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

Our mission is to transform cancer treatment for patients by developing evorpacept as a first-in-class 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 00:00:15 UTC

Dec 18, 2024

ALX Oncology to Present Updated Results from Phase 2 ASPEN-06 Clinical Trial of Evorpacept in Patients with HER2-Positive Gastric Cancer in Oral Presentation at 2025 ASCO Gastrointestinal Cancers Symposium

Dec 12, 2024

ALX Oncology to Host Virtual Company Event Highlighting New Clinical Data Presented at SABCS 2024

Dec 10, 2024

ALX Oncology Announces New Data Demonstrating Evorpacept in Combination with Zanidatamab Generates Promising Antitumor Activity in Advanced Breast Cancer

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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