You Searched For: Heat+Stress+Meters


12,449  results were found

SearchResultCount:"12449"

Sort Results

List View Easy View

Rate These Search Results

Catalog Number: (76483-832)
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.

Small Business Enterprise Minority or Woman-Owned Business Enterprise


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: (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: (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: (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: (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.

Small Business Enterprise Minority or Woman-Owned Business Enterprise


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.


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


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


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: (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: (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: (75789-178)
Supplier: Prosci
Description: Heat Shock Protein beta -11 (HSPB11) is a stress-responsive protein that is required to deal with proteotoxic stresses. HSPB11 is composed of an IFT complex B composed of IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20 and is detected in placenta. HSPB11 has beeb shown to form oligomeric complexes and prevent the aggregation of in vitro denaturated aldolase and glyceraldehyde-3-phosphate dehydrogenase in accordance with the chaperone model of HSPB1 and HSPB5. HSPB11 overexpression protected against etoposide-induced cell death that correlated with a decreased release of mitochondrial Cytochrome C into the cytosol. Inhibition of HSP90 function completely abrogated the protective effect of HSPB11. This data suggests that at least in the case of HSPB11, interaction with other chaperone machines besides HSPA1A may contribute to functional specificity and cellular functioning.


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.


Inquire for Price
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
17 - 32 of 12,449
no targeter for Bottom