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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 (N27F3-4)
Host
Alternatives

Mouse

Reactivity
Alternatives

Human, Mouse (Murine), Rat (Rattus), Cow (Bovine), Chicken, Caenorhabditis elegans (C. elegans), Beluga, Dog (Canine), Fruit Fly (Drosophila melanogaster), Fish, Hamster, Monkey, Pig (Porcine), Plant, Rabbit, Sheep (Ovine), Xenopus laevis

Application
Alternatives Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), Flow Cytometry (FACS), Immunoelectron Microscopy (IEM)
Catalog no. ABIN361706
Quantity 200µg  (1 mg/mL)  (Variants)
Price 351.00 $   Plus shipping costs $35.00
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Availability Ships within 7 to 10 Business Days

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 3303
Swiss-Prot P08107
Immunogen Recombinant Hsp70/hsc70
Format Liquid
Isotype IgG  (Matching secondary antibodies)
Clone N27F3-4
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 72 and 73kDa proteins corresponding to the molecular mass of inducible hsp and hsc70 on SDS PAGE immunoblots. Species cross-reactivity: Human, mouse, rat, bovine, C. elegans, beluga, canine, chicken, Drosophila, fish (carp, Chinook/Chum/Coho salmon, rainbow trout), guinea pig, hamster, monkey, pig, plant (cumcumber/pea) rabbit, sheep, Xenopus.
Sensitivity 1 µg/mL of SMC-104 was sufficient for detection of Hsp70/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