ATP7A Antibodies

Structure of ATP7A

ATP7A is a transmembrane copper transporter with a molecular weight of approximately 178 kDa. Its size varies slightly among different species, mainly due to minor changes in amino acid sequences and domain compositions.

This protein is composed of approximately 1500 amino acids and includes 8 N-terminal copper-binding domains, 8 transmembrane segments, and an ATP-binding domain and other core functional regions. ATP7A uses the energy generated from ATP hydrolysis to transport copper ions from the cytoplasm to the Golgi apparatus, providing copper for copper-dependent enzymes. When the intracellular copper concentration increases, this protein relocates from the Golgi apparatus to the cell membrane or vesicles, participating in copper excretion. Its molecular structure contains multiple highly conserved motifs, such as phosphorylation domains and nucleotide-binding domains, which together ensure the directional transport of copper ions and the regulation of copper homeostasis in the cell.

Fig. 1 Three-dimensional structure and key positions of ATP7A protein.¹

Key structural characteristics of ATP7A protein:

• Contains 8 N-terminal copper-binding domains, each with a conserved GMXCXXC copper-binding motif
• Has 8 transmembrane segments, forming a copper ion transmembrane transport channel
• Contains a highly conserved P-type ATPase phosphorylation domain (DKTGT sequence)
• The C-terminal nucleotide-binding domain (N-domain) provides the core for ATP hydrolysis catalysis
• The transmembrane region CPC motif is involved in the selective binding and release of copper ions
• The conformational change of the phosphorylated intermediate E1-E2 drives the directional transport of copper

Functions of ATP7A

The core function of ATP7A is to maintain intracellular copper homeostasis by transporting copper ions to the secretion pathway or out of the cell, thereby regulating the activity of various copper-dependent enzymes.

ATP7A has high specificity in copper transport. Its transport activity is precisely regulated by copper concentration and kinase phosphorylation modification to ensure that the intracellular copper level is maintained at the optimal physiological range required.

Applications of ATP7A and ATP7A Antibody in Literature

1. Li, Hao, et al. "Genetic diversity, tissue-specific expression, and functional analysis of the ATP7A gene in sheep." Frontiers in Genetics 14 (2023): 1239979. https://doi.org/10.3389/fgene.2023.1239979

The study revealed that the ATP7A gene is highly expressed in the horns of sheep, and the expression level in large horn individuals is significantly higher than that in small horn individuals. Through genome-wide analysis, multiple SNPs and potential functional sites with significant differences in frequency between the horned and hornless populations were screened out. Among them, three mutations exhibit allele-specific expression.

2. Horn, Nina, and Pernilla Wittung-Stafshede. "ATP7A-regulated enzyme metalation and trafficking in the menkes disease puzzle." Biomedicines 9.4 (2021): 391. https://doi.org/10.3390/biomedicines9040391

The research reveals that copper ions are crucial for maintaining cellular functions, and the transporter protein ATP7A is the core for regulating the copper homeostasis throughout the body. Defects in this gene can lead to Menkes disease. This article reviews how the mechanism of ATP7A-mediated copper enzyme activation explains the diverse symptoms of this disease, and emphasizes that clarifying its mechanism is helpful for early diagnosis.

3. Gao, Wei, et al. "Elesclomol induces copper‐dependent ferroptosis in colorectal cancer cells via degradation of ATP7A." Molecular Oncology 15.12 (2021): 3527-3544. https://doi.org/10.1002/1878-0261.13079

Studies have shown that the copper transporter ATP7A is a key target of the anti-cancer drug Elsclomol. This drug can induce the degradation of ATP7A, and when combined with copper, it leads to the accumulation of copper in mitochondria, triggering oxidative stress and ferroptosis, thereby inhibiting colorectal cancer.

4. Zhou, Yixuan, and Leiliang Zhang. "The interplay between copper metabolism and microbes: in perspective of host copper-dependent ATPases ATP7A/B." Frontiers in cellular and infection microbiology 13 (2023): 1267931. https://doi.org/10.3389/fcimb.2023.1267931

Studies have shown that the copper transporter ATP7A/B maintains the copper homeostasis of the organism through intracellular transport. Certain microorganisms (such as Salmonella and influenza viruses) can interfere with its regulatory mechanism to facilitate their own survival. This article reviews the transport characteristics of ATP7A/B and discusses the interaction between microorganisms and host copper metabolism.

5. Writzl, Karin, et al. "Novel ATP7A Splice-Site Variant Causing Distal Motor Neuropathy and Occipital Horn Syndrome: Two Siblings and Literature Review." Genes 16.9 (2025): 1077. https://doi.org/10.3390/genes16091077

The study identified a novel splicing variant of the ATP7A gene that can cause a rare neurological disorder combined with an overlapping phenotype of occipital bone angle syndrome. The patients initially presented with chronic diarrhea and later developed distal motor neuropathy. This finding expands the mutation spectrum of ATP7A-related diseases.

Creative Biolabs: ATP7A Antibodies for Research

Creative Biolabs specializes in the production of high-quality ATP7A antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom ATP7A 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 ATP7A antibodies, custom preparations, or technical support, contact us at email.