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Supplier: Enzo Life Sciences
Description: Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.

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: (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.


Catalog Number: (89359-730)
Supplier: Genetex
Description: In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. One class of stress proteins, termed the Hsp70 family, is comprised of multiple members, all of which bind ATPin vitro, but which are localized within different intracellular compartments. These include: i) Hsc70 (or constitutive form) present within the cytosol/nucleus; ii) Hsp70 (inducible form) present within the cytosol/nucleus/nucleolus; iii) the constitutive glucose-regulated 78 kDa (or BiP) protein present within the lumen of the endoplasmic reticulum; and iv) the constitutive glucose regulated 75 kDa protein present within the mitochondrial matrix. Members of the Hsp70 family are thought to function as molecular chaperones, assisting in the folding of other proteins in various intracellular compartments. Grp75 is localized in the mitochondrial matrix, where, in concert with Hsp60, is thought to participate in the re-folding of proteins translocated into this organelle. Like its E. coli homolog DnaK, Grp75 possesses a cation-dependent ATPase activity thought to be central to its function as a chaperone.


Supplier: Enzo Life Sciences
Description: Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.

Catalog Number: (10049-488)
Supplier: Enzo Life Sciences
Description: Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.


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: (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: (10408-650)
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: (10408-652)
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.


Catalog Number: (76083-732)
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.


Catalog Number: (103408-668)
Supplier: Novus Biologicals
Description: The HspA4L Antibody from Novus Biologicals is a goat polyclonal antibody to HspA4L. This antibody reacts with human. The HspA4L Antibody has been validated for the following applications: Peptide ELISA.


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.


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