SAM #75N98026Q00506

Custom Antibody Development for Lysine Homocysteinylation Detection in Cobalamin Disorders

The National Institutes of Health (NIH) Office of Logistics and Acquisition Operations (OLAO), under the Department of Health and Human Services, is soliciting services for the development and validation of a novel antibody targeting lysine homocysteinylation in cobalamin disorders. - Government Buyer: - Department of Health and Human Services (HHS) - National Institutes of Health (NIH) - Office of Logistics and Acquisition Operations (OLAO) - Products/Services Requested: - Custom development and validation of a post-translational modification (PTM)-specific polyclonal antibody for N-homocysteinylation of lysine - Synthesis and purification of peptide antigens with N-homocysteinylated lysine residues and matched controls - Conjugation of peptides to carrier proteins - Immunization of rabbits and generation of polyclonal sera - ELISA screening for antibody specificity - Terminal bleed and purification of the working antibody - Characterization of antibody specificity and utility in disease models - Unique/Notable Requirements: - No commercial antibody currently exists for this target; requires custom synthesis - Supports research on rare genetic diseases and precision medicine - Antibody will be used to characterize proteins affected by N-homocysteinylation - OEMs and Vendors: - No specific OEMs or commercial vendors are named in the solicitation

Description

Requirements:

The proposed development of a novel post-translational modification (PTM)-specific antibody directly supports the U.S. Government's mission to advance biomedical research on rare genetic diseases, improve public health outcomes, and accelerate the development of precision medicine approaches

Currently there is no commercially available antibody against N-homocysteine-lysine (N-homocysteinylation) so we will need to have one generated. By generating it, we are able to provide specifications for the peptide sequence based on preliminary findings in our scientific models of disease insuring it will work effectively. Our objectives are as follows:  

Synthesize and purify peptide antigens with N-homocysteinylated lysine residues and matched control peptides with unmodified lysines.  Conjugate peptides to carrier proteins (e.g., KLH) for immunization  Immunize appropriate host species (rabbit for polyclonal antibody generation)  Generate polyclonal sera prior to immunization and 2 to 3 times after following antigen boost. Test sera on lab samples of N-homocysteinylated proteins from mouse models of MMACHC delicacy in our lab. Also perform ELISA screening of antibody on modified and unmodified peptide.   Terminal bleed on immunized animal and purification of working antibody from serum  With working antibody we will characterize the proteins affected by this aberrant posttranslational modification to better understand disease development and in future design targeted therapies for it. 

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