HSP27 Antibody | StressMarq Biosciences SMC-161B product information

product summary

company name :

StressMarq Biosciences

product type :

antibody

product name :

HSP27 Antibody

catalog :

SMC-161B

quantity :

200 µg

price :

251.00 USD

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

5D12-A12

reactivity :

human

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation

more info or order :

StressMarq Biosciences product webpage

citations: 6

Published Application/Species/Sample/Dilution	Reference
immunocytochemistry; human; 1:1500; loading ...; fig 15 western blot; human; 1:1500; loading ...; fig 13a	Sugiyama S, Yoshino Y, Kuriyama S, Inoue M, Komine K, Otsuka K, et al. A Curcumin Analog, GO-Y078, Effectively Inhibits Angiogenesis through Actin Disorganization. Anticancer Agents Med Chem. 2016;16:633-47 pubmed
immunohistochemistry; human	Kötter S, Unger A, Hamdani N, Lang P, Vorgerd M, Nagel Steger L, et al. Human myocytes are protected from titin aggregation-induced stiffening by small heat shock proteins. J Cell Biol. 2014;204:187-202 pubmed publisher
	Pereira M, Tomé D, Domingues A, Varanda A, Paulo C, Santos M, et al. A Fluorescence-Based Sensor Assay that Monitors General Protein Aggregation in Human Cells. Biotechnol J. 2018;13:e1700676 pubmed publisher
	Unger A, Beckendorf L, Böhme P, Kley R, von Frieling Salewsky M, Lochmuller H, et al. Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function. Acta Neuropathol Commun. 2017;5:72 pubmed publisher
	Lee S, Dempsey Hibbert N, Vimalachandran D, Wardle T, Sutton P, Williams J. Re-examining HSPC1 inhibitors. Cell Stress Chaperones. 2017;22:293-306 pubmed publisher
	Mymrikov E, Daake M, Richter B, Haslbeck M, Buchner J. The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins. J Biol Chem. 2017;292:672-684 pubmed publisher

product information

Catalog No :

SMC-161B

Product Name :

HSP27 Antibody

Description :

Mouse Anti-Human HSP27 Monoclonal IgG2b Kappa

Target :

HSP27

Conjugate :

Unconjugated

2021 List Price :

251.00 USD

Currency :

USD

Research Area(s) :

Cell Signaling Protein Trafficking Chaperone Proteins Cell Signaling Cytoskeleton Microfilaments Actin Actin Assembly Cell Signaling Cytoskeleton Microtubules Cancer Tumor Biomarkers Cardiovascular System Atherosclerosis Cardiovascular System Heart Contractility Cancer Heat Shock

Alternative Name(s) :

28kDa heat shock protein Antibody, CMT2F Antibody, HSP25 Antibody, HSP27 Antibody, HSP28 Antibody, HSPB1 Antibody, SRP27 Antibody

Size :

200 µg

Category :

Antibodies

Product Type :

Monoclonal

Clone Number :

5D12-A12

Immunogen :

Full length human HSP27

Immunogen Species :

Human

Accession Number :

NP_001531.1

Swiss-Prot :

P04792

Applications :

WB IHC ICC/IF IP ELISA

Host Species :

Mouse

Isotype :

IgG2b Kappa

Species Reactivity Abbreviation :

Species Reactivity Full Name :

Human

Antibody Dilution :

WB (1:2000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

Purification :

Protein G Purified

Storage Buffer :

PBS pH7.4, 50% glycerol, 0.09% sodium azide

Concentration :

1 mg/ml

Specificity :

Detects ~27kDa. Has no cross-reactivity to Alpha B crystallin. Very limited cross-reactivity to other species.

Storage Temperature :

-20ºC

Shipping Temperature :

Blue Ice or 4ºC

Cite this Product :

StressMarq Biosciences Cat# SMC-161B, RRID: AB_2248586

Certificate of Analysis :

0.5 µg/ml of SMC-161 was sufficient for detection of HSP27 in 10 µg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Cellular Localization :

Cytoplasm Nucleus Cytoskeleton Spindle

Scientific Background :

HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an α-crystallin domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). For more information visit our HSP27 Scientific Resource Guide at http://www.HSP27.com.

References :

1. Kim K.K., Kim R., and Kim, S. (1998) Nature 394(6693): 595-599. 2. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 3. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 4. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 5. Sarto C., Binnz P.A., and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 6. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6.

Field of Use :

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

Image Filenames :

SMC-161_Hsp27_Antibody_5D12-A3_ICC-IF_Human_Heat-Shocked-HeLa-Cells_100x_Composite.png SMC-161_Hsp27_Antibody_5D12-A3_ICC-IF_Human_HaCaT-cells_2.png SMC-161_Hsp27_Antibody_5D12-A3_ICC-IF_Human_Heat-Shocked-HeLa-Cells_20x_Composite.png SMC-161_Hsp27_Antibody_5D12-A3_WB_Human_Cell-lysates_1.png

more info or order :

StressMarq Biosciences product webpage