You are viewing an incomplete version of our website. Please click to reload the website as full version.

HSP70 antibody (Heat Shock Protein 70)

Details for Product anti-HSP70 Antibody No. ABIN361707, Supplier: Log in to see
Antigen
  • APG-2
  • ARABIDOPSIS HEAT SHOCK PROTEIN 70
  • ATHSP70
  • CG5834
  • CG31354
  • chloroplast heat shock protein 70-2
  • cpHsc70-2
  • DmelCG5834
  • F19K16.12
  • F19K16_12
  • HEAT SHOCK PROTEIN 70
  • heat shock protein 70
  • HEAT SHOCK PROTEIN 70-7
  • HS24/P52
  • hsc70
  • HSC70-7
  • hsc71
  • hsp68
  • hsp70
  • Hsp70
  • HSP70
  • Hsp70-1
  • hsp70-5
  • Hsp70.1
  • hsp70B
  • HSP70B'
  • Hsp70Bb
  • hsp70Bb-prime
  • hsp70RY
  • Hsp110
  • HSPA1
  • HSPA6
  • HSPH2
  • irp94
  • K9P8.5
  • K9P8_5
  • LOC100305036
  • RY
Reactivity
Caenorhabditis elegans (C. elegans), Carp, Chicken, Cow (Bovine), Dog (Canine), Fruit Fly (Drosophila melanogaster), Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Pig (Porcine), Rabbit, Rat (Rattus), Sheep (Ovine)
641
305
298
142
130
125
125
87
79
77
74
68
65
63
56
52
41
41
38
38
35
22
22
20
19
18
18
17
8
6
5
5
4
4
3
3
3
3
3
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
Host
Mouse
412
322
42
18
Clonality (Clone)
Monoclonal ()
Conjugate
This HSP70 antibody is un-conjugated
34
34
24
24
22
22
20
19
19
19
19
19
19
19
19
19
19
12
11
8
7
5
5
5
5
5
5
5
5
5
3
3
3
3
3
3
1
1
1
Application
BioImaging (BI), Immunoelectron Microscopy (IEM), Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunofluorescence (IF), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
693
341
287
277
268
252
158
109
58
50
29
17
16
12
9
5
2
2
1
1
1
1
Supplier
Log in to see
Supplier Product No.
Log in to see
Request

Get this product for free

It's quick and easy to submit your validation proposal. I want to validate this product

Learn more

Available images

Immunogen Human HSP70
Clone C92F3A-5
Specificity Detects a ~70 kDa. Does not cross-react with HSC70 (HSP73).
Sensitivity 1 µg/mL of SMC-100 was sufficient for detection of Hsp70 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Alternative Name HSP70 (HSP70 Antibody Abstract)
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 C-terminal 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.
Cellular Localization: Cytoplasm
Gene ID 3303
NCBI Accession NP_005336
UniProt P08107
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:1000), IHC (1:10000), ICC/IF (1:1000), FACS (1:1000), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.1 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-HSP70 antibody (Heat Shock Protein 70) (ABIN361707) Hsp70 (C92) Mouse Melanoma.
 image for anti-HSP70 antibody (Heat Shock Protein 70) (ABIN361707) Hsp70 (C92), cell lines.
Product cited in: Ishikawa, Sakurai: "Heat-induced expression of the immediate-early gene IER5 and its involvement in the proliferation of heat-shocked cells." in: The FEBS journal, Vol. 282, Issue 2, pp. 332-40, 2015 (PubMed).

Katoh, Kubota, Kita, Nakatsu, Aoki, Mori, Maenaka, Takeda, Kidokoro: "Heat shock protein 70 regulates degradation of the mumps virus phosphoprotein via the ubiquitin-proteasome pathway." in: Journal of virology, Vol. 89, Issue 6, pp. 3188-99, 2015 (PubMed).

Sheppard, Sun, Khammash, Giffard: "Overexpression of heat shock protein 72 attenuates NF-κB activation using a combination of regulatory mechanisms in microglia." in: PLoS computational biology, Vol. 10, Issue 2, pp. e1003471, 2014 (PubMed).

Wijeratne, Xu, Scherz-Shouval, Marron, Rocha, Liu, Costa-Lotufo, Santagata, Lindquist, Whitesell, Gunatilaka: "Structure-activity relationships for withanolides as inducers of the cellular heat-shock response." in: Journal of medicinal chemistry, Vol. 57, Issue 7, pp. 2851-63, 2014 (PubMed).

Akkad, Corpeno, Larsson: "Masseter muscle myofibrillar protein synthesis and degradation in an experimental critical illness myopathy model." in: PLoS ONE, Vol. 9, Issue 4, pp. e92622, 2014 (PubMed).

Eroglu, Kimbler, Pang, Choi, Moskophidis, Yanasak, Dhandapani, Mivechi: "Therapeutic inducers of the HSP70/HSP110 protect mice against traumatic brain injury." in: Journal of neurochemistry, Vol. 130, Issue 5, pp. 626-41, 2014 (PubMed).

Muralidharan, Ambade, Fulham, Deshpande, Catalano, Mandrekar: "Moderate alcohol induces stress proteins HSF1 and hsp70 and inhibits proinflammatory cytokines resulting in endotoxin tolerance." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 193, Issue 4, pp. 1975-87, 2014 (PubMed).

Kanegasaki, Matsushima, Shiraishi, Nakagawa, Tsuchiya: "Macrophage inflammatory protein derivative ECI301 enhances the alarmin-associated abscopal benefits of tumor radiotherapy." in: Cancer research, Vol. 74, Issue 18, pp. 5070-8, 2014 (PubMed).

Berger, Ivanova, Gareau, Scherrer, Mazroui, Strub: "Direct binding of the Alu binding protein dimer SRP9/14 to 40S ribosomal subunits promotes stress granule formation and is regulated by Alu RNA." in: Nucleic acids research, Vol. 42, Issue 17, pp. 11203-17, 2014 (PubMed).

Dang, Tanabe, Tanaka, Tokumoto, Misumi, Saeki, Fujikuni, Ohdan: "Fasting enhances TRAIL-mediated liver natural killer cell activity via HSP70 upregulation." in: PLoS ONE, Vol. 9, Issue 10, pp. e110748, 2014 (PubMed).

Engels, Bilgic, Pinto, Vasquez, Wollschläger, Steinbrenner, Kellermann, Akhyari, Lichtenberg, Boeken: "A cardiopulmonary bypass with deep hypothermic circulatory arrest rat model for the investigation of the systemic inflammation response and induced organ damage." in: Journal of inflammation (London, England), Vol. 11, pp. 26, 2014 (PubMed).

Richter, Viergutz, Schwerin, Weitzel: "Prostaglandin E synthase interacts with inducible heat shock protein 70 after heat stress in bovine primary dermal fibroblast cells." in: Cytometry. Part A : the journal of the International Society for Analytical Cytology, Vol. 87, Issue 1, pp. 61-7, 2014 (PubMed).

Seguin, Morelli, Vinet, Amore, De Biasi, Poletti, Rubinsztein, Carra: "Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly." in: Cell death and differentiation, Vol. 21, Issue 12, pp. 1838-51, 2014 (PubMed).

Bauckman, Haller, Flores, Nanjundan: "Iron modulates cell survival in a Ras- and MAPK-dependent manner in ovarian cells." in: Cell death & disease, Vol. 4, pp. e592, 2013 (PubMed).

Aare, Radell, Eriksson, Akkad, Chen, Hoffman, Larsson: "Effects of corticosteroids in the development of limb muscle weakness in a porcine intensive care unit model." in: Physiological genomics, Vol. 45, Issue 8, pp. 312-20, 2013 (PubMed).

Santagata, Xu, Wijeratne, Kontnik, Rooney, Perley, Kwon, Clardy, Kesari, Whitesell, Lindquist, Gunatilaka: "Using the heat-shock response to discover anticancer compounds that target protein homeostasis." in: ACS chemical biology, Vol. 7, Issue 2, pp. 340-9, 2012 (PubMed).

Abisambra, Jinwal, Suntharalingam, Arulselvam, Brady, Cockman, Jin, Zhang, Dickey: "DnaJA1 antagonizes constitutive Hsp70-mediated stabilization of tau." in: Journal of molecular biology, Vol. 421, Issue 4-5, pp. 653-61, 2012 (PubMed).

Larkins, Murphy, Lamb: "Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers." in: American journal of physiology. Cell physiology, Vol. 303, Issue 6, pp. C654-65, 2012 (PubMed).

Chanoux, Robay, Shubin, Kebler, Suaud, Rubenstein: "Hsp70 promotes epithelial sodium channel functional expression by increasing its association with coat complex II and its exit from endoplasmic reticulum." in: The Journal of biological chemistry, Vol. 287, Issue 23, pp. 19255-65, 2012 (PubMed).

Mitsuhashi, Yamaguchi, Kojima, Nakajima, Kasai: "Effects of HSP70 on the compression force-induced TNF-α and RANKL expression in human periodontal ligament cells." in: Inflammation research : official journal of the European Histamine Research Society ... [et al.], Vol. 60, Issue 2, pp. 187-94, 2011 (PubMed).