抗EGLN1/PHD2抗体 | Anti-EGLN1/PHD2 Antibody

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Image

	Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-2219] - Analysis of EGLN1/PHD2 in ARPE-19 cells using anti-PHD2 antibody. Image from veriifed customer review.
	Immunohistochemistry-Paraffin: EGLN1/PHD2 Antibody [NB100-2219] - IHC analysis of a formalin fixed and paraffin embedded mouse lung section using 1:200 dilution of EGLN1/PHD2 antibody. The staining was developed using HRP conjugated anti-rabbit secondary antibody and DAB reagent. This PHD2 antibody generated a specific staining in the cytoplasm and nuclei of alveolar as well as bronchiolar epithelial cells. Cytoplasmic staining was observed in almost all cells while the nuclear positivity was seen in a subset of cells only.
	Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-2219] - EGLN1/PHD2 antibody (1:500) was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).
	Western Blot: EGLN1/PHD2 Antibody [NB100-2219] - Detection of EGLN1/PHD2 in mouse kidney lysate using NB 100-2219. ECL exposure, 20 seconds.
	Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-2219] - Staining of renal tubular epithelium in mouse using NB100-2219 at 2.5ug/ml. Mouse kidney cortex, 40X.

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Background

HIF prolyl 4-hydroxylases (PHDs) are proyl hydroxylase domain-containing enzymes (PHD1/ Egln2, PHD2/ Egln1, PHD3/ Egln3, and P4H-TM) that mediate important physiological responses to hypoxia by modulating HIF1alpha levels. The HIF-alpha is regulated by hydroxylation, both by a family of PHDs leading to ubiquitination and proteasomal degradation, and by transcriptional inactivation following asparaginyl hydroxylation by FIH (factor inhibiting HIF). Under normoxic conditions, HIF Prolyl Hydroxylase 2 (HIF1-PH; also called PHD1 or Egln2) catalyzes the post-translational formation of 4-hydroxyproline through hydroxylation of a specific proline found in each of NODD/CODD domains of HIF1A and also hydroxylates HIF2A with preference for CODD site of HIF1A/HIF1B. After hydroxylation, HIFs undergo proteasomal degradation via VHL (von Hippel-Lindau) ubiquitination complex. However, under hypoxic conditions, the hydroxylation reaction is tempered which allows HIFs to escape degradation process followed by their nuclear translocation, heterodimerization with HIF1B, and increased expression of hypoxia-inducible genes. HIF1-PH, through regulating HIF1 stability, is involved in various hypoxia-influenced processes such as angiogenesis in retinal/cardiac functionality as well as tumor angiogenesis, and defecticve EGLN1 have been linked to ECYT3 (familial erythrocytosis type 3).

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