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Plasmodium Vivax MSP1 Protein

$403.02$1,414.33 excl. VAT

This product is a recombinant protein expressed and purified from E. coli and can be used with Plasmodium falciparum MSP1 for developing ELISA and rapid test assays.


Plasmodium vivax MSP1 is a recombinant MSP1 protein expressed and purified from E. coli.



  • Plasmodium vivax MSP1 produced in E. coli,
  • Presented in phosphate buffered saline with 25mM arginine.
  • Can be used with Plasmodium falciparum MSP1 for ELISA and rapid test.



Merozoite surface proteins (MSP) are integral and peripheral proteins found on the membrane of merozoites, of the Plasmodia genus. During the asexual blood stage of Plasmodia’s life cycle, the parasite invades red blood cells to replicate, resulting in the common symptoms of malaria infection. The MSP surface protein complexes are involved in multiple interactions between Plasmodium and red blood cells to facilitate pathogenesis (Kadekoppala and Holder, 2010).

The merozoite surface proteins, MSP-1 and MSP-2 are the most abundant proteins on the surface of merozoites, constituting 40% of the GPI-anchored proteins on its cell surface (Cowan, et al., 2011). MSP-1 is essential in the pathogenesis of the merozoite’s blood stage, facilitating erythrocyte invasion and cell rupture. MSP-1 is first synthesized as 190-kDa precursor protein, which is deposited at the surface of the developing merozoite cell via its GPI anchor (Kauth, et al., 2003). Before invasion of a red blood cell, the GPI-anchored MSP-1 precursor protein is processed into four major MSP-1 subunits (Jaschke, et al., 2017). During invasion of the red blood cell, the merozoite then attaches to the host cell using the MSP-1 complex to gain entry. The majority of the MSP complex is then released upon entry into the host cell, though a small portion of the MSP-1 C-terminus (MSP-119) is retained. While the role of MSP-119 in unclear, it currently serves as a marker for the formation of the merozoite food vacuole (Blackman et al., 1990).

Merozoite surface proteins have been key targets for the development of malaria vaccines, with the aim of halting parasitic growth at the key stages of its life complex cycle. The MSP-1 protein interacts with several other MSPs to form protein complexes at the cell surface, which can all be inhibited by anti MSP-1 antibodies to disrupt plasmodia’s growth. However, the sequences encoding proteins such as MSP-1 vary greatly depending on the region they are found in, which makes them challenging targets for effective therapeutics.



  • Blackman et al. (1990). A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion- inhibiting antibodies. J Exp Med. 172(1): 379–382.
  • Cowan et al. (2011). A Malaria Vaccine Based on the Polymorphic Block 2 Region of MSP-1 that Elicits a Broad Serotype-Spanning Immune Response. PLoS One. 6(10).
  • Jascke, et al. (2017). Merozoite Surface Protein 1 from Plasmodium falciparum Is a Major Target of Opsonizing Antibodies in Individuals with Acquired Immunity against Malaria. Clin Vaccine Immunol. 24(11).
  • Kadekoppala and Holder (2010). Merozoite surface proteins of the malaria parasite: The MSP1 complex and the MSP7 family. International Journal for Parasitology. Volume 40, Issue 10, Pages 1155-1161.

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