ADAM10 Antibodies

Background

ADAM10 is a widely expressed transmembrane metalloproteinase, mainly existing on the surface of animal cell membranes. This enzyme participates in cell signal transduction and cell adhesion regulation by cleaving multiple transmembrane protein substrates, and plays a key role in physiological processes such as embryonic development, immune response and neural plasticity. Because it can cleave amyloid precursor proteins to produce β -amyloid peptides in the pathology of Alzheimer's disease, this enzyme has become an important target in the research of neurodegenerative diseases. Since its identification in 1990, the three-dimensional structural analysis of ADAM10 has revealed the mechanism of the synergistic interaction between its proteolytic domain and regulatory precursor domain. Related research has greatly advanced our understanding of protein splicing regulation, intercellular communication, and the molecular mechanisms of diseases.

Structure Function Application Advantage Our Products

Structure of ADAM10

ADAM10 is a transmembrane metalloproteinase with a molecular weight of approximately 84 kDa. There are slight differences in its molecular weight among different species, mainly due to the varying degrees of glycosylation modification of the extracellular domain.

Species	Human	Mouse	Rat	Zebrafish
Molecular Weight (kDa)	~84	~83	~84	~82
Primary Structural Differences	Contains signal peptide precursor, integrin, catalytic domain, solution domains and so on	The catalytic core is highly conserved	The sequence similarity of extracellular domains is high	Possess the mammalian ADAM10 homeodomain

The ADAM10 protein is composed of 748 amino acids, and its extracellular region contains a zinc ion-dependent catalytic domain responsible for the cleavage of substrate proteins. Its active center is composed of a conserved HEXXHXXGXXHD motif, in which three histidine and one glutamic acid jointly chelate zinc ions, which is the core of its protease function. There is also a "proximal membrane region" (MPD) near the cell membrane, which is crucial for regulating the activity of enzymes and substrate specificity. Its structure ensures its precise recognition and cleavage of numerous substrates on the cell membrane, including Notch receptors and amyloid precursor proteins.

Fig. 1 ADAM10 synthesis and maturation in the cell.¹

Key structural properties of ADAM10:

Multi-domain transmembrane proteins
Zinc ion-dependent catalytic center
Substrate identification and regulation module

Functions of ADAM10

The core function of the ADAM10 gene is to act as a "molecular scissors" for proteolytic cleavage, but it is also widely involved in a variety of important physiological and pathological processes.

Function	Description
Transmembrane protein shedding	The extracellular domain that cuts and releases over 100 membrane proteins, such as Notch receptors, cell adhesion molecules and cytokine precursors, is a key regulator of intercellular communication.
Notch signaling pathway activation	By cutting the Notch receptor and releasing its intracellular domain into the nucleus, the transcription of downstream genes is activated, which is crucial for embryonic development and cell fate determination.
Regulation of synaptic plasticity	Neuroadhesion molecules (such as N-cadherin) are cleaved in the hippocampus and other brain regions, which regulate the formation, maintenance and function of synapses and affect learning and memory.
Amyloid protein production	As an α -secretase, it cleases amyloid precursor protein (APP) to generate the soluble fragment sAPPα, thereby preventing the formation of β-amyloid peptide (Aβ). This non-amyloid pathway has neuroprotective effects.
Migration of immune cells	By cutting and shedding chemokines and adhesion molecules, it regulates the adhesion of white blood cells at the inflammatory site and their transendothelial migration.

Unlike the single specificity of many enzyme substrate relationships, ADAM10 achieves spatiotemporal specific cleavage of vast substrate libraries through its domain combination, cellular localization, and interactions with regulatory proteins (such as the TspanC8 family of four-transmembrane proteins). This precise regulation enables it to execute distinct biological instructions at different tissues and developmental stages, and its functional imbalance is directly related to various diseases such as Alzheimer's disease, cancer, and inflammation.

Applications of ADAM10 and ADAM10 Antibody in Literature

1. Shahid, Shifa, et al. "ADAM10: Possible functions in enamel development." Frontiers in Physiology 13 (2022): 1032383. https://doi.org/10.3389/fphys.2022.1032383

The article indicates that ADAM10 is a membrane-bound metalloproteinase that is expressed at a specific stage of ameloblasts during tooth development and is regulated by tetrastransmembrane proteins for substrate specificity. It affects cell movement and connection by cutting various membrane proteins (such as cadherin, COL17A1, etc.) and may play a key role in enamel formation.

2. Wang, Xinyue, et al. "Rescue RM/CS-AKI by blocking strategy with one-dose anti-myoglobin RabMAb." Nature Communications 16.1 (2025): 1044. https://doi.org/10.3389/fimmu.2020.00499

The article indicates that ADAM10 is a zinc-dependent transmembrane protease and has become a target for drug development due to its key role in cancer and autoimmune diseases. Although the preclinical data is positive, inhibitors face challenges in clinical trials. This review will explore its application strategies, combination therapies and potential biomarkers.

3. Liao, Shuanglin, et al. "ADAM10-a "multitasker" in sepsis: focus on its posttranslational target." Inflammation Research 72.3 (2023): 395-423. https://doi.org/10.1007/s00011-022-01673-0

The article indicates that ADAM10 acts as a key "molecular scissors" in sepsis, regulating inflammatory responses and endothelial dysfunction by cutting various membrane protein substrates (such as inflammatory factors and cadherin), and can also serve as a receptor for Staphylococcus aureus α -toxin. Targeting its specific subcellular activity may provide new directions for treatment.

4. Elsworthy, Richard J., et al. "The role of ADAM10 in astrocytes: Implications for Alzheimer's disease." Frontiers in Aging Neuroscience 14 (2022): 1056507. https://doi.org/10.3389/fnagi.2022.1056507

The article indicates that ADAM10 inhibits Aβ production by clewing amyloid precursor proteins and plays a crucial role in Alzheimer's disease. It regulates the function of astrocytes and inflammatory responses, which provides a new perspective for exploring the therapeutic mechanism of AD targeting astrocytes.

5. Alfano, Danielle N., Mark J. Miller, and Juliane Bubeck Wardenburg. "Endothelial ADAM10 utilization defines a molecular pathway of vascular injury in mice with bacterial sepsis." The Journal of Clinical Investigation 133.23 (2023).https://doi.org/10.1172/JCI168450

The article indicates that vascular endothelial ADAM10 is a key pathogenic factor for sepsis caused by Staphylococcus aureus, Pseudomonas aeruginosa and other bacteria, promoting microvascular thrombosis and lethality. Endothelial-specific knockout of ADAM10 can increase survival rates, suggesting that it can serve as a pathogen-specific precision therapeutic target.

Creative Biolabs: ADAM10 Antibodies for Research

Creative Biolabs specializes in the production of high-quality ADAM10 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom ADAM10 Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our ADAM10 antibodies, custom preparations, or technical support, contact us at email.

Reference

Khezri, Mohammad Rafi, Mehdi Mohebalizadeh, and Morteza Ghasemnejad-Berenji. "Therapeutic potential of ADAM10 modulation in Alzheimer's disease: a review of the current evidence." Cell Communication and Signaling 21.1 (2023): 60. https://doi.org/10.1186/s12964-023-01072-w