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Catalog Number: (10104-628)
Supplier: Prosci
Description: HSF2 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.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. 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.


Catalog Number: (76120-448)
Supplier: Bioss
Description: JWA is a four-transmembrane environmental responsive protein which binds to the CC chemokine receptor 5 (CCR5), a major co-receptor for human immunodeficiency virus (HIV). JWA is involved in environmental stress-responsive pathways in K562 cells, an erythroleukemia cell line derived from patients with chronic myeloid leukemia. Environmental stressors to K562 cells such as heat shock, a higher temperature than the ideal body temperature of the organism from which the cell line was derived, and oxidative stress, the production of oxygen-centered free radicals, regulate and increase the expression of JWA. This response to environmental stressors suggests similarity of JWA to heat shock protein 70 (HSP70), which is upregulated by heat stress and toxic chemicals.


Catalog Number: (10414-104)
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: (76194-964)
Supplier: Prosci
Description: HSP27 is induced by environmental stress and developmental changes. It is involved in stress resistance and actin organization and translocates from the cytoplasm to the nucleus upon stress induction. [RefSeq]


Catalog Number: (76100-748)
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: (76194-110)
Supplier: Prosci
Description: Recognizes a 60kDa 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: (76194-112)
Supplier: Prosci
Description: Recognizes a 60kDa 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: (76483-824)
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: (76262-726)
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.


Catalog Number: (10106-402)
Supplier: Prosci
Description: HSF1 mediates the stress induced expression of heat shock proteins.


Catalog Number: (10106-404)
Supplier: Prosci
Description: HSF1 mediates the stress induced expression of heat shock proteins.


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: (10347-384)
Supplier: Bioss
Description: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress.


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: (10325-610)
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: (10326-324)
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.


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