PfHSP70

Plasmodium Falciparum HSP70 Recombinant
Cat. No.
BT28586
Source
Synonyms
Appearance
Sterile Filtered clear solution.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

The E.Coli derived recombinant Plasmodium falciparum contains the Plasmodium falciparum HSP70 protein epitopes 33-114 amino acids.

Product Specs

Introduction
Heat shock proteins (HSPs) produced by the malaria parasite Plasmodium falciparum play a role in the immune system's response to infection, potentially contributing to disease severity. Among these, PfHSP70s are particularly important due to their potential involvement in parasite adaptation and their ability to trigger a strong immune response. This has made them a key target in the development of protective immunity against malaria.
Description
This recombinant Plasmodium falciparum HSP70 protein, derived from E. coli, encompasses amino acids 33 to 114 of the full PfHSP70 sequence.
Purity
The protein exhibits a purity exceeding 95%, confirmed through two methods: 10% PAGE with Coomassie staining and RP-HPLC.
Physical Appearance
The product appears as a clear solution that has undergone sterile filtration.
Formulation
The protein is supplied in a buffer composed of 150mM Imidazole (pH 8.0), 150mM NaCl, 150mM Sodium Phosphate, and 50% glycerol.
Stability
For optimal storage, PfHSP70 should be maintained at a temperature below -18°C. While it can remain stable at 4°C for up to one week, it is crucial to minimize freeze-thaw cycles to preserve its integrity.
Applications
This product is intended for research use as an antigen in ELISA and Western Blot applications.
Purification Method

Purified by proprietary chromatographic technique

Product Science Overview

Introduction

Plasmodium falciparum is the primary causative agent of the most severe form of human malaria. The parasite’s survival and pathogenicity are heavily reliant on a family of proteins known as heat shock proteins (HSPs). Among these, the heat shock protein 70 (HSP70) family plays a crucial role in the parasite’s ability to withstand the physiological stresses encountered during its life cycle.

Heat Shock Proteins (HSPs)

Heat shock proteins are a group of highly conserved proteins that function as molecular chaperones. They assist in the proper folding of nascent polypeptides, the refolding of misfolded proteins, and the prevention of protein aggregation. HSPs are upregulated in response to various stress conditions, including heat shock, oxidative stress, and infection.

HSP70 Family in Plasmodium falciparum

The HSP70 family in Plasmodium falciparum consists of six members, each localized to different subcellular compartments. One of the most studied members is PfHSP70-x, which is exported to the infected erythrocyte. These proteins are essential for the parasite’s survival and are involved in various cellular processes, including protein folding, translocation, and degradation .

Recombinant HSP70

Recombinant HSP70 refers to the HSP70 protein that has been genetically engineered and produced in a host organism, such as Escherichia coli. This recombinant protein is used in various research applications to study its structure, function, and interactions with other proteins. The production of recombinant HSP70 involves cloning the gene encoding the protein into an expression vector, transforming the host organism with the vector, and inducing the expression of the protein.

Biological Functions and Importance

HSP70 proteins are central to cellular proteostasis, ensuring the proper folding and functioning of other proteins. In Plasmodium falciparum, HSP70 proteins are implicated in the parasite’s ability to survive under the stressful conditions encountered in the human host. They are also involved in the development of antimalarial drug resistance, making them potential targets for new therapeutic interventions .

Research and Therapeutic Potential

The study of recombinant HSP70 proteins from Plasmodium falciparum has provided valuable insights into their structure-function relationships and their role in the parasite’s biology. These proteins are considered potential targets for antimalarial drug development, especially in combination therapies aimed at overcoming drug resistance. Additionally, HSP70 proteins are involved in modulating the host immune response, further highlighting their importance in the pathogenesis of malaria .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.