Lunaxafusp Biosimilar - Research Grade

Human

ERBB2

>1mg/ml

scFv - heavy - kappa

CHO Cells

Trastuzumab Biosimilar - Research Grade (ICH4013), Ado-Trastuzumab Emtansine Biosimilar - Research Grade (ICH4014), Pertuzumab Biosimilar - Research Grade (ICH4030), Margetuximab Biosimilar - Research Grade (ICH5057), Anbenitamab Biosimilar - Research Grade (ICH5344), Calotatug Biosimilar - Research Grade (ICH5421), Coprelotamab Biosimilar - Research Grade (ICH5448), Disitamab Biosimilar - Research Grade (ICH5482), Gancotamab Biosimilar - Research Grade (ICH5562), Timigutuzumab Biosimilar - Research Grade (ICH5925), Zanidatamab Biosimilar - Research Grade (ICH6002)

https://www.imgt.org/mAb-DB/

ICH3002

P04626

Blue ice

This is an unconjugated, non-therapeutic recombinant research-grade analog of Lunaxafusp, an ERBB2 (HER2)-directed biologic, supplied for research use only and not for human or veterinary use. It is built around the same HER2-binding specificity as the originator and is expressed in an scFv-based format (single-chain variable fragment with heavy and kappa-derived variable domains). Note that the "-fusp" stem in the originator's name indicates a fusion-protein construct, so this analog reproduces the HER2-targeting binding module rather than a conventional full-length IgG; researchers should confirm the exact molecular format needed for their assays. Because it is offered as a research reagent, it is well suited to in-vitro binding characterization, use as a positive/targeting control alongside other anti-HER2 tools, epitope and receptor-engagement studies, and antibody- or ADC-development workflows. It is available with low-endotoxin grades (<1 EU/mg research grade; <0.5 EU/mg ultra-low) and in bulk milligram-to-gram quantities to support preclinical and assay-development programs requiring consistent, defined material. ERBB2 (HER2, gene ERBB2; UniProt P04626) is a member of the human epidermal growth factor receptor (EGFR/HER) family of single-pass transmembrane receptor tyrosine kinases. Unlike other family members, HER2 has no known high-affinity soluble ligand; it functions as the preferred heterodimerization partner for HER1 (EGFR), HER3, and HER4. Ligand binding to a partner receptor drives dimerization with HER2, transphosphorylation of intracellular tyrosine residues, and activation of downstream RAS-MAPK and PI3K-AKT signaling that promotes proliferation, survival, and migration. HER2 is amplified or overexpressed in a subset of breast, gastric, and other carcinomas, where high receptor density enables constitutive signaling. Its extracellular domain comprises four subdomains, with domain IV and domain II serving as key epitopes for therapeutic and research antibodies. This central role in growth-factor signaling makes HER2 a widely studied oncology target.

Metastatic lymph node gene 19 protein, MLN 19, Proto-oncogene Neu, Proto-oncogene c-ErbB-2, Tyrosine kinase-type cell surface receptor HER2, p185erbB2, Receptor tyrosine-protein kinase erbB-2, HER2, NEU, NGL

This monoclonal antibody was purified using Protein A

Sterile, preservative-free, solution in PBS. BSA and Azide free.

This biosimilar is stable when stored at 2-8°C. For longer term storage (> 3 months) it is recommended to store this antibody at -20°C or -70°C.

Functional Assays

This biosimilar is for research use only (RUO): it is not for diagnostic or therapeutic procedures and cannot be purchased by patients.

Products are for research use only. Not for use in diagnostic or therapeutic procedures.

3-4 weeks

Q: Is the Lunaxafusp biosimilar available in bulk mg to gram quantities?

A: Yes — it is manufactured in scalable milligram to gram quantities for high-throughput and bulk in vivo experiments.

Q: Is this research-grade Lunaxafusp biosimilar suitable for in vivo use?

A: Yes, it is a low-endotoxin, in vivo-ready formulation intended for preclinical and in vivo research use only (RUO).

Q: What does the Lunaxafusp biosimilar target?

A: It is an unconjugated, non-therapeutic analog of Lunaxafusp that binds ERBB2; for research use only.