HSP70 antibody

Catalog No. ABIN263937

Product Details anti-HSP70 Antibody

Target: HSP70 (Heat Shock Protein 70 (HSP70))

Reactivity: Human, Mouse, Rat, Chicken, Drosophila melanogaster, Cow, Pig, Monkey, Dog, Hamster, Sheep, Guinea Pig, Rabbit, C. elegans, Carp

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSP70 antibody is un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunoprecipitation (IP), Flow Cytometry (FACS), Immunoelectron Microscopy (IEM), Immunohistochemistry (Frozen Sections) (IHC (fro)), Enzyme Immunoassay (EIA)

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).

Characteristics: Synonyms: HSP70.1, HSP70-1/HSP70-2, HSPA1A, HSPA1B, HSPA1, Heat shock 70 kDa protein 1A/1B

Purification: Affinity Chromatography on Protein G

Immunogen: Human HSP70 (1)

Clone: C92F3A-5

Isotype: IgG1

Application Details

Application Notes: ELISA (10). Western blot (7,8,14)1 μg/mL was sufficient for detection of HSP70 in 20 μg of HeLa lysate by colorimetric

Restrictions: For Research Use only

Handling

Concentration: 1.0 mg/mL

Buffer: PBS, pH 7.2, 0.09 % Sodium Azide, 50 % Glycerol

Preservative: Sodium azide

Precaution of Use: WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.

Handling Advice: Avoid repeated freezing and thawing.

Storage: 4 °C/-20 °C

Storage Comment: Store the antibody at 2-8 °C for one month or (in aliquots) at -28 °C for longer.
Shelf life: one year from despatch.

Expiry Date: 12 months

References for anti-HSP70 antibody (ABIN263937)

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-?B activation using a combination of regulatory mechanisms in microglia." in: PLoS computational biology, Vol. 10, Issue 2, pp. e1003471, (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).

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).

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).

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).

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).

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).

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).

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).

Morshed, Ma, Latif, Davies: "How one TSH receptor antibody induces thyrocyte proliferation while another induces apoptosis." in: Journal of autoimmunity, Vol. 47, pp. 17-24, (2013) (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).

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).

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).

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).

Zhang, Ahn, Benjamin, Honda, Hicks, Calabrese, Cole, Dinkova-Kostova: "HSF1-dependent upregulation of Hsp70 by sulfhydryl-reactive inducers of the KEAP1/NRF2/ARE pathway." in: Chemistry & biology, Vol. 18, Issue 11, pp. 1355-61, (2012) (PubMed).

Mitsuhashi, Yamaguchi, Kojima, Nakajima, Kasai: "Effects of HSP70 on the compression force-induced TNF-? 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).

Batista-Nascimento, Neef, Liu, Rodrigues-Pousada, Thiele: "Deciphering human heat shock transcription factor 1 regulation via post-translational modification in yeast." in: PLoS ONE, Vol. 6, Issue 1, pp. e15976, (2011) (PubMed).

Shipp, Watson, Jones: "Associations of HSP90 client proteins in human breast cancer." in: Anticancer research, Vol. 31, Issue 6, pp. 2095-101, (2011) (PubMed).

Target Details for HSP70

Target: HSP70 (Heat Shock Protein 70 (HSP70))

Alternative Name: Heat Shock Protein 70 / HSP70 (HSP70 Products)

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.Synonyms: HSP70-1/HSP70-2, HSP70.1, HSPA1, HSPA1A, HSPA1B, Heat shock 70 kDa protein 1A/1B

Gene ID: 3303

UniProt: P08107