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Heat Shock 70 KDa (HSP70) antibody

Antigen

Heat Shock 70 KDa (HSP70)

Synonyms BIP, MIF2, GRP78, FLJ26106, Bip, Sez7, mBiP, Grp78, SEZ-7, Hsce70, AL022860, AU019543, D2Wsu17e, D2Wsu141e, hspa5a
Clonality Monoclonal
Host
Alternatives

Mouse

Reactivity
Alternatives

Human, Mouse (Murine), Rat (Rattus), Sheep (Ovine)

Application
Alternatives Immunohistochemistry (IHC), ELISA, Western Blotting (WB), Immunoprecipitation (IP)
Catalog no. ABIN233748
Quantity 100ug  (1.0 mg/ml (by UV absorbance at 280 ...)  (Variants)
Price 309.00 $   Plus shipping costs $35.00
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Additional Information

Alternative name Hsp70
Gene ID NP_005337
Swiss-Prot Q5JQI4
Immunogen This Protein G purified monoclonal antibody was prepared using conventional hybridoma technology after repeated immunizations with a synthetic peptide from the region of amino acid residues 436-503 of human Hsp70 protein.
Format Liquid (sterile filtered)
Isotype IgG  (Matching secondary antibodies)
Description Hsp70 genes encode abundant heat- inducible 70-kDa hsps (hsp70s). In most eukaryotes, hsp70 genes exist as part of a multigene family. Hsp70s 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 50% identity (2). The N-terminal two-thirds of hsp70s are more conserved than the C-terminal one-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.
Specificity This Protein G purified monoclonal antibody reacts with human Hsp70 protein. A BLAST analysis was used to suggest cross-reactivity with Hsp70 from human, bovine, mouse, rat, C.elegans, dog, chicken, Drosophila, carp, guinea pig, hamster, monkey, pig, rabbit and sheep sources based on 100% homology with the immunizing sequence. No cross-reactivity occurs with hsc70 (hsp73). Cross-reactivity with Hsp70 from other sources has not been determined.

Application Details

Application Notes This Protein G purified antibody has been tested for use in ELISA, immunofluorescence microscopy, western blotting, FACS, immunoelectron microscopy, immunohistochemistry and immunoprecipitation. Specific conditions for reactivity should be optimized by the end user. Expect a band approximately 70 kDa in size corresponding to Hsp70 by western blotting in the appropriate cell lysate or extract. In general, a 1:1,000 dilution is suggested for most applications and is suitable to detect Hsp70 in 20 u g of heat shocked HeLa cell lysate by western blotting.
Concentration 1.0 mg/ml (by UV absorbance at 280 nm)
Buffer Stabilizer: 50% (v/v) Glycerol. Preservative: 0.09% (w/v) Sodium Azide. Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2.
Storage Store vial at -20° C or below prior to opening. Dilute only prior to immediate use. For extended storage, aliquot contents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of opening.
Research Area Cancer, Heat Shock Proteins, Signaling
Restrictions For Research Use only