HSP70 (P. falciparum) Antibody

HSP70 proteins are a highly conserved family of 70-kDa molecular chaperones essential for protein folding, stabilization, and intracellular transport. In Plasmodium falciparum, the causative agent of the most severe form of human malaria, HSP70 plays a critical role in parasite survival and adaptation to host-induced stress. PfHSP70-I (PF08_0054) is the major cytosolic HSP70 isoform in P. falciparum, abundantly expressed during the blood stages of the parasite life cycle—constituting up to 1–2% of total parasite protein. Like other HSP70s, PfHSP70-I binds ATP with high affinity and exhibits ATPase activity that is stimulated by interaction with unfolded proteins. This activity is essential for preventing protein aggregation and ensuring proper folding under febrile conditions experienced during malaria infection. This antibody specifically recognizes PfHSP70-I, enabling precise detection of PfHSP70-I in parasite lysates and infected erythrocytes; monitoring of stress responses and chaperone dynamics during the parasite life cycle; and investigation of PfHSP70-I interactions with other chaperones such as PfHSP90 and PfHSP40.

0.15 µg/ml of SPC-186 was sufficient for detection of PfHSP70 in 20 µg of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

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