A synthetic peptide made to a C-terminal fragment of the human protein sequence of HIF prolyl hydroxylase 2 (residues 350-426).
Buffer
0.05% sodium azide
Clone Name
Isotype
Species Reactivity
human
Concentration
1 mg/ml
Purification
peptide affinity purified
Guaranteed Application *
WB
Suggested Dilutions
WB (1:1000)
Background
HIF prolyl hydroxylase 2 is a prolyl hydroxylase that modifies HIF-alpha. Classic prolyl hydroxylases are found in the endoplasmic reticulum and modify collagen, whereas HIF is an intracellular protein and the HPH sites do not resemble those modifying collagen. HIF is a transcriptional complex that plays a critical role in oxygen homeostasis. HPH is an essential component of the pathway through which cells sense oxygen. In the presence of oxygen, HPHs convert specific prolyl residues in HIF-alpha to hydroxyproline, leading to HIF-alpha destruction. Low oxygen levels, sensed at the cellular level, cause the HIF conversion to be reduced so that HIF is stable and there is increased angiogenesis. HPH-2, specifically, catalyzes the posttranslational formation of 4-hydroxyproline in HIF alpha proteins. It hydroxylates HIF-1 alpha at Pro(402) and Pro(564), and HIF-2 alpha. It targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitylation complex.
Related Pathway
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HEK293T cells were transfected with the pCMV6-ENTRY control or pCMV6-ENTRY EGLN1 (RC215158) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-EGLN1.
