PCBP1 antibodies are immunological reagents designed to detect and analyze PCBP1, a protein that binds single-stranded nucleic acids with a preference for polycytosine (poly-C) sequences. These antibodies enable researchers to study PCBP1's roles in:
Iron chaperoning (delivering iron to ferritin and prolyl hydroxylases) .
RNA stability and splicing (e.g., regulating CDKN1A and CD81 mRNA levels) .
Antiviral signaling (suppressing MAVS-mediated immune responses) .
Cancer progression (acting as a tumor suppressor in hepatocellular carcinoma and lung cancer) .
Commercial PCBP1 antibodies vary in clonality, host species, and applications:
Detects PCBP1 at ~37–40 kDa in human cell lines (HeLa, HEK-293, K-562) .
Validated in studies analyzing PCBP1 knockdown effects on CDKN1A and CD81 mRNA stability .
Used to study PCBP1 interactions with viral proteins (e.g., poliovirus 3CD) and RNA substrates .
Critical for identifying PCBP1’s role in MAVS degradation during antiviral responses .
Localizes PCBP1 in tumor tissues, revealing reduced expression in hepatocellular carcinoma (HCC) compared to normal liver .
Tumor Suppression: PCBP1 loss correlates with poor prognosis in HCC and lung cancer .
Iron Dysregulation: PCBP1 depletion disrupts iron homeostasis, promoting ferroptosis in bladder cancer .
Intracellular Checkpoint: PCBP1 maintains effector T cell functions by blocking FoxP3+ regulatory T cell differentiation .
Antiviral Activity: Suppresses MAVS-mediated interferon responses, enhancing viral replication .
Binds heavily oxidized RNA (≥2 adjacent 8-oxoG residues), triggering apoptosis via caspase-3 activation and PARP-1 cleavage .
KH domains (KH1 and KH3) are critical for RNA binding and apoptosis induction .
Anti-human PCBP1 mAb, clone PAT2A10AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PCBP1 protein 1-163 amino acids purified from E. coli.
Poly (rC) Binding Protein 1 (PCBP1) is a multifunctional protein that plays a crucial role in various cellular processes. It is known for its ability to bind to polycytosine (poly (rC)) sequences in RNA and DNA, influencing gene expression, RNA stability, and translation. This article delves into the background, functions, and significance of PCBP1, particularly focusing on its role in human and mouse models.
PCBP1 was first cloned from a human lymphocyte cDNA library in 1994 . It has a relative molecular weight of 38 kDa and is characterized by its ability to bind to RNA and DNA. The protein contains three KH (K-homology) domains, which are responsible for its nucleic acid-binding properties. These domains enable PCBP1 to interact with various RNA and DNA sequences, thereby regulating multiple cellular processes.
One of the critical functions of PCBP1 is its role as a cytosolic iron chaperone. It binds and transfers iron to recipient proteins in mammalian cells, ensuring proper iron distribution and utilization . In the liver, PCBP1 is essential for maintaining iron homeostasis. Mice lacking PCBP1 in hepatocytes exhibit defects in liver iron regulation, leading to conditions such as hepatic steatosis, inflammation, and degeneration .
PCBP1 has been identified as a tumor suppressor in various cancer types. It is often downregulated in cancers, and its reduced expression is associated with tumorigenesis, development, and metastasis . PCBP1 regulates gene transcription, alternative splicing, and translation of many cancer-related genes. Its role in the hypoxic microenvironment, autophagy, apoptosis, and chemotherapy of cancer cells is also being extensively studied .
Research on PCBP1 continues to uncover its multifaceted roles in cellular processes and disease mechanisms. Studies have shown that PCBP1 is involved in immune responses and may play a role in protecting cells from oxidative stress and ferroptosis . The protein’s ability to regulate iron homeostasis and its tumor-suppressive properties make it a potential target for therapeutic interventions in diseases such as cancer and iron-related disorders.