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Catalog Number: (10326-328)
Supplier: Bioss
Description: Hsp20 is a small heat shock protein related to Hsp25, Hsp27 and may form different hetercomplexes with these proteins. The specific physiological function of Hsp20 is not yet known. It is distributed ubiquitously in tissues, but is found in higher levels in skeletal, smooth and heart muscle. Under normal conditions, Hsp20 is diffusely distributed in the cytosol, but under heat stress conditions, it translocates to the nucleus. Unlike other heat shock proteins the amount of Hsp20 does not increase after heat shock. The Hsp20 was demonstrated to constitute up to 1.3% of the total cellular protein in vertebrate tissues, especially in muscle, and its expression is related to muscle contraction, specifically in slow-twitch muscle. Hsp20 may form different heterocomplexes with other Hsp's, such as alpha-crystalline and Hsp25. Phosphorylated form of Hsp20 is proposed to interact with monomeric actin whereas dephosphorylated form binds polymeric actin filaments. In normal conditions Hsp20 is diffusely disturbed in cytosol but under the heat stress it undergoes translocation to membrane fraction.


Catalog Number: (75953-498)
Supplier: Biotium
Description: This antibody recognizes a 60 kDa protein, identified as the heat shock protein 60 (hsp60). A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (HSPs), more appropriately called as stress response proteins (SRPs). Hsp60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial hsp60, but also against its mammalian homolog.


Catalog Number: (10325-622)
Supplier: Bioss
Description: Hsp20 is a small heat shock protein related to Hsp25, Hsp27 and may form different hetercomplexes with these proteins. The specific physiological function of Hsp20 is not yet known. It is distributed ubiquitously in tissues, but is found in higher levels in skeletal, smooth and heart muscle. Under normal conditions, Hsp20 is diffusely distributed in the cytosol, but under heat stress conditions, it translocates to the nucleus. Unlike other heat shock proteins the amount of Hsp20 does not increase after heat shock. The Hsp20 was demonstrated to constitute up to 1.3% of the total cellular protein in vertebrate tissues, especially in muscle, and its expression is related to muscle contraction, specifically in slow-twitch muscle. Hsp20 may form different heterocomplexes with other Hsp's, such as alpha-crystalline and Hsp25. Phosphorylated form of Hsp20 is proposed to interact with monomeric actin whereas dephosphorylated form binds polymeric actin filaments. In normal conditions Hsp20 is diffusely disturbed in cytosol but under the heat stress it undergoes translocation to membrane fraction.


Catalog Number: (10820-448)
Supplier: Mettler Toledo
Description: The HC103 halogen moisture analyzer combines fast halogen heating with proven weighing technology to create a compact and durable instrument ideal for laboratory and production environments. Halogen heating element.

UL Listed CSA Certified


Catalog Number: (76262-728)
Supplier: Rockland Immunochemical
Description: Anti-HSF1 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Heat shock factor 1 (HSF1) is a highly conserved transcription factor that coordinates stress-induced transcription and directs versatile physiological processes in eukaryotes. Upon stress, HSF1 is the key transcriptional activator of chaperones, co-chaperones and ubiquitin, and also coordinates the expression of many transcriptional and translational regulators, signaling molecules and mitotic determinants. HSF1 is involved in balancing core cellular processes during stress and enables their rapid re-establishment once conditions suitable for proliferation have been restored. Importantly, HSF1 controls a distinct set of target genes in cell stress, development and cancer progression. The central role of HSF1 in diverse cellular functions is reflected in pathologies, such as neurodegenerative diseases and cancer, where an imbalance in HSF1 activity facilitates disease onset. The ability of cancer cells to harness HSF1 for metastatic progression highlights the plasticity of HSF1 in rewiring transcription and coordinating cellular processes. Anti-HSF1 antibody is thus ideal for investigators involved in cancer research and neurodegenerative diseases.


Supplier: Biotium
Description: This antibody recognizes a 60 kDa protein, identified as the heat shock protein 60 (hsp60). A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (HSPs), more appropriately called as stress response proteins (SRPs). Hsp60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial hsp60, but also against its mammalian homolog.

Supplier: Bio-Serv
Description: Chewable, flavored, medicated tablet replaces more stressful dosing methods.

Catalog Number: (75790-712)
Supplier: Prosci
Description: Alpha-Crystallin A Chain (CRYAA) belongs to the small heat shock protein (HSP20) family and can be induced by heat shock. The expression of CRYAA is preferentially restricted to the lens cell. CRYAA may contribute to the transparency and refractive index of the lens. CRYAA has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Two additional functions of CRYAA are an autokinase activity and participation in the intracellular architecture.


Catalog Number: (10067-460)
Supplier: Thermo Scientific Chemicals
Description: Herbimycin A is a sparingly soluble benzoquinone anti-tumor agent which interacts with the stress induced chaperone protein Hsp90 (heat shock protein 90).

Catalog Number: (10449-370)
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.


Catalog Number: (10449-368)
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.


Catalog Number: (76193-872)
Supplier: Prosci
Description: This antibody recognizes a 60kDa protein, identified as the heat shock protein 60. The antibody's epitope is localized between amino acids 383-447 of human HSP60. A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (hsp’s), more appropriately called as stress response proteins (srp’s). HSP60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial HSP60, but also against its mammalian homolog. Clone LK1 antibody, unlike LK2 antibody, recognizes only the mammalian (not bacterial) HSP60 and is useful in distinguishing HSP60 from mammals and bacteria.


Catalog Number: (10240-666)
Supplier: Bioss
Description: Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.


Catalog Number: (10242-938)
Supplier: Bioss
Description: Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.


Catalog Number: (10814-100)
Supplier: Prosci
Description: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response.


Supplier: Ohaus
Description: The next generation of MB series moisture analyzers come in a sleek design offering improved durability and stability in performance, with an upgraded loadcell and carbon fiber heating technology.

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