Antibody-Drug Conjugate (ADC) Target Proteins

The target antigen plays a crucial role in distinguishing cancer cells from normal cells, thereby reducing off-target toxicity. Therefore, the selection of the appropriate target antigen is the initial step in developing an ideal ADC.
Specific Expression:The target antigen should be highly expressed on the surface of cancer cells compared to healthy cells[1], to reduce off-target effects and related toxicity. Ideally, the target antigen should be located on the cell surface or extracellular domain, rather than intracellular antigens, so that antibody-drug conjugates can effectively recognize and bind in the circulatory system.
Non-secretory:The target antigen should be non-secretory to avoid excessive secretion of antigens causing non-specific binding of antigen-antibody complexes in circulation, which would lead to non-specific binding of ADCs outside the tumor site, thereby reducing drug targeting and potentially increasing safety risks[2].
Internalization Properties:After binding with antibody, the target antigen should be able to effectively internalize into tumor cells, ensuring that ADC complexes enter cells through endocytosis, and then promote rapid release of cytotoxic payloads through appropriate intracellular transport pathways[3] to exert anti-tumor effects.
ACROBiosystems has developed over 90 high-quality ADC target proteins, covering Human, Mouse, Cynomolgus, Rat and other species with multiple tags, featuring high purity and bioactivity, suitable for immunization, antibody screening, species cross-validation, quality control release, pharmacokinetic studies and various application scenarios.

Product Features

Comprehensive coverage of 90+ hot ADC target proteins;

Multiple species and tags;

Proteins with uniform structure and high purity verified by SEC-MALS;

High bioactivity validated by ELISA/SPR/BLI/FACS, etc.

Validation Data

High purity verified by SEC-MALS

Dimer structure and purity of PSMA verified by SEC-MALS
PSMA dimer verified by SEC-MALS

The purity of Mouse PSMA Protein, Fc Tag (Cat. No. PSA-M5266) is more than 90% and the molecular weight of this protein is around 240-280 kDa verified by SEC-MALS.

High purity of LRRC15 verified by SEC-MALS
LRRC15 SEC-MALS verification high purity

The purity of Biotinylated Human LRRC15, His,Avitag (Cat. No. LR5-H82E4) is more than 90% and the molecular weight of this protein is around 80-95 kDa verified by SEC-MALS.

The binding activity verified by ELISA

PSMA binding activity verified by ELISA

Immobilized Monoclonal Anti-Human PSMA Antibody, Human IgG1 at 2 μg/mL (100 μL/well) can bind Human PSMA, His Tag (Cat. No. PSA-H52H3) with a linear range of 2-39 ng/mL (QC tested).

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TROP-2 binding activity verified by ELISA

Immobilized Human TROP-2, His Tag (Cat. No. TR2-H5223) at 1 μg/mL (100 μL/well) can bind Mouse Monoclonal Antibody Against Human TROP-2, Mouse IgG1 with a linear range of 0.1-2 ng/mL (QC tested).

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Claudin-18.2 binding activity verified by ELISA

Immobilized Human Claudin-18.2 Full Length Protein-VLP (Cat. No. CL2-H52P7) at 5 μg/mL (100 μL/well) can bind Monoclonal Anti-Chimeric Claudin-18.2 Antibody, Human IgG1 with a linear range of 0.2-3 ng/mL (QC tested).

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B7-H4 binding activity verified by ELISA

Immobilized Human B7-H4, His Tag (Cat. No. B74-H5222) at 2 μg/mL (100 μL/well) can bind Anti-B7-H4 MAb (Human IgG1) with a linear range of 0.2-6 ng/mL (QC tested).

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The binding activity verified by SPR

TROP-2 binding activity verified by SPR

Captured Trop2 antibody on CM5 chip via anti-mouse antibodies surface can bind Human TROP-2, His Tag (Cat. No. TR2-H5223) with an affinity constant of 5.98 nM as determined in a SPR assay (Biacore T200) (Routinely tested).

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CDH17 binding activity verified by SPR

Anti-Cadherin-17 antibody captured on CM5 chip via Anti-human IgG Fc antibodies surface can bind Human Cadherin-17, His Tag (Cat. No. CA7-H52H3) with an affinity constant of 2.9 μM as determined in a SPR assay (Biacore 8K) (Routinely tested).

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Nectin-4 binding activity verified by SPR

Mouse Anti-Nectin-4 Antibody (Mouse IgG1) captured on CM5 chip via anti-mouse antibodies surface can bind Human Nectin-4, His Tag (Cat. No. NE4-H52H3) with an affinity constant of 58.2 nM as determined in a SPR assay (Biacore T200) (Routinely tested).

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FRα binding activity verified by SPR

Biotinylated Human FOLR1, His,Avitag (Cat. No. FO1-H82E2) immobilized on SA Chip can bind Folic acid-BSA with an affinity constant of 83.8 pM as determined in a SPR assay (Biacore 8K) (Routinely tested).

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The binding activity verified by BLI

B7-H3 binding activity verified by BLI

Loaded Monoclonal Anti-Human B7-H3 / B7-H3 (4Ig) Antibody, Human IgG1 on Protein A Biosensor, can bind Human B7-H3 Protein, His Tag (Cat. No. B73-H52E2) with an affinity constant of 479 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

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ROR1 binding activity verified by BLI

Loaded Biotinylated Human / Cynomolgus / Rhesus macaque ROR1, His,Avitag (Cat. No. RO1-H82E6) on SA Biosensor, can bind Zilovertamab with an affinity constant of 0.252 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

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Resources

Webinar playback and appointment

‘ADC Potency Analysis and Quality Control Technology Breakthrough’ Webinar Series

ACROBiosystems proudly presents the flagship 'ADC Potency Analysisand Quality Control Technology Breakthrough' live webinar series. This series will systematicallydeconstruct critical aspects ofADC drug development through five coremodules-from potency analysis to quality control technologiesempowering breakthroughs in ADC therapeutics by overcoming keytechnical bottlenecks.

Building the Perfect Antibody-based Therapeutic from Selection to Engineering and Manufacturing

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Addressing Challenges in Antibody-Drug Conjugate Development

Here is the brief recap of the webinar:ADCs have the potential to enable 'precision medicine' with a wide market reach.Challenges in ADCs include managing Target Affinity, enhancing payload conjugation, and assessing Payload Delivery in vivo Pharmacokinetics. We can provide high-quality solutions to address these challenges.

Addressing Challenges in Antibody-Drug Conjugate Development

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Building the Perfect Antibody-based Therapeutic from Selection to Engineering and Manufacturing

In this webinar, discover how advanced techniques such as Al-driven candidate selection optimization of antibody sequences, and precise conjugation methods come together to address some of the current challenges in antibody-based therapeutics.

Building the Perfect Antibody-based Therapeutic from Selection to Engineering and Manufacturing

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Brochure Download

ADC Development
AGLink site-specific onjugation kit
Tools for ADC PK Analysis
Bispecific Antibody Drug Development
Antibody Drug Development

Poster/Application Note Download

Advanced Endocytosis Assays Sensitive Detection and Parameter Optimization for HER2CD20 Antibody Internalization
Development and validation of bioanalytical assays for the quantification of ADC

References

  • [1] Damelin Marc, Zhong Wenyan, Myers Jeremy, et al. Evolving Strategies for Target Selection for Antibody-Drug Conjugates.[J]. Pharmaceutical research, 2015, 32(11):3494-507. DOI: 10.1007/s11095-015-1624-3.
  • [2] Ritchie Michael, Tchistiakova Lioudmila, Scott Nathan, et al. Implications of receptor-mediated endocytosis and intracellular trafficking dynamics in the development of antibody drug conjugates.[J]. mAbs, 2013, 5(1):13-21. DOI: 10.4161/mabs.22854.
  • [3] Donaghy Heather, . Effects of antibody, drug and linker on the preclinical and clinical toxicities of antibody-drug conjugates.[J]. mAbs, 2016, 8(4):659-71. DOI: 10.1080/19420862.2016.1156829.
  • ADC Target Proteins
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