Anti-Human HER2 antibody ( Cax

Caxmotabart 是一种靶向 HER2 的 IgG1κ 型人源化抗体，对应的同型对照为：Human IgG1 kappa, Isotype Control。

Caxmotabart is an HER2-targeting IgG1κ type humanized antibody, the recommed isotype control is Human IgG1 kappa, Isotype Control

caxmotabart entudotin
An antibody-drug conjugate (ADC) composed of trastuzumab, a humanized monoclonal antibody targeting the tumor-associated antigen (TAA) epidermal growth factor receptor 2 (EGFR2; HER2; ErbB2), site-specifically conjugated, via a tumor-selective beta-glucuronide linker, to the auristatin analog and potent microtubule inhibitor monomethyl auristatin F (MMAF), with potential antineoplastic activity. Upon administration of caxmotabart entudotin, the trastuzumab moiety targets and binds to HER2 expressed on tumor cells. Upon binding, internalization and linker cleavage, MMAF is released. MMAF binds to and inhibits tubulin polymerization, which results in G2/M phase arrest and tumor cell apoptosis. HER2, a tyrosine kinase receptor, is overexpressed by many cancer cell types.

ADC FS-1502
anti-HER2 ADC FS-1502
antibody-drug conjugate FS-1502
trastuzumab MMAF
trastuzumab monomethyl auristatin F
trastuzumab/MMAF ADC IKS014
trastuzumab/MMAF antibody-drug conjugate IKS014

FS 1502
FS-1502
FS1502
IKS 014
IKS-014
IKS014
LCB 14
LCB-14
LCB14
LCB14-0110

Structure of the HER2 and Neu proteins. The domain structure is shown on the left consisting of two ligand binding regions (LD1 & LD2), two cysteine-rich regions (CR1 & CR2), a short transmembrane domain (TM), a catalytic tyrosine kinase domain (TK), and a carboxy terminal tail (CT). Numerous sites of tyrosine phosphorylation wiithin the TK and CT domains are indicated by circled P.The letters on the right point to specific areas that are altered or mutated in certain naturally occuring or experimentally induced cancers discussed in the text. A) site of somatic mutations found in tumors arising in MMTV-neu mice. B) site of the 48bp deletion in the naturally occuring human ΔHER2 isoform. C) site of the mutation in the neuT oncogene initially discovered in a rat carcinogen induced tumor model and subsequently used in numerous in vitro and transgenic experimental models. D) site of mutations found in rare cases of human lung cancers.

The HER2 receptor has no known ligand that directly binds to it. Instead, HER2 is the preferred partner for forming heterodimers (pairing) with other EGFR family members . HER2 dimerization is a crucial aspect of its signaling mechanism and plays a significant role in the biology of various cancers. The formation of dimers—either homodimers or heterodimers—is a key step in the activation of HER2 signaling pathways . The nature and consequences of HER2 dimerization can vary significantly across different cancer types. In breast cancer, HER2 frequently forms heterodimers with HER3 . The HER2/HER3 heterodimer is highly potent in activating downstream signaling pathways, such as PI3K/AKT and MAPK, promoting cell proliferation and survival. HER2 expression in gastric cancer can be more heterogeneous than in breast cancer, with variable patterns of expression within and between tumors. HER2 in gastric cancer also dimerizes with HER3 and potentially dimerizes with other EGFR family members, contributing to aggressive tumor behavior . HER2 mutations, such as insertions in exon 20, can promote constitutive heterodimerization  and the activation of HER2 without ligand binding in non-small-cell lung cancer (NSCLC) . HER2 can dimerize with EGFR in colorectal cancer, influencing responsiveness to EGFR-targeted therapies such as cetuximab . HER2 is overexpressed in a subset of ovarian cancers, often forming dimers with other EGFR family members .

HER2 can form homodimers or heterodimers with other EGFR family members in a ligand-independent manner. HER2 homodimers are generally less potent in signaling than heterodimers. However, HER2/HER3 heterodimers are particularly potent, activating robust downstream signaling pathways . HER3, with its six binding sites for the p85 subunit of PI3K, plays a critical role in PI3K/AKT pathway activation when dimerized with HER2

Dysregulation of HER2. The expression of HER2 is primarily regulated at the level of gene transcription. Transcription factors and epigenetic modifications can regulate HER2 gene expression by modulating the chromatin structure and accessibility to transcriptional machinery. Endocytosed receptors can undergo lysosomal degradation, leading to the attenuation of HER2-mediated signaling pathways. Figure was made using BioRender.