TAP1 Antibodies

Background

The TAP1 (Antigen Processing Associated transporter 1) gene encodes a transporter located on the endoplasmic reticulum membrane. Its main function is to transport the antigen peptides produced by the degradation of intracellular proteasomes to the endoplasmic reticulum lumen and bind them to major histocompatibility complex (MHC) Class I molecules, thereby initiating the recognition and clearance of pathogens and abnormal cells in the immune response. This gene was identified in the early 1990s and is a key component of the antigen presentation pathway. The research on its structure and function has greatly promoted people's understanding of adaptive immune mechanisms, autoimmune diseases and infection immunity. The variation or dysfunction of the TAP1 gene is closely related to various immune deficiency diseases and autoimmune disorders, and has become an important molecular target in immunology and clinical medical research.

Structure Function Application Advantage Our Products

Structure of TAP1

TAP1 (Antigen treatment-associated transport protein 1) is a key membrane transport protein with a molecular weight of approximately 80 kDa. Its weight varies among different species, mainly determined by its specific amino acid sequence.

Species	Human	Mouse	Rat	Bovine
Molecular Weight (kDa)	About 80	About 78	About 79	About 81
Primary Structural Differences	Members of the ABC transporter superfamily, including transmembrane domains and nucleotide binding domains	Sequence is highly conserved, the function is similar to human	Core structure highly homologous	Species-specific amino acid variation was found

This protein is composed of approximately 808 amino acid residues, and its primary structure contains multiple hydrophobic transmembrane α -helices, which jointly form peptide binding and transport channels. Its core functional domain includes an ATP-binding cassette (ABC) domain facing the cytoplasmic side, which hydrolyzes ATP to provide energy for the active transmembrane transport of antigenic peptides. The secondary structure of proteins is dominated by these transmembrane α -helices, which assemble into specific three-dimensional conformations within the membrane to form functional peptide transport complexes.

Fig. 1 TAP1's Role in Innate Antiviral Defense.¹

Key structural properties of TAP1:

Pore structure formed by multiple transmembrane α-helices
Peptide-binding pockets formed by hydrophobic transmembrane regions
Cytoplasmic side ATP combination box (ABC) structure domain transfer power

Functions of TAP1

The TAP1 gene encodes antigen peptide transporter 1, whose core function is to mediate the transport of endogenous antigen peptides from the cytoplasm to the endoplasmic reticulum, which is a key initiating step in the MHC Class I molecule antigen presentation pathway.

Function	Description
Antigenic peptide transport	Form a heterodimer with TAP2, and use the energy generated by hydrolysis of ATP to actively transport the antigenic peptide generated by proteasome degradation in the cytoplasm to the endoplasmic reticulum cavity.
Immune recognition activation	The transported antigenic peptides are assembled with MHC class I molecules in the endoplasmic reticulum and eventually presented to the cell surface for recognition by CD8⁺ T cells, initiating cellular immune responses.
Maintenance of immune homeostasis	By continuously presenting autoantigen peptides, it participates in the establishment of central and peripheral tolerance and prevents autoimmune responses.
Anti-infection defense	When a virus infects or cells become cancerous, it is responsible for presenting the corresponding abnormal antigen peptides, thereby activating cytotoxic T cells and eliminating diseased cells.
Immune editing effect	Its expression level or functional status can affect the antigen presentation efficiency of tumor cells and is an important link in immune editing and tumor immune escape.

The transport process of TAP1 is substrate selective and ATP-dependent, which is different from the oxygenation balance mechanism of myoglobin. Its functional efficiency directly affects the body's immune surveillance ability against intracellular pathogens and cancer cells.

Applications of TAP1 and TAP1 Antibody in Literature

Attaran, Nima, et al. "Downregulation of TAP1 in tumor-free tongue contralateral to squamous cell carcinoma of the oral tongue, an indicator of better survival." International journal of molecular sciences 21.17 (2020): 6220. https://doi.org/10.3390/ijms21176220

Research has found that a lower expression of TAP1 mRNA in the contralateral tumor-free tongue tissue of patients with oral tongue squamous cell carcinoma (SCCOT) is significantly associated with better overall survival and disease-free survival, providing a new direction for early diagnosis and prognosis assessment.

Tabassum, Anika, et al. "Transporter associated with antigen processing 1 (TAP1) expression and prognostic analysis in breast, lung, liver, and ovarian cancer." Journal of Molecular Medicine 99.9 (2021): 1293-1309. https://doi.org/10.1007/s00109-021-02088-w

This study, through bioinformatics analysis, found that the expression, mutation and methylation patterns of the TAP1 gene in different cancers were significantly different, and its expression level was closely related to the prognosis of patients, providing a new basis for understanding the role of TAP1 in tumor progression and chemotherapy resistance.

Laplana Lafaja, Marina, et al. "Resilience effects of SGK1 and TAP1 DNA markers during PRRSV outbreaks in reproductive sows." International journal of molecular sciences (2020) 10(5), 902. https://doi.org/10.3390/ani10050902

Research has found that specific variations in the SGK1 and TAP1 genes can affect the reproductive performance of sows during an outbreak of porcine reproductive and respiratory syndrome virus (PRRSV). Sows carrying specific genotypes can maintain stable litter sizes and piglet survival rates during the epidemic, providing potential molecular markers for breeding and selection.

Zhou, Xiao‐Tian, et al. "Hedgehog signalling mediates drug resistance through targeting TAP1 in hepatocellular carcinoma." Journal of Cellular and Molecular Medicine 24.7 (2020): 4298-4311. https://doi.org/10.1111/jcmm.15090

Research has found that the key transcription factor GLI1/2 of the Hedgehog signaling pathway directly regulates the expression of TAP1 and mediates multidrug resistance in liver cancer. Inhibiting this pathway or TAP1 can significantly enhance the sensitivity to chemotherapy drugs such as sorafenib, providing a new target for the treatment of refractory liver cancer.

Li, Boya, et al. "Antigen peptide transporter 1 (TAP1) promotes resistance to MEK inhibitors in pancreatic cancers." International Journal of Molecular Sciences 23.13 (2022): 7168. https://doi.org/10.3390/ijms23137168

Research has found that antigen peptide transporter 1 (TAP1) leads to drug resistance in pancreatic cancer by promoting the efflux of MEK inhibitors. Inhibiting TAP1 can significantly enhance the sensitivity of tumors to MEK inhibitors, providing a new strategy for combined therapy.

Creative Biolabs: TAP1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality TAP1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom TAP1 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 TAP1 antibodies, custom preparations, or technical support, contact us at email.

Reference

Zhao, Jin, et al. "Broadly antiviral activities of TAP1 through activating the TBK1-IRF3-mediated type I interferon production." International Journal of Molecular Sciences 22.9 (2021): 4668. https://doi.org/10.3390/ijms22094668