Anti-PHD2/EGLN1 Polyclonal Antibody for IF/ICC, ELISA - Q9GZT9

Core Product Specifications and Parameters

Biological Background: PHD2/EGLN1 Function and Localization

• PHD2/EGLN1 is a cellular oxygen sensor that functions as a prolyl hydroxylase, catalyzing the hydroxylation of hypoxia-inducible factor (HIF) alpha subunits under normoxic conditions.
• It specifically hydroxylates proline residues within the oxygen-dependent degradation (ODD) domains of HIF1A and HIF2A, marking them for proteasomal degradation via the von Hippel-Lindau (VHL) ubiquitination complex.
• Under hypoxia, PHD2 activity is reduced, allowing HIF-alpha subunits to stabilize, translocate to the nucleus, and activate transcription of genes involved in angiogenesis, erythropoiesis, and metabolic adaptation.
• PHD2 is the primary HIF prolyl hydroxylase under normoxia and plays critical roles in retinal and cardiac angiogenesis, as well as other hypoxia-influenced processes.
• The protein belongs to the EGLN family (EGLN1-3) and contains a prolyl hydroxylase domain along with zinc-finger motifs, contributing to its catalytic and regulatory functions.
• It undergoes post-translational modifications including acetylation, phosphorylation, and S-nitrosylation, which may modulate its activity and stability.
• Subcellularly, PHD2 localizes to both the cytoplasm and the nucleus, enabling it to sense oxygen levels and interact with HIF substrates in multiple compartments.
• Widely expressed with highest levels in adult heart, brain, lung, and liver, as well as fetal brain, heart, spleen, and skeletal muscle, consistent with its role in systemic oxygen homeostasis.

Experimental Guidance and Technical Tips

• The immunogen consists of a recombinant fusion protein spanning amino acids 1–426 of human PHD2/EGLN1 (full-length). This design may enable recognition of both native and denatured conformations.
• For IF/ICC, consider using appropriate fixation and permeabilization protocols, as PHD2 is present in both cytoplasmic and nuclear compartments. Validate signal specificity using appropriate controls (e.g., siRNA knockdown or PHD2-deficient cell lines).
• For ELISA, test a range of antibody dilutions and confirm linearity with recombinant PHD2 protein or cell lysates. Due to the oxygen-dependent regulation of PHD2 expression, cell culture conditions (normoxia vs. hypoxia) may affect target abundance.
• If applying this antibody in other applications (e.g., WB, IP), in-house validation is recommended. Cross-reactivity with other EGLN family members (EGLN2, EGLN3) should be assessed based on sequence homology.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio offers comprehensive IVD raw-material solutions, supporting diagnostic developers from early R&D to commercialization. This anti-PHD2/EGLN1 polyclonal antibody complements our catalog of oxygen-sensing and hypoxia-related reagents. We provide validated antibody pairs, bulk polyclonal and recombinant antibodies, and customized sourcing for rare targets, ensuring your project has reliable access to critical research tools.