To analyze a protein of interest, it is necessary to develop reagents that can detect it. Furthermore, to investigate the role of a protein in rheumatic disease models, it is frequently desirable to inject monoclonal antibodies (mAbs) or recombinant proteins that block the function of the protein in question. The Protein Core thus will be established to provide services through a 1) Hybridoma facility to produce mAbs; and 2) Production and Purification facility to produce high quality purified mAbs or recombinant proteins of interest. The production of new mAbs will take place in an established hybridoma facility that is particularly expert in generating Armenian hamster mAbs against mouse antigens. New services are planned including the development of rabbit hybridomas. The Production and Purification Facility will be newly established by first generating large quantities of purified mAbs from hybridomas using Protein A affinity chromatography. Other mAbs that are routinely used by RDCC investigators will be produced in large quantities and then purified. Once established, the facility will develop new services to produce large quantities of recombinant proteins carrying tags such as Fc, myc, and 6-His. Subsequent purification can then use standard affinity chromatography protocols. Thus, the facility will provide investigators with large quantities of proteins that can be used to analyze their molecules in relationship to rheumatic disease models.

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
Type
Center Core Grants (P30)
Project #
1P30AR048335-01
Application #
6552007
Study Section
Special Emphasis Panel (ZAR1)
Project Start
2001-09-28
Project End
2006-08-31
Budget Start
Budget End
Support Year
1
Fiscal Year
2001
Total Cost
Indirect Cost
Name
Washington University
Department
Type
DUNS #
062761671
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
Yokoyama, Christine C; Baldridge, Megan T; Leung, Daisy W et al. (2018) LysMD3 is a type II membrane protein without an in vivo role in the response to a range of pathogens. J Biol Chem 293:6022-6038
Wu, Xiaobo; Hutson, Irina; Akk, Antonina M et al. (2018) Contribution of Adipose-Derived Factor D/Adipsin to Complement Alternative Pathway Activation: Lessons from Lipodystrophy. J Immunol 200:2786-2797
Kulkarni, Hrishikesh S; Liszewski, M Kathryn; Brody, Steven L et al. (2018) The complement system in the airway epithelium: An overlooked host defense mechanism and therapeutic target? J Allergy Clin Immunol 141:1582-1586.e1
Triebwasser, Michael P; Wu, Xiaobo; Bertram, Paula et al. (2018) Timing and mechanism of conceptus demise in a complement regulatory membrane protein deficient mouse. Am J Reprod Immunol 80:e12997
Roberson, Elisha D O (2018) Motif scraper: a cross-platform, open-source tool for identifying degenerate nucleotide motif matches in FASTA files. Bioinformatics 34:3926-3928
Paing, May M; Salinas, Nichole D; Adams, Yvonne et al. (2018) Shed EBA-175 mediates red blood cell clustering that enhances malaria parasite growth and enables immune evasion. Elife 7:
Wilke, Georgia; Ravindran, Soumya; Funkhouser-Jones, Lisa et al. (2018) Monoclonal Antibodies to Intracellular Stages of Cryptosporidium parvum Define Life Cycle Progression In Vitro. mSphere 3:
Kulkarni, Hrishikesh S; Elvington, Michelle L; Perng, Yi-Chieh et al. (2018) Intracellular C3 Protects Human Airway Epithelial Cells from Stress-Associated Cell Death. Am J Respir Cell Mol Biol :
Garber, Charise; Vasek, Michael J; Vollmer, Lauren L et al. (2018) Astrocytes decrease adult neurogenesis during virus-induced memory dysfunction via IL-1. Nat Immunol 19:151-161
Knoop, Kathryn A; Gustafsson, Jenny K; McDonald, Keely G et al. (2017) Microbial antigen encounter during a preweaning interval is critical for tolerance to gut bacteria. Sci Immunol 2:

Showing the most recent 10 out of 156 publications