TA326356 Heat shock protein 70 / HSP70 antibody

Mouse monoclonal Hsp70 Antibody

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0.2 mg / €440.00
Please visit the country specific website of OriGene Technologies or contact your local Distributor to buy this product.

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Mouse anti Bovine, C. elegans, Canine, Carp, Chicken, Drosophila, Guinea Pig, Hamster, Human, Monkey, Mouse, Porcine, Rabbit, Rat, Sheep Heat shock protein 70 / HSP70 C92F3A-5

TA326356

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  • TA326356

Product Description for Heat shock protein 70 / HSP70

Mouse anti Bovine, C. elegans, Canine, Carp, Chicken, Drosophila, Guinea Pig, Hamster, Human, Monkey, Mouse, Porcine, Rabbit, Rat, Sheep Heat shock protein 70 / HSP70 C92F3A-5.
Presentation: Aff - Purified
Product is tested for Frozen Sections, Enzyme Immunoassay, Immunocytochemistry/Immunofluorescence, Immunoprecipitation, Western blot / Immunoblot, Immunoelectron Microscopy, Flow Cytometry.

Properties for Heat shock protein 70 / HSP70

Product Category Primary Antibodies
Target Category
Quantity 0.2 mg
Synonyms HSP70-1/HSP70-2, HSP70.1, HSPA1, HSPA1A, HSPA1B, Heat shock 70 kDa protein 1A/1B
Presentation Aff - Purified
Reactivity Bov, Can, Carp, Ce, Chk, Dros, GP, Hst, Hu, Mky, Ms, Por, Rb, Rt, Sh
Applications C, E, EM, F, ICC/IF, IP, WB
Clonality Monoclonal
Clone C92F3A-5
Host Mouse
Isotype IgG1
Shipping to Europe, USA/Canada
PDF datasheet View Datasheet
Manufacturer OriGene Technologies, Inc.

Datasheet Extract

Immunogen
Swiss Prot Num:
P08107
Immunogen:
Human HSP70 (Ref.1).
GeneID:
3303
Application ELISA (Ref.10).
Western blot (See also Ref.7,8,14). 
1 µg/ml was sufficient for detection of HSP70 in 20 µg of HeLa lysate by colorimetric immunoblot analysis using HRP conjugated Goat anti-Mouse IgG as the secondary antibody.
FACS (Ref.12).
Immunocytochemistry (Ref.1,11). 
Immunoprecipitation (Ref.9).
Electron Microscopy (Ref.11). 
Protein Inhibition. 
Immunohistochemistry (Ref.11).
Background Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (2). The N-terminal two thirds of hsp70s are more conserved than the C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the Cterminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5).
All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.
Concentration 1.0 mg/ml
Product Citations
Originator or purchased from resellers:
  1. Guess AJ, Ayoob R, Chanley M, Manley J, Cajaiba MM, Agrawal S, et al. Crucial roles of the protein kinases MK2 and MK3 in a mouse model of glomerulonephritis. PLoS One. 2013;8(1):e54239. doi: 10.1371/journal.pone.0054239. Epub 2013 Jan 23. PubMed PMID: 23372691. (Free PMC Article available, 7 images available)
  2. Bauckman KA, Haller E, Flores I, Nanjundan M. Iron modulates cell survival in a Ras- and MAPK-dependent manner in ovarian cells. Cell Death Dis. 2013 Apr 18;4:e592. doi: 10.1038/cddis.2013.87. PubMed PMID: 23598404. (Free PMC Article available, 8 images available)
  3. Aare S, Radell P, Eriksson LI, Akkad H, Chen YW, Hoffman EP, et al. Effects of corticosteroids in the development of limb muscle weakness in a porcine intensive care unit model. Physiol Genomics. 2013 Apr 16;45(8):312-20. doi: 10.1152/physiolgenomics.00123.2012. Epub 2013 Feb 19. PubMed PMID: 23429211.
  4. Heat-induced expression of the immediate-early gene IER5 and its involvement in the proliferation of heat-shocked cells. FEBS J. [Epub ahead of print]. 2014. Ishikawa, Y. and Sakurai, H. PubMed ID : 25355627.
  5. Prostaglandin E Synthase Interacts with Inducible Heat Shock Protein 70 After Heat Stress in Bovine Primary Dermal Fibroblast Cells. Journal of the International Society for Advancement of Cytometry. [Epub ahead of print]. 2014. Richter, C., Viergutz, T., Schwerin, M. and Weitzel, J.M. PubMed ID : 25412999.
  6. Fasting Enhances TRAIL-Mediated Liver Natural Killer Cell Activity via HSP70 Upregulation. (View PDF) PLoS One. 9(10): e110748. 2014. Dang, V.T.A. et al. PubMed ID: 25356750.
  7. Engels, M. et al. A cardiopulmonary bypass with deep hypothermic circulatory arrest rat model for the investigation of the systemic inflammation response and induced organ damage. (View PDF) J Inflamm. 2014. 11(26).
  8. Sheppard PW, Sun X, Khammash M, Giffard RG. Overexpression of heat shock protein 72 attenuates NF-κB activation using a combination of regulatory mechanisms in microglia. PLoS Comput Biol. 2014 Feb 6;10(2):e1003471. doi: 10.1371/journal.pcbi.1003471. eCollection 2014 Feb. PubMed PMID: 24516376. (Free PMC Article available, 7 images available)
  9. Structure-Activity Relationships for Withanolides as Inducers of the Cellular Heat-Shock Response. J Med Chem. 57(7):2851-63. 2014. Wijeratne, E.M., et al. PubMed ID: 24625088.
  10. Akkad H, Corpeno R, Larsson L. Masseter muscle myofibrillar protein synthesis and degradation in an experimental critical illness myopathy model. PLoS One. 2014 Apr 4;9(4):e92622. doi: 10.1371/journal.pone.0092622. eCollection 2014. PubMed PMID: 24705179. (Free PMC Article available, 4 images available)
  11. Therapeutic Inducers of the HSP70/HSP110 Protect Mice Against Traumatic Brain Injury. J Neurochem. 130(5):626-41. 2014. Eroglu, B. et al. PubMed ID: 24903326.
  12. Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly. (View PDF) Cell Death Differ. 21(12):1838-51. 2014. Seguin, S.J. et al. PubMed ID: 25034784.
  13. Iron modulates cell survival in a Ras- and MAPK-dependent manner in ovarian cells. (View PDF) Cell Death and Disease. 4.e592. 2013. Bauckman, K.A., Haller, E., Flores. I., and Nanjundan, M. PubMed ID: 23598404.
  14. Larkins NT, Murphy RM, Lamb GD. Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers. Am J Physiol Cell Physiol. 2012 Sep 15;303(6):C654-65. doi: 10.1152/ajpcell.00180.2012. Epub 2012 Jul 3. PubMed PMID: 22763123.
  15. DnaJA1 Antagonizes Constitutive Hsp70-Mediated Stabilization of Tau. (View PDF) J. Mol. Biol. 421, 653-661. 2012. Abisambra, J.F., et al. PubMed ID: 22343013.
  16. Molecular and Cellular Networks in Critical Illness Associated Muscle Weakness: Skeletal Muscle Proteostasis in the Intensive Care Unit. (View PDF) Acta Universitatis Upsaliensis. Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine 841. 63 pp. Uppsala. ISBN 978-91-554-8542-9. 2012. Banduseela, V.C.
  17. Using the Heat-Shock Response To Discover Anticancer Compounds that Target Protein Homeostasis. (View PDF) ACS Chem. Biol.7 (2), 340-349. 2012. Santagata, S. et al. PubMed ID: 22050377.
  18. Hsp70 Promotes Epithelial Sodium Channel Functional Expression by Increasing Its Association with Coat Complex II and Its Exit from Endoplasmic Reticulum. (View PDF) J Biol Chem. 287, 19255-19265. 2012. Chanoux, R.A. et al. PubMed ID: 22496374.
  19. Shipp C, Watson K, Jones GL. Associations of HSP90 client proteins in human breast cancer. Anticancer Res. 2011 Jun;31(6):2095-101. PubMed PMID: 21737627.
  20. Co-overexpression of Bag-1 and heat shock protein 70 in human epidermal squamous cell carcinoma: Bag-1-mediated resistance to 5-fluorouracil induced apoptosis. (View PDF) British Journal of Cancer. 104 (9), 1459-1471. 2011. Wood, J. et al. PubMed ID: 21522149.
  21. Withaferin A Analogs and Uses Thereof. United States Patent Application US20110230551 A1. 2011. Gunatilaka, L., Lindquist, S.L., Whitesell, L.,Wijeratne, E.M.K., and Xu, Y. PubMed ID: N/A Reactivity: Mouse Applications: Western Blot
  22. Larkins NT, Murphy RM, Lamb GD. Absolute amounts and diffusibility of HSP72, HSP25, and αB-crystallin in fast- and slow-twitch skeletal muscle fibers of rat. Am J Physiol Cell Physiol. 2012 Jan 1;302(1):C228-39. doi: 10.1152/ajpcell.00266.2011. Epub 2011 Oct 5. PubMed PMID: 21975426.
  23. Mitsuhashi M, Yamaguchi M, Kojima T, Nakajima R, Kasai K. Effects of HSP70 on the compression force-induced TNF-α and RANKL expression in human periodontal ligament cells. Inflamm Res. 2011 Feb;60(2):187-94. doi: 10.1007/s00011-010-0253-x. PubMed PMID: 20924639.
  24. Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: underlying mechanisms. (View PDF) J Physio. 589 (8). 2007-2026.2011. Ochala, J. et al. PubMed ID: 21320889.
  25. Heat Shock Protein 70 Prevents both Tau Aggregation and the Inhibitory Effects of Preexisting Tau Aggregates on Fast Axonal Transport. (View PDF) Biochem. 50 (47), 10300-10310. 2011. Patterson, K.R. et al. PubMed ID: 22039833.
  26. Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model. (View PDF) Physiol Genomics. 43 (24), 1334-1350. 2011. Aare, S. et al. PubMed ID: 22010006.
  27. Batista-Nascimento L, Neef DW, Liu PC, Rodrigues-Pousada C, Thiele DJ. Deciphering human heat shock transcription factor 1 regulation via post-translational modification in yeast. PLoS One. 2011 Jan 6;6(1):e15976. doi: 10.1371/journal.pone.0015976. PubMed PMID: 21253609. (Free PMC Article available, 7 images available)
  28. HSF1-Dependent Upregulation of Hsp70 by Sulfhydryl-Reactive Inducers of the KEAP1/NRF2/ARE Pathway. (View PDF) Chem & Biol. 18 (11), 1355-1361. 2011. Zhang, Y. et al. PubMed ID: 22118669.
  29. Tamm-Horsfall protein and urinary exosome isolation. (View PDF) Kidney International. 77, 736-742. 2010. Fernández-Llama, P. et al. PubMed ID: 20130532.
  30. HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans. (View PDF) The Journal of Clinical Investigation. 120 (10), 3578-3593. 2010. Marubayashi, S. et al. PubMed ID: 20852385.
  31. Olkku A, Leskinen JJ, Lammi MJ, Hynynen K, Mahonen A. Ultrasound-induced activation of Wnt signaling in human MG-63 osteoblastic cells. Bone. 2010 Aug;47(2):320-30. doi: 10.1016/j.bone.2010.04.604. Epub 2010 May 7. PubMed PMID: 20435172.
  32. 2,3-Dihydrowithaferin A-3β-O-sulfate, a new potential prodrug of withaferin A from aeroponically grown Withania somnifera. Bioorganic & Medicinal Chemistry. 17 (6), 2210-2214. 2009. Xu, Y. et al. PubMed ID: 19056281.
  33. Identification of Phosphorylation-Dependent Binding Partners of Aquaporin-2 Using Protein Mass Spectrometry. (View PDF) J. Proteome Res. 8 (3), 1540-1554. 2009. Zwang, N.A. et al. PubMed ID: 19209902.
  34. Gene expression and muscle fiber function in a porcine ICU model. (View PDF) Physiol Genomics. 39 (3), 141-159. 2009. Banduseela, V.C. et al. PubMed ID: 19706692.
  35. Heat shock protein 70 regulates degradation of the mumps virus phosphoprotein via the ubiquitin-proteasome pathway. J Virol. [Epub ahead of print]. 2014. Katoh, H. et al. PubMed ID : 25552722.
General Readings
  1. Welch WJ, Suhan JP. Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. J Cell Biol. 1986 Nov;103(5):2035-52. PubMed PMID: 3536957. (Free PMC Article available)
  2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol. 38(1): 1-17.
  3. Rothman JE. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell. 1989 Nov 17;59(4):591-601. PubMed PMID: 2573430.
  4. DeLuca-Flaherty C, McKay DB, Parham P, Hill BL. Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell. 1990 Sep 7;62(5):875-87. PubMed PMID: 1975516.
  5. Bork P, Sander C, Valencia A. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7290-4. PubMed PMID: 1323828. (Free PMC Article available)
  6. Fink AL. Chaperone-mediated protein folding. Physiol Rev. 1999 Apr;79(2):425-49. PubMed PMID: 10221986.
  7. Galán A, García-Bermejo ML, Troyano A, Vilaboa NE, de Blas E, Kazanietz MG, et al. Stimulation of p38 mitogen-activated protein kinase is an early regulatory event for the cadmium-induced apoptosis in human promonocytic cells. J Biol Chem. 2000 Apr 14;275(15):11418-24. PubMed PMID: 10753958.
  8. Kondo T, Matsuda T, Tashima M, Umehara H, Domae N, Yokoyama K, et al. Suppression of heat shock protein-70 by ceramide in heat shock-induced HL-60 cell apoptosis. J Biol Chem. 2000 Mar 24;275(12):8872-9. PubMed PMID: 10722733.
  9. Misaki T, Takeuchi R, Miyamoto S, Hirano A, Kasagi K, Konishi J. Induction in vitro of 72-kD heat shock protein in a continuous culture of rat thyroid cells, FRTL5. Clin Exp Immunol. 1994 Nov;98(2):234-9. PubMed PMID: 7955528. (Free PMC Article available)
  10. Pockley AG, Shepherd J, Corton JM. Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serum of normal individuals. Immunol Invest. 1998 Dec;27(6):367-77. PubMed PMID: 9845422.
  11. Moon IS, Park IS, Schenker LT, Kennedy MB, Moon JI, Jin I. Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses. Cereb Cortex. 2001 Mar;11(3):238-48. PubMed PMID: 11230095.
  12. Dressel R, Elsner L, Quentin T, Walter L, Günther E. Heat shock protein 70 is able to prevent heat shock-induced resistance of target cells to CTL. J Immunol. 2000 Mar 1;164(5):2362-71. PubMed PMID: 10679071.
  13. Verma AK, Pal AK, Manush SM, Das T, Dalvi RS, Chandrachoodan PP, et al. Persistent sub-lethal chlorine exposure augments temperature induced immunosuppression in Cyprinus carpio advanced fingerlings. Fish Shellfish Immunol. 2007 May;22(5):547-55. Epub 2006 Aug 16. PubMed PMID: 17046286.
  14. Banduseela VC, Ochala J, Chen YW, Göransson H, Norman H, Radell P, et al. Gene expression and muscle fiber function in a porcine ICU model. Physiol Genomics. 2009 Nov 6;39(3):141-59. doi: 10.1152/physiolgenomics.00026.2009. Epub 2009 Aug 25. PubMed PMID: 19706692.
Storage Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.
Avoid repeated freezing and thawing.
Shelf life: one year from despatch.
Format
Purification:
Affinity Chromatography on Protein G
Buffer System:
PBS, pH 7.2
Preservatives:
0.09% Sodium Azide
Stabilizers:
50% Glycerol
State:
Liquid purified IgG fraction
Aff - Purified
Specificity
Specificity:
This antibody Detects a ~70 kDa protein corresponding to the Molecular Mass of inducible HSP70 on SDS PAGE Immunoblots.
The mapped epitope is in the region of amino acid residues 436-503.
Does not cross-react with HSC70 (HSP73).
Species:
Human, Mouse, Rat, Bovine, C. elegans, Canine, Chicken, Drosophila, Fish (carp), Guinea Pig, Hamster, Monkey, Pig, Rabbit and Sheep.

Accessory Products

Proteins and/or Positive Controls

Proteins for Heat shock protein 70 / HSP70 (24 products)

Catalog No. Species Pres. Purity   Source  

Heat shock protein 70 / HSP70 (active)

Heat shock protein 70 / HSP70 Human Purified > 90 % pure as determined by SDS-PAGE analysis. E. coli
2x0.1 mg / €790.00
  OriGene Technologies GmbH

Heat shock protein 70 / HSP70 (active)

Heat shock protein 70 / HSP70 Human Purified > 90 % pure as determined by SDS-PAGE analysis. E. coli
0.1 mg / €455.00
  OriGene Technologies GmbH

Heat shock protein 70 / HSP70 (active)

Heat shock protein 70 / HSP70 Human Purified > 90 % pure as determined by SDS-PAGE analysis. E. coli
50 µg / €350.00
  OriGene Technologies GmbH

Heat shock protein 70 / HSP70 (active)

Heat shock protein 70 / HSP70 Human Aff - Purified > 95 % pure as determined by SDS-PAGE analysis E. coli
2x0.1 mg / €790.00
  OriGene Technologies GmbH

Heat shock protein 70 / HSP70 (active)

Heat shock protein 70 / HSP70 Human Aff - Purified > 95 % pure as determined by SDS-PAGE analysis E. coli
0.1 mg / €455.00
  OriGene Technologies GmbH

Heat shock protein 70 / HSP70 (active)

Heat shock protein 70 / HSP70 Human Aff - Purified > 95 % pure as determined by SDS-PAGE analysis E. coli
50 µg / €350.00
  OriGene Technologies GmbH

Heat shock protein 70 / HSP70 (1-641, His-tag)

Heat shock protein 70 / HSP70 Human Purified > 95 % pure by SDS PAGE E. coli
0.5 mg / €600.00
  OriGene Technologies GmbH

Heat shock protein 70 / HSP70 (1-641, His-tag)

Heat shock protein 70 / HSP70 Human Purified > 95 % pure by SDS PAGE E. coli
0.1 mg / €250.00
  OriGene Technologies GmbH

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human in vitro transl.
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human 12.5% SDS-PAGE Stained with Coomassie Blue. in vitro transl.
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human 12.5% SDS-PAGE Stained with Coomassie Blue. in vitro transl.
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human 12.5% SDS-PAGE Stained with Coomassie Blue. in vitro transl.
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human 12.5% SDS-PAGE Stained with Coomassie Blue. in vitro transl.
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

Heat shock protein 70 / HSP70 Human
  Abnova Taiwan Corp.

Heat shock protein 70 / HSP70

SDS-Page: Hsp70 Protein [NBC1-18356] - Dna K, 17.7kDa (163aa) with a purity of 95% by SDS - PAGE Protein
  Novus Biologicals Inc.

Heat shock protein 70 / HSP70

SDS-Page: Hsp70 Protein [NBC1-18357] - Dna K, 69kDa (638aa) with a purity of 95% by SDS - PAGE Protein
  Novus Biologicals Inc.

Heat shock protein 70 / HSP70

SDS-Page: Hsp70 Protein [NBC1-18358] - Dna K, 41.6kDa (384aa) with a purity of 95% by SDS - PAGE Protein
  Novus Biologicals Inc.

Heat shock protein 70 / HSP70

SDS-Page: Hsp70 Protein [NBC1-18359] - Dna K, 27.7kDa (255aa) with a purity of 95% by SDS - PAGE Protein
  Novus Biologicals Inc.

Heat shock protein 70 / HSP70

SDS-Page: Hsp70 Protein [NBC1-18360] - Dna K, 14.6kDa (132aa) with a purity of 95% by SDS - PAGE Protein
  Novus Biologicals Inc.

Heat shock protein 70 / HSP70

SDS-Page: Hsp70 Protein [NBC1-18367] - HSP70, 72.2kDa (661aa), confirmed by MALDI-TOF with a purity of 95% by SDS - PAGE Protein
  Novus Biologicals Inc.

Positive controls for Heat shock protein 70 / HSP70 (1 products)

Catalog No. Species Pres. Purity   Source  

Hsp70 Lysate

Western Blot: Hsp70 Lysate [NBL1-11749] - Western Blot experiments. 
Left-Control; Right -Over-expression Lysate for HSPA1A
  Novus Biologicals Inc.
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