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MABC1612

Sigma-Aldrich

Anti-phospho-PHD2 (Ser 125) Antibody, clone 4

Synonym(s):

Egl nine homolog 1, EC:1.14.11.29, Hypoxia-inducible factor prolyl hydroxylase 2, HIF-PH2, HIF-prolyl hydroxylase 2, HPH-2, Prolyl hydroxylase domain-containing protein 2, SM-20

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Pricing and availability is not currently available.

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

species reactivity

human

packaging

antibody small pack of 25 μg

isotype

IgG2aκ

UniProt accession no.

shipped in

ambient

target post-translational modification

phosphorylation (pSer125)

Gene Information

human ... EGLN1(54583)

General description

Egl nine homolog 1 (UniProt: Q9GZT9; also known as EC:1.14.11.29, Hypoxia-inducible factor prolyl hydroxylase 2, HIF-PH2, HIF-prolyl hydroxylase 2, HPH-2, Prolyl hydroxylase domain-containing protein 2, PHD2, SM-20) is encoded by the EGLN1 (also known as C1orf12, PNAS-118, PNAS-137) gene (GeneID: 54583) in human. PHD2 acts as a cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. It is widely expressed with highest levels in skeletal muscle and heart, moderate levels in pancreas, brain and kidney, and lower levels in lung and liver. PHD2 is mainly cytoplasmic, but it shuttles between the nucleus and cytoplasm. It hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1alpha and is also reported to hydroxylate HIF2alpha. PHD2 is reported to be phosphorylated on serine 125 by p70S6K and this phosphorylation increased its ability to degrade HIF1alpha. PHD2 exhibits a preference for the CODD site for both HIF1alpha and HIF1beta. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus and heterodimerization with HIF1beta. It is one of the most important isozyme under normoxia and, through regulating the stability of HIF1, it is involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Defects in EGLN1 gene cause familial type erythrocytosis, an autosomal dominant disorder that is characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels. (Ref.: Di Conza, G., et al. (2017). Cell Rep. 18(7): 1699-1712).

Specificity

Clone 4 detects PHD2 in lysate of HEK293 cells overexpressing PHD2.

Immunogen

A linear peptide corresponding to 11 amino acids surrounding Ser125 phosphorylation site from the N-terminal half of human PHD2.

Application

.
Research Category
Apoptosis & Cancer

Quality

Evaluated by Western Blotting in lysates of HEK293 cells overexpressing PHD2.

Western Blotting Analysis: 1 µg/mL of this antibody detected phospho-PHD2 (Ser 125) in 10 µg of lysate from HEK293 cells overexpressing PHD2.

Physical form

Format: Purified
Protein G purified
Purified mouse monoclonal antibody IgG2a in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Zhuqing Li et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 25(19), 5947-5960 (2019-07-10)
Up to 80% of patients with ovarian cancer develop platinum resistance over time to platinum-based chemotherapy. Increased HIF1α level is an important mechanism governing platinum resistance in platinum-resistant ovarian cancer (PROC). However, the mechanism regulating HIF1α stability in PROC remains

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