The Mouse Monoclonal anti-HSP70 antibody is suitable to detect HSP70 in samples from Human, Mouse, Rat, Drosophila melanogaster, Fish, Saccharomyces cerevisiae, Amphibian, Rabbit and Avian. It has been validated for WB, IF, IP and IHC (p).
This antibody detects several members of the heat shock protein 70 kDa gene family including Hsp70, Hsc70, Grp78, and following heat shock, Hsp72. Immunfluorescence staining of Hsp70 in heat shocked HeLa cells results in cytoplasmic staining.
Cross-Reactivity (Details)
Species reactivity (tested):Human, Mouse, Rat, Amphibian, Bird, Fish, Rabbit, Saccharomyces cerevisiae, Fruit Fly
Immunocytochemistry. Immunohistochemistry on frozen sections. Immunflourescence. Immunoprecipitation. Western blot: 1 - 1000. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions
For Research Use only
Concentration
1.0 mg/mL
Buffer
PBS pH 7.2, 50 % Glycerol, 0.09 % Sodium Azide
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 up to one month or (in aliquots) at -20 °C for longer. Shelf life: one year from despatch.
Expiry Date
12 months
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 (1). 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 (2). 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 (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). 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 (5). 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