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: Polyclonal

Host: Rabbit

Reactivity: Plasmodium falciparum

Catalog no.: ABIN361730

Additional Information

Alternative name: Hsp70

Immunogen: His-tagged and purified PfHsp70, C-terminus

Format: Protein A purified

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 (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. PfHsp70-I (PF08_0054) is the major cytosolic Hsp70 in Plasmodium falciparum. It is abundantly expressed in the blood stages of the parasite and is thought to constitute 1-2% of total parasite protein. It is induced upon heat shock. It is present in the pasrasite in different complexes with PfHsp90 and some PfHsp40 (6, 7).

Specificity: This protein A affinity purified antibody detects ~70kDa protein, corresponding to P. falciparum PfHsp70 on SDS PAGE immunoblots, in samples from P. falciparum origins. Species cross-reactivity: It is species specific to P. falciparum, and does not cross-react to any protein from erythrocytes.

Application Details

Application Notes: A 1:2000 dilution for WB, a 1:50 for IF. Higher dilutions can be tried.

Concentration: 0.318mg/ml

Buffer: In PBS pH 7.4, 50% glycerol, 0.09% azide. Protein A affinity purified.

Storage: -20°C, 1 year+, shipped on cold packs or ambient

Research Area: Cancer, Heat Shock Proteins, Signaling

Restrictions: For Research Use only

Images

PfHsp70, malarial parasite lysate