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Catalog Number: (77437-992)
Supplier: Bioss
Description: The product of this gene is a heat-shock transcription factor. Transcription of heat-shock genes is rapidly induced after temperature stress. Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of this gene. [provided by RefSeq, Jul 2008].


Catalog Number: (76483-826)
Supplier: AAT BIOQUEST INC
Description: Reactive oxygen species (ROS) are natural byproducts of the normal metabolism of oxygen and play important roles in cell signaling.

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Catalog Number: (76100-746)
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: (10325-624)
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: (89358-042)
Supplier: Genetex
Description: HSF2, as well as the related gene HSF1, encodes a protein that binds specifically to the heat-shock element and has homology to HSFs of other species. Heat shock transcription factors activate heat-shock response genes under conditions of heat or other stresses. Although the names HSF1 and HSF2 were chosen for historical reasons, these peptides should be referred to as heat-shock transcription factors. [provided by RefSeq]


Catalog Number: (10414-080)
Supplier: Bioss
Description: Two HSFs have been identified in human cells, HSF 1 and HSF 2, which bind to the same HSEs and have 38% sequence identity. These factors are activated by distinct stimuli, HSF 1 is responsive to classical stress signals such as heat, heavy metals and oxidative reagents, whereas HSF 2 is activated during hemin-mediated differentiation of human erythroleukemia cells.HSF 1 exists constitutively in the cytoplasm and the nucleus of unstressed cells as a monomer which lacks DNA binding activity. Through an unknown signal generated during stress, HSF 1 becomes activated to a nuclear localized, trimeric state which binds to DNA. The phosphorylation of HSF 1 is necessary for maximal transcription of heat shock genes.


Catalog Number: (89359-340)
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 ""small heat shock proteins"" is comprised of a diverse group of proteins from ~15 to >30kDa, with a single form found in yeast and human cells and multiple related forms found in higher plants. A direct relationship between elevated stress protein expression and neoplasia has been suggested from studies on estrogen-induced proteins in breast cancer cells. In addition, Hsp27 exhibits rapid increased phosphorylation in response to various mitogens, tumor promoters (e.g. phorbol esters) and calcium ionophores. The expression of a 24kDa protein was shown to correlate with steroid hormone receptors in cell lines, organs , and tumors. The 24kDa estrogen-induced protein was found to be expressed at high levels in carcinoma of the breast. Another study has suggested that the levels of Hsp27 correlate with endometrial adenocarcinomas. Interestingly, the regulation of human Hsp27 by estrogens and heat shock is reminiscent of the ecdysteroid and heat shock activation of the drosophila Hsp20 genes.


Catalog Number: (102552-944)
Supplier: BioVendor
Description: The Heat shock protein 70(HSP70) family was found in many intracellular compartments. Members of this protein occur in chloroplasts, endoplasmic reticulum, mitochondria, and cytosol. These proteins are induced by a variety of biological stresses, including heat stress, in every organism. HSP70 serves a variety of roles: It acts as molecular chaperones facilitating the assembly of multi-protein complexes, It participates in the translocation of polypeptides across cell membranes and to the nucleus It aids in the proper folding of nascent polypeptide chains. HSP70 is mitochondrial import machinery and plays key roles in the cytosolic endoplasmic reticulum. Recently, extracellular localized HSP have been found to play key roles in the induction of a cellular immune response.


Catalog Number: (10326-326)
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: (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: (10782-000)
Supplier: Biosensis
Description: The heat shock proteins were discovered, as the name suggests, since they are heavily upregulated when cells are stressed by temperatures above the normal physiological range. They are expressed in unstressed cells also and have a normal function as chaperones, helping other proteins to fold correctly, and are required in much greater amounts if the cell or tissue is stressed by heat. The increased levels are generated transcriptionally under the influence of a powerful transcription factor, the heat shock factor 1 (HSF1). The different heat shock proteins were originally named based on their SDS-PAGE mobility, so HSP27 has an apparent molecular weight of 27kDa. It is an abundant protein even under non-stress conditions and frequently shows up as a major spot on 2 dimensional gels of cells or tissues. It is known to associate with a variety of other proteins such as actin, intermediate filament subunits and ubiquitin and is found both in the cytoplasm and the nucleus of cells. HSP27 can become heavily phosphorylated under the influence of multiple protein kinases particularly as a result of activation of the p38/SAPK pathway. Upregulation of this protein is protective against neurodegenerative diseases at least in certain mouse models (1). Point mutations in the HSP27 gene are associated with two neurological diseases, Charcot-Marie-Tooth disease type 2F and distal hereditary motor neuropathy IIB (2). These diseases are associated with axonal loss apparently following defects in the transport of neurofilaments.


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: (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: (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.


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