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Catalog Number: (89415-552)
Supplier: Prosci
Description: p53DINP1 Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible gene was identified recently and designated p53DINP1 (for p53-dependent damage-inducible nuclear protein 1) and SIP (for stress induced protein) in human and mouse. A p53DINP1 antisense oligonucleotide inhibits and overexpression of p53DINP1 enhances Ser46 phosphorylation of p53, induction of p53AIP1, and cell death induced by DNA double-strand breaks. p53DINP1 may regulate p53-dependent apoptosis through phosphorylation at Ser46 and induction of p53AIP1. The p53DINP1/SIP gene encodes two proteins of 27 and 18 kDa in human and mouse termed p53DINP1-alpha and p53DINP1-beta or SIP27 and SIP18. p53DINP1/SIP is expressed in many tissues and induced by a variety of stress agents including UV stress, mutagenic stress, heat shock, and oxidative stress.


Catalog Number: (10749-518)
Supplier: Prosci
Description: p53DINP1 Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible gene was identified recently and designated p53DINP1 (for p53-dependent damage-inducible nuclear protein 1) and SIP (for stress induced protein) in human and mouse. A p53DINP1 antisense oligonucleotide inhibits and overexpression of p53DINP1 enhances Ser46 phosphorylation of p53, induction of p53AIP1, and cell death induced by DNA double-strand breaks. p53DINP1 may regulate p53-dependent apoptosis through phosphorylation at Ser46 and induction of p53AIP1. The p53DINP1/SIP gene encodes two proteins of 27 and 18 kDa in human and mouse termed p53DINP1-alpha and p53DINP1-beta or SIP27 and SIP18. p53DINP1/SIP is expressed in many tissues and induced by a variety of stress agents including UV stress, mutagenic stress, heat shock, and oxidative stress.


Catalog Number: (77438-268)
Supplier: Bioss
Description: Reactive oxygen species (ROS) are highly reactive molecules that are a normal consequence of aerobic metabolism. Cellular ROS damage can induce apoptosis and spontaneous mutagenesis. Oxr1 (Oxidation resistance protein 1) is a 758 amino acid mitochondrial protein that is most likely involved in protection from oxidative damage. Oxr1 is highly conserved from yeast to humans and is specific to eukaryotes.Induced by heat and oxidative stress, the carboxyl-terminal half of Oxr1 is required for its function. Upregulation of superoxide dismutase and catalase was observed in developing drosophila mutants that lacked the gene encoding Oxr1, suggesting that oxidative stress may trigger compensatory protein expression. There are four isoforms of Oxr1 that are produced as a result of alternative splicing events.


Catalog Number: (76193-812)
Supplier: Prosci
Description: First described in relation to heat shock, HSPs are now known to be produced in response to additional stressful conditions including cold and UV light, as well as during wound healing. Heat shock protein 60 (HSP60) is responsible for protein transportation from the cytoplasm to the mitochondrial matrix and the subsequent refolding of the transported proteins. HSP60 also functions as a molecular chaperone, or chaperonin, assisting linear amino acid chains to fold into their three-dimensional structure.


Catalog Number: (89359-280)
Supplier: Genetex
Description: Heme oxygenase (HO) is a microsomal enzyme that catalyzes the oxidation of heme to the antioxidant molecules, biliverdin and carbon monoxide. HO consists of two homologous isozymes, an inducible HO1 and a constitutively expressed HO2. HO1 is induced by a wide variety of stimuli including conditions of oxidative stress, inflammatory agents, transforming growth factor beta and heat shock. The increase in expression of HO1 is thought to be a cellular defense mechanism against oxidative stress since elevated HO could eventually generate more bilirubin, an anti-oxidant.


Supplier: Diagnostic Biosystems
Description: This antibody is specific to constitutive (HSP73) and inducible (HSP72) form of HSP70. HSP70 is found to be associated with steroid receptors, actin, P53, polyoma T antigen, nucleotides and other known proteins. HSP70 has been shown to be involved in protective roles against thermal stress, cytotoxic drugs and other damaging conditions.

Supplier: Enzo Life Sciences
Description: FKBP59, also known as Hsp56/p59 is an immunophilin that is a component of Hsp70/Hsp90/steroid receptor complexes. Expression of FKBP59 is increased in response to heat shock and ischemic stress, and is thought to play a role in the folding and cytoplasmic/nuclear distribution of steroid receptors.

Catalog Number: (75930-712)
Supplier: Rockland Immunochemical
Description: p53DINP1 antibody detects human p53DINP1. Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible gene was identified recently and designated p53DINP1 (for p53-dependent damage-inducible nuclear protein 1) and SIP (for stress induced protein) in human and mouse. A p53DINP1 antisense oligonucleotide inhibits and overexpression of p53DINP1 enhances Ser46 phosphorylation of p53, induction of p53AIP1, and cell death induced by DNA double-strand breaks. p53DINP1 may regulate p53-dependent apoptosis through phosphorylation at Ser46 and induction of p53AIP1. The p53DINP1/SIP gene encodes two proteins of 27 and 18 kDa in human and mouse termed p53DINP1-alpha and p53DINP1-beta or SIP27 and SIP18. p53DINP1/SIP is expressed in many tissues and induced by a variety of stress agents including UV stress, mutagenic stress, heat shock, and oxidative stress. Anti-p53DINP1 antibodies are ideal for investigators involved in Apoptosis and Cancer research.


Catalog Number: (75934-608)
Supplier: Rockland Immunochemical
Description: HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function (2). The up-regulation of HSP (heat shock proteins) expression by stressors is achieved at the level of transcription through a heat shock element (HSE) and a transcription factor (HSF) (3, 4, 5). Most HSFs have highly conserved amino acid sequences. On all HSFs there is a DNA binding domain at the N-terminus. Hydrophobic repeats located adjacent to this binding domain are essential for the formation of active trimers. Towards the C-terminal region another short hydrophobic repeat exists, and is thought to be necessary for suppression of trimerization (6). There are two main heat shock factors, 1 and 2. Mouse HSF1 exists as two isoforms, however in higher eukaryotes HSF1 is found in a diffuse cytoplasmic and nuclear distribution in un-stressed cells. Once exposed to a multitude of stressors, it localizes to discrete nuclear granules within seconds. As it recovers from stress, HSF1 dissipates from these granules to a diffuse nuceloplasmic distribution. HSF2 on the other hand is similar to mouse HSF1, as it exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form (7, 8). Various experiments have suggested that HFS2 may have roles in differentiation and development (9, 10, 11). Anti-HSF1 Antibody is ideal for research in Genetics, Transcription, Cell Signaling and pathways including ERK and MAPK.


Catalog Number: (75928-594)
Supplier: Rockland Immunochemical
Description: HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function (2). The up-regulation of HSP (heat shock proteins) expression by stressors is achieved at the level of transcription through a heat shock element (HSE) and a transcription factor (HSF) (3, 4, 5). Most HSFs have highly conserved amino acid sequences. On all HSFs there is a DNA binding domain at the N-terminus. Hydrophobic repeats located adjacent to this binding domain are essential for the formation of active trimers. Towards the C-terminal region another short hydrophobic repeat exists, and is thought to be necessary for suppression of trimerization (6). There are two main heat shock factors, 1 and 2. Mouse HSF1 exists as two isoforms, however in higher eukaryotes HSF1 is found in a diffuse cytoplasmic and nuclear distribution in un-stressed cells. Once exposed to a multitude of stressors, it localizes to discrete nuclear granules within seconds. As it recovers from stress, HSF1 dissipates from these granules to a diffuse nuceloplasmic distribution. HSF2 on the other hand is similar to mouse HSF1, as it exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form (7, 8). Various experiments have suggested that HFS2 may have roles in differentiation and development (9, 10, 11). Anti-HSF1 Antibody is ideal for research in Genetics, Transcription, Cell Signaling and pathways including ERK and MAPK.


Catalog Number: (200062-774)
Supplier: Enzo Life Sciences
Description: Grp94 (Glucose-regulated protein 94) is an abundant resident endoplasmic reticulum (ER) lumenal stress protein, which together with cytosolic Hsp90 belongs to the Hsp90 family of molecular chaperones. Grp94 expression is upregulated by stress conditions such as glucose starvation and heat shock, which promote protein misfolding or unfolding. 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.


Catalog Number: (75790-844)
Supplier: Prosci
Description: DnaJ Homolog Subfamily B Member 1 (DNAJB1) is a member of the heat shock protein family. Heat shock proteins (HSPs) are a highly conserved family of stress response proteins. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. DNAJB1 regulates cellular processes by aiding in the folding, transport and assembly. DNAJB1 contains a J-domain which controls interaction with the ATPase domain of DnaK. DNAJB1 interacts with HSP70 and can stimulate its ATPase activity. In addition, DNAJB1 stimulates the association between HSC70 and HIP.


Catalog Number: (76118-332)
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. Sequence similarities Belongs to the heat shock protein 70 family.


Supplier: Sper Scientific
Description: Wide Range Pressure Meter covers a wide pressure range, 0–725psi, not usually found in a single manometer

Catalog Number: (10800-928)
Supplier: Rockland Immunochemical
Description: CRYAA or crystallin alpha A is the major protein components of the vertebrate eye lens which is composed of 2 primary gene products--alpha-A and alpha-B. CRYAA can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family (1). CRYAA plays an important role in the normal embryologic development of the anterior segment of the eye. In the Elo mouse, a 1-bp deletion in the gamma-E-crystallin gene causes autosomal dominant cataract and microphthalmia (2). CRYAA Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Cancer, Metabolic Disorder, and Neurobiology research.


Catalog Number: (76193-814)
Supplier: Prosci
Description: First described in relation to heat shock, HSPs are now known to be produced in response to additional stressful conditions including cold and UV light, as well as during wound healing. Heat shock protein 60 (HSP60) is responsible for protein transportation from the cytoplasm to the mitochondrial matrix and the subsequent refolding of the transported proteins. HSP60 also functions as a molecular chaperone, or chaperonin, assisting linear amino acid chains to fold into their three-dimensional structure.


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