heat shock proteins (sHsps), an evolutionarily conserved family of stress proteins which exhibit moleclular weights between 14-45 kDa. The sHsps are related to the alpha-crystallins, and generally exist as large oligomeric complexes that serve to stabilize and assist in refolding of denatured proteins. Hsp25 is highly homologous to the human Hsp27, and its expression is seen in many species, including mouse, rat, bovine, canine, and hamster cells.

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Catalog Number: (10408-650)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (10408-644)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (10408-652)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (10408-654)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Supplier: JULABO
Description: An entirely new generation of highly dynamic temperature control systems by JULABO. The new PRESTO® systems are designed for precise temperature control as well as rapid temperature changes, making them ideal for reactor vessels, material stress tests, or temperature simulations.

Catalog Number: (10070-654)
Supplier: Prosci
Description: PRAK (p38-regulated /activated kinase), also referred to as mitogen-activated protein kinase (MAPK)-activated protein kinase (MAPKAPK)-5, is an ubiquitously expressed serine/threonine kinase regulated by p38beta and p38beta MAP kinases. Activated JNK, p38gamma or p38δ are unable to induce phosphorylation of PRAK in vitro. Phosphorylation of PRAK occurs in vivo in response to p38 activation by stress-related extracellular stimuli including UV light, oxidation and proinflammatory cytokines. Two other substrates for p38, MAPKAPK-2 and MAPKAPK-3/3pK, share approximately 45% sequence homology with PRAK including the phosphorylation motif recognized by p38, Lys-X-Thr-Pro. Activated PRAK has been shown to specifically phosphorylate HSP 27 in vitro, suggesting that the protein may play a role in stress-induced small heat shock protein phosphorylation in vivo.


Catalog Number: (10408-648)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (10408-646)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (10800-824)
Supplier: Rockland Immunochemical
Description: c-Jun is a proto-oncogene that forms a complex with c-Fos which regulates transcription from promoters containing AP-1 activation elements (1). c-Jun has specific DNA binding activity and following in vitro translation, c-Jun binds as a homodimer to the AP-1 DNA site. The transactivating function of c-Jun is acutely regulated by a wide variety of cellular signals via modulation of phosphorylation of two serines (63 and 73). Jun N-terminal domain kinases (JNKs), are responsible for mediating S63/73 phosphorylation on c-Jun in response to a variety of cellular stimuli including TNF-a, heat stress and u.v. light (2). c-JUN Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Apoptosis/Autophagy, Cardiovascular Disease, Cellular Stress, Inflammation, JNK/SAPK Pathway, Neurobiology, and NfkB Pathway research.


Catalog Number: (76079-764)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (10814-034)
Supplier: Prosci
Description: This gene encodes a member of the Ser/Thr protein kinase family. This kinase is regulated through direct phosphorylation by p38 MAP kinase. In conjunction with p38 MAP kinase, this kinase is known to be involved in many cellular processes including stress and inflammatory responses, nuclear export, gene expression regulation and cell proliferation. Heat shock protein HSP27 was shown to be one of the substrates of this kinase in vivo. Two transcript variants encoding two different isoforms have been found for this gene.


Catalog Number: (10070-936)
Supplier: Prosci
Description: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells By similarity. Phosphorylates heat shock factor protein 4 (HSF4). /Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells. JNK2 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to c-Jun, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it./Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. Required for stress-induced neuronal apoptosis and the pathogenesis of glutamate excitotoxicity


Catalog Number: (10104-338)
Supplier: Prosci
Description: HSPA2 belongs to the heat shock protein 70 family.In cooperation with other chaperones, HSPA2 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.


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