Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-2219] - Immunofluorescence of wounded tissue and normal unwounded skin. Representative images for immunofluorescent staining of PHD-2 on healed wounded skin and adjacent ...read more
Genetic Strategies: Knockdown Validated: EGLN1/PHD2 Antibody [NB100-2219] - In vitro analysis of PHD-2 knockout and protein quantification.Western blot data for PHD-2 knockout in fibroblasts of heterozygous Col1 ...read more
Immunohistochemistry-Paraffin: EGLN1/PHD2 Antibody [NB100-2219] - Analysis of a FFPE mouse lung section using 1:200 dilution of EGLN1/PHD2 antibody. The staining was developed using HRP conjugated anti-rabbit secondary ...read more
Western Blot: EGLN1/PHD2 Antibody [NB100-2219] - Detection of EGLN1/PHD2 in mouse kidney lysate. ECL exposure, 20 seconds.
Immunocytochemistry/ Immunofluorescence: EGLN1/PHD2 Antibody [NB100-2219] - EGLN1/PHD2 antibody at 1:500 in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight ...read more
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: EGLN1/PHD2 Antibody [NB100-2219] - Staining of renal tubular epithelium in mouse using NB100-2219 at 2.5 ug/mL.
In Western blot a band is seen ~43 kDa representing HIF Prolyl Hydroxylase 2. There is also a non-specific band of similar intensity at ~75 kDa. Knockout Validation was reported in scientific literature (PMID: 24695462).
43 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
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).
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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PRODUCT AVAILABILITY: Update Regarding the Evolving COVID-19 Situation
Bio-Techne appreciates the critical role that you and our products and services play in research efforts to further scientific innovation and discovery. We are continually assessing our manufacturing and supplier capabilities during the COVID-19 situation and are implementing precautionary measures to ensure uninterrupted supply of products and services. Currently, and as we abide by local shelter in place orders across the world, we are fully operational and do not anticipate any material supply disruptions across our Bio-Techne brands and product lines. As the situation evolves, our goal is to utilize preventive measures to reduce the threat that COVID-19 poses to our ability to meet the needs of our customers globally.