GLYR1 antibodies are designed to target the GLYR1 protein, which contains PWWP, AT-hook, and NAD-binding domains. These antibodies are used for detecting GLYR1 in various experimental settings, including Western blotting (WB), immunohistochemistry (IHC), and immunofluorescence (IF).
GLYR1 antibodies have been instrumental in elucidating the protein’s role in cancer, chromatin dynamics, and signaling pathways.
Colorectal Cancer: Downregulation of GLYR1 correlates with microsatellite instability (MSI) and poor differentiation. GLYR1 interacts with MLH1, a mismatch repair protein, to regulate its nuclear import. Loss of GLYR1 accelerates G1/S phase transition and reduces sensitivity to 5-fluorouracil (5-FU) via mitochondrial apoptosis inhibition .
Breast Cancer: Overexpression of GLYR1 is linked to tumorigenesis, though its exact mechanism remains under investigation .
GLYR1 binds histone H3K36me3 and facilitates transcriptional activation by destabilizing nucleosomes. It interacts with KDM1B, a histone demethylase, to modify chromatin structure and promote Pol II transcription .
GLYR1 regulates p38 MAPK (MAPK14) signaling under stress conditions, indirectly promoting ATF2 activation via phosphorylation of MAPK14 . Dysregulation of GLYR1 also impacts the PI3K/Akt pathway, affecting p21 expression and cell cycle progression .
GLYR1 antibodies undergo rigorous validation to ensure specificity. For example:
Abcam’s EPR10076B: Demonstrated loss of signal in GLYR1 knockout HEK293T cells, confirming target specificity .
Thermo Fisher’s 14833-1-AP: Validated for IHC and WB in human tissues, with no cross-reactivity reported .
GLYR1 downregulation in microsatellite instability (MSI) colorectal cancer (CRC) is associated with:
Accelerated Proliferation: Increased G1/S phase transition via p21 downregulation .
Reduced 5-FU Sensitivity: Inhibition of mitochondrial apoptosis pathways .
GLYR1’s interaction with EP300 facilitates histone H3K56 acetylation, enhancing transcriptional elongation . This activity is critical for maintaining chromatin accessibility in actively transcribed genes.
Here’s a structured FAQ collection for GLYR1 antibody research, synthesized from peer-reviewed studies and technical resources:
Experimental framework:
Analysis strategy:
Context-dependent signaling: In neurology, anti-GlyR antibodies target extracellular receptor domains (e.g., PERM/SPS ), while in cancer, nuclear GLYR1 modulates chromatin .
Tissue-specific isoforms: Prioritize isoform-specific antibodies (e.g., ab154838 for human studies) .
Pathway crosstalk: Map interactions between GlyRα1 (neurological) and GLYR1-MAPK14 (cancer) using dual RNA-seq/proteomics .
Integrated methods:
Scoring protocol:
Critical controls:
Case study: In autoimmune encephalitis, anti-GlyR antibodies cause synaptic inhibition defects , while nuclear GLYR1 modulates neuroinflammation via KDM1B . Combine CSF antibody testing (ELISA) and neuronal chromatin profiling .
Multiplex design: