CRY1 antibodies have been pivotal in uncovering the protein’s dual roles in circadian biology and oncogenesis:
Circadian Regulation: CRY1 antibodies confirmed its interaction with CLOCK/BMAL1 heterodimers, essential for feedback repression in circadian oscillations .
Cancer Mechanisms:
Prostate Cancer: CRY1 overexpression correlates with androgen receptor (AR)-mediated DNA repair and poor clinical outcomes. Antibodies identified CRY1 stabilization post-genotoxic stress, enhancing homologous recombination (HR) repair .
Cervical Cancer: CRY1 overexpression linked to chemoresistance and poor survival. CRY1 knockdown via siRNA reduced NANOG expression and activated p53 signaling .
Breast Cancer: CRY1 antibodies revealed its role in suppressing YAP/TAZ oncogenic activity and modulating Hippo pathway kinases .
CRY1 antibodies undergo rigorous validation:
Western Blot: Detects CRY1 at ~60–66 kDa in human and mouse tissues .
Immunocytochemistry: Nuclear localization confirmed in fibroblasts and cancer cell lines .
Functional Assays: CRY1 ablation reduced HR repair efficiency by 3.9-fold in U2OS-DR-GFP reporter cells .
Prognostic Marker: CRY1 overexpression in metastatic prostate cancer associates with advanced stage and resistance to genotoxic therapies .
Therapeutic Target: CRY1 stabilizers (e.g., KL001) enhance DNA damage-induced cell cycle arrest, while inhibitors sensitize tumors to radiation .
This antibody targets Cryptochrome 1 (CRY1), a photoreceptor protein crucial for mediating various blue light responses in plants. CRY1's functions encompass inhibition of hypocotyl elongation, photoperiodic control of flowering, and regulation of diverse light-dependent processes. These include circadian rhythms, tropic growth, stomatal opening, guard cell development, root development, responses to biotic and abiotic stresses, cell cycles, programmed cell death, apical dominance, fruit and ovule development, seed dormancy, and even magnetoreception.
Upon photoexcitation by blue light, CRY1 undergoes a conformational change and interacts with signaling partners to modulate gene expression at both transcriptional and post-translational levels, thereby controlling associated metabolic and developmental pathways. CRY1's blue light absorption involves a flavin photoreduction process facilitated by an electron transport chain or alternative pathways utilizing metabolites like NADPH, NADH, and ATP. The activated signaling state exhibits a half-life of approximately 5 minutes. CRY1 also plays a role in sensing blue/green light ratios, enabling adaptation to varying light conditions (e.g., shade). In darkness, flavin reoxidation returns CRY1 to its inactive state.
CRY1 directly interacts with bHLH transcription factors (PIF4 and PIF5) under low blue light (LBL) conditions, stimulating their activity and influencing gene expression to adjust physiological responses such as hypocotyl elongation and hyponastic growth. High-intensity blue light activates CRY1's capacity for converting molecular oxygen to reactive oxygen species (ROS) and hydrogen peroxide, potentially leading to cell death. CRY1 is essential for blue light-triggered and singlet oxygen-mediated programmed cell death (PCD).
CRY1 is involved in inducing the expression of photoprotective genes under extreme light conditions, mediating blue light-induced gene expression and hypocotyl elongation via modulation of transcription factor degradation and anion channel activation. It plays a critical role in hypocotyl hook formation, stomatal opening, and the regulation of various growth parameters, possibly through auxin and abscisic acid (ABA) signaling. CRY1 further influences lateral root growth and shade avoidance syndrome (SAS), working in conjunction with phototropins to regulate phototropism, and affecting shoot regeneration in vitro. It modulates anthocyanin and chlorophyll accumulation in a PHY-dependent manner, contributes extensively to blue light deetiolation responses, and exhibits characteristics suggestive of a role in magnetoreception. CRY1 also participates in strigolactone signaling, temperature-dependent growth regulation, and disease resistance mechanisms, including systemic acquired resistance (SAR).
The following studies provide further insights into CRY1 function: