The PCBP1 antibody is a polyclonal immunoglobulin (IgG) raised in rabbits, designed to specifically target the Poly(rC)-binding protein 1 (PCBP1), a key RNA-binding protein involved in post-transcriptional gene regulation . PCBP1 is characterized by its three KH (K homology) domains, which enable binding to poly(C) motifs in RNA, stabilizing mRNA and regulating translation . The antibody is widely used in molecular biology research to detect PCBP1 in human, mouse, and rat samples via techniques such as Western blotting (WB), immunoprecipitation (IP), and immunohistochemistry (IHC) .
The antibody detects a single band at ~35 kDa in WB, corresponding to PCBP1 . It is commonly used to study PCBP1 expression in cancer immunity, where PCBP1 stabilizes effector T-cell functions by restricting regulatory T-cell differentiation .
Used to isolate PCBP1 from cell lysates, facilitating downstream analysis of its RNA-binding partners or associated proteins (e.g., cGAS in innate immunity) .
Localizes PCBP1 in tissue sections, aiding studies of its subcellular distribution (e.g., nuclear vs. cytoplasmic localization in immune cells) .
PCBP1 was identified as an intracellular immune checkpoint that prevents effector T-cell exhaustion by repressing regulatory T-cell programs . Antibody-based detection confirmed that PCBP1 deletion in T cells enhances tumor growth and reduces antitumor immunity .
The antibody revealed PCBP1’s interaction with cGAS, a key DNA sensor, enhancing its ability to detect cytosolic DNA and activate downstream immune signaling (e.g., IFN-β production) . PCBP1 deficiency impaired cGAS-mediated responses to herpes simplex virus (HSV-1), increasing viral replication .
PCBP1 stabilizes mRNAs with C-rich motifs, such as those encoding α-globin and tyrosine hydroxylase . The antibody has been used to study its role in translational silencing during cell differentiation (e.g., 15-lipoxygenase mRNA) .