Scholar Rock is delivering muscle-targeted breakthroughs to transform the treatment of spinal muscular atrophy (SMA) and other rare neuromuscular diseases where muscle atrophy remains a critical unmet need.
As a global leader in myostatin biology, a field focused on proteins that regulate muscle mass, the biopharmaceutical company is named for the visual resemblance of a scholar rock to protein structures. Our commitment to unlock fundamentally different treatment approaches is powered by broad application of a proprietary platform, which has developed novel monoclonal antibodies to modulate protein growth factors with extraordinary selectivity. Scholar Rock works every day to create new possibilities for patients through its highly innovative anti-myostatin program, including opportunities in additional rare neuromuscular diseases. Learn more about our neuromuscular franchise at ScholarRock.com and follow @ScholarRock on X and on LinkedIn.
Summary of Position:
At Scholar Rock, we strive to develop best-in-class antibody-based therapeutics across multiple disease areas by leveraging our Antibody Engineering and Structural Biology expertise. Scholar Rock is seeking highly motivated, energetic and collaborative Senior Scientist to join the Antibody Discovery and Engineering group. The successful candidate will design and execute antibody discovery and optimization campaigns using phage display and yeast display technology, contribute to the development and application of display-based screening strategies, and advance high-quality leads through biochemical and biophysical characterization. Hands-on experience with phage display is required; experience with yeast display is preferred. Experience in recombinant protein purification and characterization are highly desirable.
Position Responsibilities
Design, execute, and troubleshoot antibody discovery campaigns using phage display, including library screening, selection strategy development, clone recovery, and sequence analysis.
Optimizing antibody leads with display-based technologies, including affinity maturation, specificity engineering, and developability-focused screening.
Express and purify recombinant antibodies, antibody fragments, antigens, and related proteins using appropriate chromatographic methods.
Characterize binding, specificity, affinity, stability, purity, and other biochemical or biophysical properties of antibody candidates.
Analyze and interpret experimental data, maintain clear records, and communicate results and recommendations to project teams.
Collaborate cross-functionally with protein sciences, structural biology, assay biology, and therapeutic-area teams to advance discovery programs.
Evaluate and implement new technologies, workflows, and automation opportunities that strengthen antibody discovery and optimization capabilities.
Provide scientific leadership for project workstreams and mentor junior colleagues as appropriate.
Candidate Requirements
Ph.D. in biochemistry, molecular biology, protein engineering, biophysics, or a related life-science field with relevant industry or postdoctoral experience; or an M.S./B.S. with commensurate relevant experience. Level will be determined by qualifications and experience.
Hands on experience with antibody discovery and optimization using phage display is required, yeast display experience is highly preferred.
Working knowledge of antibody formats, library design or screening principles, molecular biology, and sequence-based clone assessment.
Experience with protein purification techniques such as affinity, ion-exchange, and size-exclusion chromatography.
Ability to characterize proteins and antibodies using biochemical and biophysical methods such as SPR, BLI, ELISA, and flow cytometry.
Strong experimental design, problem-solving, documentation, communication, and teamwork skills.
Experience in applying structural insights to antibody design and optimization is preferred.
Scholar Rock is an Equal Opportunity Employer. We celebrate diversity and are committed to creating an inclusive environment for all employees.
