We’ve developed a new approach to CD47 blockade that is designed to maximize clinical activity and minimize toxicities

Our goal is to transform cancer treatment options for patients by developing evorpacept (ALX148) as a foundational checkpoint immunotherapy

Evorpacept Mechanism of Action

ALX Oncology was founded by a team of industry veterans to address fundamental challenges in blocking CD47 and to realize the full potential of this therapeutic target.

Cancer cells employ CD47, a cell surface protein, as a “don’t eat me” signal to evade detection by the immune system. ALX is developing a next-generation checkpoint inhibitor designed to have a high affinity for CD47 and to avoid the limitations caused by hematologic toxicities inherent in other CD47 blocking approaches. We believe our lead product candidate, evorpacept (ALX148), will have a wide therapeutic window to block the “don’t eat me” signal on cancer cells, and to leverage the immune activation of broadly used anti-cancer agents through combination strategies. Based on our clinical results to date in multiple oncology indications showing encouraging anti-tumor activity and tolerability, our strategy is to pursue evorpacept as a potentially critical component for future combination treatments in oncology.

Latest News updated at 08:23:45 UTC

May 11, 2023

ALX Oncology Reports First Quarter 2023 Financial Results and Provides Clinical Development and Operational Highlights

May 09, 2023

ALX Oncology Announces First Patient Dosed in Phase 2 Investigator-Sponsored Trial of Evorpacept in Patients with Ovarian Cancer

Apr 25, 2023

ALX Oncology Announces Clinical Trial Collaboration with Sanofi to Evaluate Evorpacept in Combination with SARCLISA (isatuximab-irfc) in Patients with Multiple Myeloma

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Our Technology

ALX Oncology’s fusion proteins are engineered to bind CD47 with significantly greater affinity than natural SIRPα. Our lead candidate, evorpacept, is an intravenously administered fusion protein containing two engineered high affinity CD47 binding domains of SIRPα linked to an inactive Fc region of human immunoglobulin.

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