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 (C92F3A-5)

Host: Mouse

Reactivity: Human, Mouse (Murine), Rat (Rattus), Cow (Bovine), Chicken, Caenorhabditis elegans (C. elegans), Dog (Canine), Fruit Fly (Drosophila melanogaster), Carp, Hamster, Monkey, Pig (Porcine), Rabbit, Sheep (Ovine)

Application: Western Blotting (WB), ELISA, Immunocytochemistry (ICC), Immunohistochemistry (IHC), Flow Cytometry (FACS), Immunoelectron Microscopy (IEM)

Catalog no.: ABIN361708

Additional Information

Characteristics: Detects a ~70kDa 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).

Alternative name: Hsp70

Gene ID: 3303

Swiss-Prot: P08107

Immunogen: Human Hsp70

Format: Liquid

Isotype: IgG  (Matching secondary antibodies)

Clone: C92F3A-5

Description: 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 . 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. 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. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. 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. 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, Hsp72, HSPA1, HSPA1A, HSPA1B

Specificity: Detects a 70kDa 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. There is no cross-reactivity to hsc70 (hsp73). Species cross-reactivity: Human, mouse, rat, bovine, C. elegans, canine, chicken, Drosophila, fish [carp-Cyprinus carpio (13)], guinea pig, hamster, monkey, pig, rabbit, sheep.

Sensitivity: 1 µg/mL of SMC-100 was sufficient for detection of Hsp70 in 20µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Application Details

Concentration: 1 mg/mL

Purification: Protein G Purified

Buffer: PBS pH7.2, 50% glycerol

Storage: -20 °C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Cancer, Heat Shock Proteins, Signaling

Restrictions: For Research Use only

Images

Hsp70 (C92) Mouse Colon Cancer, Amplifier

Hsp70 (C92), Human Colon Cancer, Amplifier

Hsp70 (C92) Mouse Melanoma

Publications

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