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HSP27 Scientific Resource Guide | HSP27Heat Shock Protein 27 (HSP27) information database. A resource for all HSP27 structure, isoform, function, disease relevance, and inhibitor information.
http://www.hsp27.com/
Heat Shock Protein 27 (HSP27) information database. A resource for all HSP27 structure, isoform, function, disease relevance, and inhibitor information.
http://www.hsp27.com/
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HSP27 Scientific Resource Guide | HSP27 | hsp27.com Reviews
https://hsp27.com
Heat Shock Protein 27 (HSP27) information database. A resource for all HSP27 structure, isoform, function, disease relevance, and inhibitor information.
HSP27 Structure | HSP27
http://hsp27.com/structure
Click image for larger version). As mentioned previously, Hsp27 belongs to the family of the α-crystallins as they share an α-crystalline domain. These molecular chaperones proteins act to prevent improper polypeptide association. The amino-terminal extension modulates oligomerization, subunit dynamics and substrate binding, whereas the flexible carboxy-terminal extension promotes solubility, chaperoning and oligomerization. The latter is by inter- subunit linkage. HspB and HspC, and.
HSP27 Function and Regulation | HSP27
http://hsp27.com/function-and-regulation
HSP27: Function and Regulation. Staining of somites of a rat embryo at 11 days of gestation. Red is rhodamine-phalloidin labeled actin and green is Hsp27, using Anti-Hsp27 (clone: 8A7). Characteristically, Hsp27 is ubiquitously expressed and involved in the regulation of main cellular physiologic functions. And d) the regulation of the cytoskeleton. Moreover, it has been implicated in promotion, generation and/or cytoprotection in few pathologies. A) Inhibition of Apoptosis. Regulation of apoptosis by Hs...
HSP27 Molecular Weight | HSP27
http://hsp27.com/molecular-weight
ICC staining of Hsp27 (green) in mouse spinal cord sections (DAPI merged with Alexa 488) using Anti-Hsp27 (clone: 5D12-A12). Hsp27 (HspB1) belongs to the α-crystallin related small heat shock proteins (sHSPs) family. These include proteins with monomeric molecular weight ranging from 16 to 28 kDa and are encoded by a multigene family of 10 genes, ( Table 2. Mammalian Hsp27 has a molecular weight of 27 kDa while it can form oligomeric complexes in the range 100 to 800 kDa.
Species Variation - HSP27 | HSP27
http://hsp27.com/species-variation
IHC staining of Hsp22 in mouse spinal cord sections (DAPI merged with Alexa 488) using Anti-Hsp22 (rabbit polyclonal). The case in plants is more complicated since they have more than 20 sHSP genes. Thus, they are divided in 6 classes, of which, 3 classes (CI, CII and CIII) are in the cytosol or in the nucleus and the other three (CIV, CV and CVI) in the plastids. Thermophilic archea and bacteria thermophiles like. Species sequenced lack genes coding for ClpA, ClpP, ClpX, HtpG, DegP, and sHsps. From Mymr...
HSP27 Isoforms | HSP27
http://hsp27.com/isoforms
Staining of somites of a rat embryo at 11 days of gestation. Red is rhodamine-phalloidin labeled actin and green is Hsp27, using Anti-Hsp27 (clone: 8A7). Hsp27 has been also named as Growth-related 25 kDa protein, Heat shock 25 kDa protein (Short name, HSP 25), Heat shock 27 kDa protein (Short name, HSP 27) and Hsp28 and more recently as HspB1 ( Table 2. For instance, heat shock protein B1 (HSP27, UnitProt ID #P04792.
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Figures - HSP90 | HSP90
http://hsp90.ca/figures
Mechanisms & Interactions. Structure of the tetragonal form of the N-terminal domain of Hsp90 from yeast ( PDB ID: 1ah6. Figure 1. Structure of the tetragonal form of the N-terminal domain of Hsp90 from yeast ( PDB ID: 1ah6. Structure of full-length yeast Hsp90. Figure 2. Structure of full-length yeast Hsp90. Crystal structure of dimeric full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba-1 ( PDB ID: 2CG9. Structures of the full-length Hsp90 dimer. The N-terminal nucleoti...
HSP90 Isoforms | HSP90
http://hsp90.ca/isoforms
Mechanisms & Interactions. IHC staining of inflammatory cells in mouse colon tissue, using Anti-Hsp90 (clone: D7A). The HSP90 proteins are ubiquitous and highly conserved molecular chaperones present from bacteria to mammals. HSP90 proteins can be found in the cytosol, ER, chloroplasts, mitochondria, and the nucleus. Eubacteria express a single Hsp90 homolog, referred to as. High-temperature protein G) which is absent in Archaebacteria with the exception of. 1 (Hsp90AA1, HspC1) and the constitutive Hsp90.
HSP90 Mechanisms & Interactions | HSP90
http://hsp90.ca/mechanisms-interactions
Mechanisms & Interactions. HSP90: Mechanisms and Interactions. IF detection of Hsp90 in cancerous human colon tissue, using Anti-Hsp90 (clone: H9010). A comprehensive list of Hsp90-interacting proteins can be found at the website of Didier Picard. According to their biological function, Hsp90 client proteins can be classified in several groups such as transcription factors, TPR-domain proteins, protein kinases, structural proteins, and others. The Cdc-37/Hsp90 complex can be formed in an open or closed c...
Tables - HSP90 | HSP90
http://hsp90.ca/tables
Mechanisms & Interactions. Table 1: Human and mouse orthologs of Hsp90α1 (HspC1). Chr 14:102,547,075-102,606,086. Chr 12: 110,691,036-110,696,395. Table 2: HSP90s of various pro- and eukaryotic organisms. Hsp90α1, Hsp90AA1, Hsp86, HspCA, Hsp89, Hsp90A, renal carcinoma antigen NY-REN-38. Hsp90α2, Hsp90AA2, Hsp90α-like 3, HspCA. Hsp90β, Hsp90AB1, Hsp84, HSP90B, HspCB. Endoplasmin, Grp94, Gp96, Tra-1, Hsp90B1. Trap-1, Hsp75, Hsp90L. Slo, sloth, akineto, heat shock protein 90-alpha 1. AtHsp90.2, Hsp81-2.
HSP90 Structure | HSP90
http://hsp90.ca/structure
Mechanisms & Interactions. HSP90s are abundant and highly specialized molecular chaperones crucially involved in several signalling pathways. They primarily exist as homodimers whose activity is regulated by ATP. Dimerization is essential for the vital functions of HSP90s. Nevertheless, higher oligomeric states including hexamers have been reported. It has been shown previously that oligomerization is induced after heat shock and in the presence of non-ionic detergents. Click image for larger version).
HSP90 Protein Type | HSP90
http://hsp90.ca/protein-type
Mechanisms & Interactions. Hsp90 (total) visualized on a human keratinocyte line HaCat, using Anti-Hsp90 (total) (clone: 4F3.E8). The HSP90 family represents a group of well-conserved proteins with an average molecular mass of 90 kDa. There are two major cytosolic Hsp90 isoforms, the inducible Hsp90. 1 (HspC1) and the constitutive Hsp90. HspC3), commonly termed Hsp90. The HSP90 family members are encoded by a multigene family encompassing six genes and 11 pseudogenes in humans. The most studied genes are.
Discovery of HSP90 | HSP90
http://hsp90.ca/history
Mechanisms & Interactions. IHC staining of inflammatory cells in mouse colon tissue, using Anti-Hsp90 alpha (clone: Hyb-K41009). Heat shock protein 90 (Hsp90) was originally described amongst a defined set of heat shock proteins (HSPs) that are rapidly induced in fungal, plant and animal cells in response to acute thermal up-regulation. This HSP induction is referred to as the heat shock response (HSR) that is ubiquitous across the bacterial, archaeal and eukaryotic kingdoms. 83 kDa heat shock protein 2.
HSP90 Disease Relevance | HSP90
http://hsp90.ca/disease-relevance
Mechanisms & Interactions. IHC detection of Hsp90 in cancerous human colon tissue, using Anti-Hsp90 (clone: H9010). A growing wealth of evidence indicates the pivotal role of Hsp90 in tumourigenesis. Constitutively elevated levels of Hsp90 can be found in a broad spectrum of cancers suggesting a central role in survival and growth of malignant cells. 1 to the heterodimeric cell surface receptor Her-2/Her-3 thereby inducing HSF-1 stabilization which consequently enhanced cell survival and transformation.
HSP90 Molecular Weight | HSP90
http://hsp90.ca/molecular-weight
Mechanisms & Interactions. IHC staining of inflammatory cells and epithelia mucosa in mouse colon tissues, using Anti-Hsp90 (clone: AC-16). The HSP90 family represents a group of well-conserved proteins with an average molecular mass of 90 kDa. There are two major cytosolic Hsp90 isoforms, the inducible Hsp90. 1 (HspC1) and the constitutive Hsp90. HspC3), commonly termed Hsp90. The HSP90 family members are encoded by a multigene family encompassing six genes and 11 pseudogenes in humans.
References - HSP90 | HSP90
http://hsp90.ca/references
Mechanisms & Interactions. 1 Csermely,P., Schnaider,T., Soti,C., Prohaszka,Z., and Nardai,G. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79, 129-168 (1998). [PubMed]. 2 Felts,S.J. et al. The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 275, 3305-3312 (2000). [PubMed]. Novartis. Found. Symp. 291, 86-95 (2008). [PubMed]. 10 Lindquist,S. Regulation of protein ...
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HSP27 Scientific Resource Guide | HSP27
The Heat Shock Protein 27 (Hsp27) is a 25-kDa protein also known as Heat Shock Protein Beta-1 (HspB1). That belongs to the family of small Hsps ( Table 1. And is the human homologue of murine Hsp25. Throughout this website, Hsp27 and HspB1 will be used interchangeably. Hsp27 is ubiquitously expressed and has been implicated in various biological functions. In contrast to large Hsps, Hsp27 acts through ATP-independent mechanisms, and. Activation of the heat shock-responsive element on the. 8220;3q9p”...
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