Abstract: Identification of immunodominant Babesia microti antigens using genome-wide immunoscreening is described. Candidate antigens were screened against sera from patients with clinical babesiosis. Also described are diagnostic assays with high sensitivity and specificity for detecting B. microti-specific antibodies in patient samples using the identified immunodominant antigens.

Abstract: Identification of immunodominant Babesia microti antigens using genome-wide immunoscreening is described. Candidate antigens were screened against sera from patients with clinical babesiosis. Also described are diagnostic assays with high sensitivity and specificity for detecting B. microti-specific antibodies in patient samples using the identified immunodominant antigens.

Abstract: Identification of immunodominant Babesia microti antigens using genome-wide immunoscreening is described. Candidate antigens were screened against sera from patients with clinical babesiosis. Also described are diagnostic assays with high sensitivity and specificity for detecting B. microti-specific antibodies in patient samples using the identified immunodominant antigens.

Abstract: Identification of immunodominant Babesia microti antigens using genome-wide immunoscreening is described. Candidate antigens were screened against sera from patients with clinical babesiosis. Also described are diagnostic assays with high sensitivity and specificity for detecting B. microti-specific antibodies in patient samples using the identified immunodominant antigens.

Abstract: Human cathepsin L inhibitors and probes containing a vinyl sulfonate ester moiety are described. The inhibitors are highly potent (low nM affinity), selective, and cell permeable, and can inhibit ultra-low concentration of active cathepsin L. The developed probes are highly sensitive and can detect an ultra-low amount of probe-labeled active cathespin L.

Abstract: Human cathepsin L inhibitors and probes containing a vinyl sulfonate ester moiety are described. The inhibitors are highly potent (low nM affinity), selective, and cell permeable, and can inhibit ultra-low concentration of active cathepsin L. The developed probes are highly sensitive and can detect an ultra-low amount of probe-labeled active cathespin L.

Abstract: In this application is described the expression and purification of a recombinant Plasmodium falciparum (3D7) LSA-NRC polypeptide. The method of the present invention produces a highly purified polypeptide which is useful as a vaccine and as a diagnostic reagent.

Abstract: Provided are compounds capable of covalently binding to a protein tyrosine phosphatase (PTP). The compounds comprise Formula A: Also provided are compositions comprising one of the above compounds covalently bound to a member of the PTP superfamily, methods of labeling a PTP using the compounds, methods of isolating a PTP from a mixture of proteins using the compounds, methods of evaluating whether a substance is an inhibitor of a PTP using the compounds, methods of evaluating the specificity of an inhibitor of a PTP using the compounds, methods of identifying a PTP involved in a disease in a mammal using the compounds, and methods of diagnosing a disease in a mammal using the compounds.

Abstract: In this application is described the expression and purification of a recombinant Plasmodium falciparum (3D7) LSA-NRC polypeptide. The method of the present invention produces a highly purified polypeptide which is useful as a vaccine and as a diagnostic reagent.

Abstract: In this application is described the expression and purification of a recombinant Plasmodium falciparum (3D7) LSA-NRC polypeptide. The method of the present invention produces a highly purified polypeptide which is useful as a vaccine and as a diagnostic reagent.

Abstract: In this application is described the expression and purification of a recombinant Plasmodium falciparum (3D7) LSA-NRC polypeptide. The method of the present invention produces a highly purified polypeptide which is useful as a vaccine and as a diagnostic reagent.

Abstract: Provided are compounds capable of covalently binding to a protein tyrosine phosphatase (PTP). The compounds comprise Formula A: Also provided are compositions comprising one of the above compounds covalently bound to a member of the PTP superfamily, methods of labeling a PTP using the compounds, methods of isolating a PTP from a mixture of proteins using the compounds, methods of evaluating whether a substance is an inhibitor of a PTP using the compounds, methods of evaluating the specificity of an inhibitor of a PTP using the compounds, methods of identifying a PTP involved in a disease in a mammal using the compounds, and methods of diagnosing a disease in a mammal using the compounds.

Abstract: A purified peptide which induces proliferation or activation of cytotoxic T cells specifically against circumsporozoite protein of P. falciparum is described. The peptide has an amino acid sequence KPKDELDYENDIEKKICKMEKCS in single letter amino acid code.