• Species Reactivity

  Human

• Specificity

  Detects human EGLN3/PHD3 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human (rh) EGLN1/PHD2 or rhEGLN2/PHD1 is observed.

• Source

  Monoclonal Mouse IgG    _2B Clone # 700210

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  E. coli-derived recombinant human EGLN3/PHD3    
  Pro2-Asp239    
  Accession # Q9H6Z9

• Formulation

  Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 μm filtered solution in PBS.

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Immunocytochemistry

  8-25 μg/mL

  See below

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Preparation and Storage

• Reconstitution

  Sterile PBS to a final concentration of 0.5 mg/mL.

• Shipping

  The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

• Stability & Storage

  Use a manual defrost freezer and avoid repeated freeze-thaw cycles.    

• 12 months from date of receipt, -20 to -70 °C as supplied.

• 1 month, 2 to 8 °C under sterile conditions after reconstitution.

• 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: EGLN3/PHD3

Egl nine homolog 3 (EGLN3), also known as PHD3, is a widely expressed 27 kDa enzyme that hydroxylates proline residues on target proteins including HIF-1 alpha. HIF-1 is an alpha / beta heterodimeric transcriptional activator that upregulates genes involved in mitigating the effects of hypoxia. Normally, and in the presence of abundant oxygen, the HIF-1 alpha -chain is hydroxylated by PHD family members, which results in its ubiquitylation and degradation. Under low oxygen tension, EGLN3 activity is decreased, the HIF-1 alpha subunit is retained, and HIF-1 activates genes. EGLN3 also hydroxylates and promotes the degradation of the beta -2-adrenergic receptor, promotes myogenic differentiation, promotes apoptosis via caspase activation, and blocks tumor angiogenesis. EGLN3 forms homomultimers and heteromultimers with other EGLN proteins, and this is enhanced during hypoxia. EGLN3 contains one iron 2-oxoglutarate (Fe2OG) dioxygenase domain (aa 278-376), an iron-binding site (Asp 137 and His196), and a 2-oxoglutarate-binding site (Arg205). Within aa 2-239, human EGLN3 shares 97% aa sequence identity with mouse and rat EGLN3.

• Long Name:

  Egl Nine Homolog 3/Prolyl Hydroxylase Domain-containing Protein 3

• Entrez Gene IDs:

  112399 (Human); 112407 (Mouse); 54702 (Rat)

• Alternate Names:

  EC 1.14.11; EC 1.14.11.-; EGL nine (C.elegans) homolog 3; egl nine homolog 3 (C. elegans); egl nine homolog 3; egl nine-like protein 3 isoform; EGLN3; FLJ21620; HIF prolyl hydroxylase 3; HIFPH3 MGC125998; HIFPH3; HIF-PH3; HIF-prolyl hydroxylase 3; HPH-1; HPH-3; Hypoxia-inducible factor prolyl hydroxylase 3; MGC125999; pdh3; PHD3; Prolyl hydroxylase domain-containing protein 3