HSP27 monoclonal antibody (G3.1) | Enzo Life Sciences ADI-SPA-800-J product information

product summary

company name :

Enzo Life Sciences

other brands :

Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

product type :

antibody

product name :

HSP27 monoclonal antibody (G3.1)

catalog :

ADI-SPA-800-J

quantity :

1 mg

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

G3.1

reactivity :

human, mouse, rat, bovine

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation

more info or order :

Enzo Life Sciences product webpage

citations: 21

Published Application/Species/Sample/Dilution	Reference
immunocytochemistry; human; loading ...; fig 2	Zeng X, Han I, Abd El Barr M, Aljuboori Z, Anderson J, Chi J, et al. The Effects of Thermal Preconditioning on Oncogenic and Intraspinal Cord Growth Features of Human Glioma Cells. Cell Transplant. 2016;25:2099-2109 pubmed publisher
western blot; human; fig s3	MorlÃ© A, Garrido C, Micheau O. Hyperthermia restores apoptosis induced by death receptors through aggregation-induced c-FLIP cytosolic depletion. Cell Death Dis. 2015;6:e1633 pubmed publisher
western blot; mouse	Dang V, Tanabe K, Tanaka Y, Tokumoto N, Misumi T, Saeki Y, et al. Fasting enhances TRAIL-mediated liver natural killer cell activity via HSP70 upregulation. PLoS ONE. 2014;9:e110748 pubmed publisher
immunohistochemistry; rat; 1:1000	Moloney T, Hyland R, O Toole D, Paucard A, Kirik D, O Doherty A, et al. Heat shock protein 70 reduces ?-synuclein-induced predegenerative neuronal dystrophy in the ?-synuclein viral gene transfer rat model of Parkinson's disease. CNS Neurosci Ther. 2014;20:50-8 pubmed publisher
western blot; human	Mao R, Rubio V, Chen H, Bai L, Mansour O, Shi Z. OLA1 protects cells in heat shock by stabilizing HSP70. Cell Death Dis. 2013;4:e491 pubmed publisher
western blot; human	Middlekauff H, Vigna C, Verity M, Fonarow G, Horwich T, Hamilton M, et al. Abnormalities of calcium handling proteins in skeletal muscle mirror those of the heart in humans with heart failure: a shared mechanism?. J Card Fail. 2012;18:724-33 pubmed publisher
	Sevin M, Kubovcakova L, Pernet N, Causse S, Vitte F, Villeval J, et al. HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis. Nat Commun. 2018;9:1431 pubmed publisher
	Homa J, Ortmann W, Kolaczkowska E. Conservative Mechanisms of Extracellular Trap Formation by Annelida Eisenia andrei: Serine Protease Activity Requirement. PLoS ONE. 2016;11:e0159031 pubmed publisher
	Qvit N, Joshi A, Cunningham A, Ferreira J, Mochly Rosen D. Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) Protein-Protein Interaction Inhibitor Reveals a Non-catalytic Role for GAPDH Oligomerization in Cell Death. J Biol Chem. 2016;291:13608-21 pubmed publisher
	Asano Y, Kawase T, Okabe A, Tsutsumi S, Ichikawa H, Tatebe S, et al. IER5 generates a novel hypo-phosphorylated active form of HSF1 and contributes to tumorigenesis. Sci Rep. 2016;6:19174 pubmed publisher
	Shi L, Gehin T, Chevolot Y, Souteyrand E, MangÃ© A, Solassol J, et al. Anti-heat shock protein autoantibody profiling in breast cancer using customized protein microarray. Anal Bioanal Chem. 2016;408:1497-506 pubmed publisher
	Xiong R, Zhou W, Siegel D, Kitson R, Freed C, Moody C, et al. A Novel Hsp90 Inhibitor Activates Compensatory Heat Shock Protein Responses and Autophagy and Alleviates Mutant A53T Î±-Synuclein Toxicity. Mol Pharmacol. 2015;88:1045-54 pubmed publisher
	Lash L, Putt D, Jankovich A. Glutathione Levels and Susceptibility to Chemically Induced Injury in Two Human Prostate Cancer Cell Lines. Molecules. 2015;20:10399-414 pubmed publisher
	Mu T, Ong D, Wang Y, Balch W, Yates J, Segatori L, et al. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell. 2008;134:769-81 pubmed publisher
	Othmen Z, Golli E, Abid Essefi S, Bacha H. Cytotoxicity effects induced by Zearalenone metabolites, alpha Zearalenol and beta Zearalenol, on cultured Vero cells. Toxicology. 2008;252:72-7 pubmed publisher
	Vidyasagar A, Reese S, Acun Z, Hullett D, Djamali A. HSP27 is involved in the pathogenesis of kidney tubulointerstitial fibrosis. Am J Physiol Renal Physiol. 2008;295:F707-16 pubmed publisher
	Paulsen G, Vissing K, Kalhovde J, Ugelstad I, Bayer M, Kadi F, et al. Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans. Am J Physiol Regul Integr Comp Physiol. 2007;293:R844-53 pubmed
	Sakamoto H, Mashima T, Yamamoto K, Tsuruo T. Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification. J Biol Chem. 2002;277:45770-5 pubmed
	Radice S, Ferraris M, Marabini L, Chiesara E. Estrogenic activity of procymidone in primary cultured rainbow trout hepatocytes (Oncorhynchus mykiss). Toxicol In Vitro. 2002;16:475-80 pubmed
	Jonak C, Klosner G, Kokesch C, FOdinger D, HOnigsmann H, Trautinger F. Subcorneal colocalization of the small heat shock protein, hsp27, with keratins and proteins of the cornified cell envelope. Br J Dermatol. 2002;147:13-9 pubmed
	Garcia J, Wang P, Schaphorst K, Becker P, Borbiev T, Liu F, et al. Critical involvement of p38 MAP kinase in pertussis toxin-induced cytoskeletal reorganization and lung permeability. FASEB J. 2002;16:1064-76 pubmed

product information

Product ID :

ADI-SPA-800

Catalog Number :

ADI-SPA-800-J

Product Name :

HSP27 monoclonal antibody (G3.1)

Host species :

Mouse

Clonality :

Monoclonal

Product Type :

Antibody

Size :

1 mg

list of Pubmed id :

26056813, 18775310, 18755238, 18596079, 17522120, 12226095, 12110288, 12100179, 12100179, 12087068

Clone :

G3.1

Isotype :

IgG1

SPECIES REACTIVITY :

Human, Mouse, Rat, Monkey, Fish, Bovine

Background :

Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.

ALTnames :

HspB1, Heat shock protein 27

Immunogen :

Native human Hsp27.

Buffer :

Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.

Uses :

Detects a band of ~27kDa by Western blot.

Application Summary :

ELISA, ICC, IHC (PS), IP, WB, in vitro Assay, Electron microscopy

Storage :

-20°C

more info or order :

Enzo Life Sciences product webpage