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HSP70 antibody (FITC)

This Mouse Monoclonal antibody specifically detects HSP70 in FACS. It exhibits reactivity toward Human, Mouse, Rat, Chicken, Drosophila melanogaster, Cow, Pig, Monkey, Dog, Hamster, Sheep, Guinea Pig, Rabbit and Carp. It has been mentioned in 9+ publications
Catalog No. ABIN263935
$948.00
Plus shipping costs $50.00
0.2 mg
Shipping to: United States
Delivery in 1 to 2 Business Days

Quick Overview for HSP70 antibody (FITC) (ABIN263935)

Target

See all HSP70 Antibodies
HSP70 (Heat Shock Protein 70 (HSP70))

Reactivity

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Human, Mouse, Rat, Chicken, Drosophila melanogaster, Cow, Pig, Monkey, Dog, Hamster, Sheep, Guinea Pig, Rabbit, Carp

Host

  • 200
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Mouse

Clonality

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Monoclonal

Conjugate

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This HSP70 antibody is conjugated to FITC

Application

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Flow Cytometry (FACS)

Clone

C92F3A-5
  • 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)

    Isotype

    IgG1
  • Application Notes

    FACS (12). Flow cytometry.

    Restrictions

    For Research Use only
  • Concentration

    0.33 mg/mL

    Buffer

    PBS, pH 7.2, 0.01 % 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

    DO NOT FREEZE! This product is photosensitive and should be protected from light.

    Storage

    4 °C

    Storage Comment

    Store the antibody at 2 - 8 °C.
    Shelf life: one year from despatch.

    Expiry Date

    12 months
  • 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).

    Nelson, Manhardt, Kamath, Sui, Santamaria-Pang, Can, Bello, Corwin, Dinn, Lazare, Gervais, Sequeira, Peters, Ginty, Gerdes, Larsen: "Quantitative single cell analysis of cell population dynamics during submandibular salivary gland development and differentiation." in: Biology open, Vol. 2, Issue 5, pp. 439-47, (2013) (PubMed).

    Cheng, Djajadi, Molday: "Cell-specific markers for the identification of retinal cells by immunofluorescence microscopy." in: Methods in molecular biology (Clifton, N.J.), Vol. 935, pp. 185-99, (2012) (PubMed).

    Orr, Haffner, Nelson, Yegnasubramanian, Eberhart: "Decreased 5-hydroxymethylcytosine is associated with neural progenitor phenotype in normal brain and shorter survival in malignant glioma." in: PLoS ONE, Vol. 7, Issue 7, pp. e41036, (2012) (PubMed).

    Fang, Liu, Lin, Fan, Tsai, Tzeng: "Mps one binder 2 gene upregulation in the stellation of astrocytes induced by cAMP-dependent pathway." in: Journal of cellular biochemistry, Vol. 113, Issue 9, pp. 3019-28, (2012) (PubMed).

    Gui, Xiong, Yang, Li, Huang: "Effects of acupuncture on LIF and IL-12 in rats of implantation failure." in: American journal of reproductive immunology (New York, N.Y. : 1989), Vol. 67, Issue 5, pp. 383-90, (2012) (PubMed).

    Simão, Yadav, Narisawa, Bolean, Pizauro, Hoylaerts, Ciancaglini, Millán: "Proteoliposomes harboring alkaline phosphatase and nucleotide pyrophosphatase as matrix vesicle biomimetics." in: The Journal of biological chemistry, Vol. 285, Issue 10, pp. 7598-609, (2010) (PubMed).

    Miyoshi, Kasahara, Miyazaki, Shimizu, Taniguchi, Matsuzaki, Tohyama, Asanuma: "Pericentrin, a centrosomal protein related to microcephalic primordial dwarfism, is required for olfactory cilia assembly in mice." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 23, Issue 10, pp. 3289-97, (2009) (PubMed).

  • Target

    HSP70 (Heat Shock Protein 70 (HSP70))

    Alternative Name

    Heat Shock Protein 70 / HSP70

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

    Gene ID

    3303

    UniProt

    P08107
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