Heat Shock 70kDa Protein 8 (HSPA8) antibody

Antigen: Heat Shock 70kDa Protein 8 (HSPA8)

Synonyms: LAP1, HSC54, HSC70, HSC71, HSP71, HSP73, NIP71, HSPA10, MGC29929, MGC131511

Clonality: Monoclonal (BB70)

Host: Mouse

Reactivity: Human, Mouse (Murine), Rat (Rattus), Sheep (Ovine), Dog (Canine), Beluga, Cow (Bovine), Fish, Scallop, Hamster, Rabbit, Chicken, Xenopus laevis, Fruit Fly (Drosophila melanogaster), Yeast (Pichia pastoris)

Application: Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC)

Catalog no.: ABIN361710

Additional Information

Characteristics: Detects ~72 and ~73kDa proteins corresponding to the molecular mass of inducible Hsp and Hsc on SDS PAGE immunoblots.

Alternative name: Hsp70/Hsc70

Gene ID: 423504

Swiss-Prot: P08106

Immunogen: Chicken Hsp70/Hsp90 complex

Format: Liquid

Isotype: IgG2a  (Matching secondary antibodies)

Clone: BB70

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: HSC54, Hsc70, HSC71, Hsp70 1, Hsp701/Hsp70 2, Hsp70.1, Hsp71, Hsp72, Hsp73, HSPA1, HSPA10, HSPA1A, HSPA1B, LAP1, NIP71

Specificity: Detects 72 and 73kDa proteins corresponding to the molecular mass of inducible hsp and hsc70 on SDS PAGE immunoblots. Species cross-reactivity: Human, mouse, rat, sheep, dog, beluga, bovine, fish (carp, rainbow trout, Chinook/Chum/Coho salmon), pacific oyster, guinea pig, scallop pig, hamster, rabbit, chicken, Artemia, Xenopus, Drosophila, and yeast.

Sensitivity: 1 µg/mL of SMC-106 was sufficient for detection of Hsp70 and Hsc70 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: Heat Shock Proteins

Restrictions: For Research Use only

Images

Hsp70-Hsc70 ( BB70), rat nuclear smears and liver sections (top control)

Hsp70Hsc70 (BB70), heat shock Hela

Hsp70Hsc70 (BB70), Human Colon Cancer, Amplifier