PUBLIC NOTICE OF PROPOSED ACQUISITION
National Eye Institute / National Institute of Health
Post Date: July 29, 2021
Closing Response Date: August 9, 2021
Proposed Award Date: August 12, 2021
Project Title: Production of larvae expressing Tyrp2 mutants, C30S and C61W to purify Tyrp2 mutant proteins
Contracting Office: National Eye Institute, Building 31, Room 6A52
Contact Point/Contracting Officer/Contract Specialist: Elaine Estrella, firstname.lastname@example.org
North American Classification System (NAICS) Code (include): 325414
Classification Code: Biological Product (except Diagnostic) Manufacturing
The research of our lab involves a genotype-to-phenotype study in ocular disease. We approach this task in several ways including experiments with recombinant proteins and their mutant variants. All these experiments require the production of large quantities of pure proteins (>10mg) for biochemical, biophysical, and structural protein characterization with the purpose to use these proteins as potential targets in drug screens. Recently we successfully purified in mg-quantities recombinant human tyrosinase and Tyrp1 intra-melanosomal domains, mutant variants, and de-glycosylated proteins in biologically active form.
Recently we successfully purified the human Tyrp2 intra-melanosomal domain, Tyrp2tr, in larvae. Dopachrome tautomerase Tyrp2 is a protein important for regulating eumelanin and phaeomelanin levels in melanosomes. Tyrp2 catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA). At present, we are interested to express 2 mutant variants of TYRP2 protein, C30S, and C61W, causing OCA8 disease in humans.
It will be important to understand the mechanism of protein-protein interaction in albinism. Therefore, we are interested in the in vitro study of the chemical reaction catalyzed by these three proteins, tyrosinase, Tyrp1, Tyrp2, and their mutant variants expressed at a large scale, which will permit us to mimic a chemical reaction occurring in vivo and analyze the products of the chemical reaction by using mass spectrometry and other methods.
The larval system is appropriate because we could easily scale up the protein production and purify protein in the Lab in large quantities using our original purification protocols.
- Design of Two unique Baculovirus expressing Tyrp2tr human protein with C-terminal
- Preparation of two Baculovirus expressing Tyrp2tr protein.
Payment will be made 30 days after internal receiving in NIH system.
NATIONAL EYE INSTITUTE/ NIH
10 CENTER DRIVE
BLDG 10 RM 5B47
BETHESDA MD 20892
BASIS OF AWARD
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Closing Statement: This notice is not a request for competitive proposals. However, interested parties may identify their interest and capability to respond to this notice. Responses to this notice shall contain sufficient information to establish the interested parties’ bona-fide capabilities for fulfilling the requirement and include: unit price, list price, shipping and handling costs, the delivery period after contract award, the prompt payment discount terms, the F.O.B. Point (Destination or Origin), the Dun & Bradstreet Number (DUNS), the Taxpayer Identification Number (TIN), and the certification of business size. All offerors must have an active registration in the System for Award Management (SAM) www.sam.gov
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