Rabbit Polyclonal PHD2 / prolyl hydroxylase antibody. C-terminal. Suitable for WB, ICC/IF, IHC-Fr and reacts with Human, Rat, Mouse samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human EGLN1.
pH: 7
Preservative: 0.025% Proclin 300
Constituents: 79% PBS, 20% Glycerol (glycerin, glycerine)
WB | ICC/IF | IHC-Fr | |
---|---|---|---|
Human | Tested | Tested | Expected |
Mouse | Expected | Expected | Tested |
Rat | Expected | Tested | Expected |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/500.00000 - 1/3000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Rat, Mouse | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Rat | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
Species Human | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human, Rat | Dilution info Use at an assay dependent concentration. | Notes - |
Select an associated product type
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. 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, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.
C1orf12, PNAS-118, PNAS-137, EGLN1, Egl nine homolog 1, Hypoxia-inducible factor prolyl hydroxylase 2, Prolyl hydroxylase domain-containing protein 2, SM-20, HIF-PH2, HIF-prolyl hydroxylase 2, HPH-2, PHD2
Rabbit Polyclonal PHD2 / prolyl hydroxylase antibody. C-terminal. Suitable for WB, ICC/IF, IHC-Fr and reacts with Human, Rat, Mouse samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human EGLN1.
pH: 7
Preservative: 0.025% Proclin 300
Constituents: 79% PBS, 20% Glycerol (glycerin, glycerine)
The protein PHD2 also known as prolyl hydroxylase 3 EGLN1 or 366G is a member of the prolyl hydroxylase family with a molecular mass of approximately 46 kDa. PHD2 is expressed in a variety of tissues particularly those in the human body's oxygen-sensing cellular machinery. This protein functions mechanically by adding hydroxyl groups to proline residues on its target proteins an enzymatic activity essential for its role in cellular oxygen sensing.
This hydroxylation process influences the stability of hypoxia-inducible factor (HIF) by marking it for degradation under normal oxygen levels. PHD2 is a monomeric enzyme but its hydroxylase activity does not require association with other proteins to function. By regulating HIF PHD2 plays a critical role in cellular responses to oxygen availability controlling genes involved in processes such as angiogenesis metabolism and cell survival.
PHD2 participates in the HIF signaling pathway and oxygen homeostasis pathways. The regulation of HIF by PHD2 occurs alongside PHD1 and PHD3 which have similar hydroxylase activities. Importantly PHD2 protects cells from hypoxia-related stress by ensuring the degradation of HIF-α subunits under normoxic conditions thereby maintaining cellular homeostasis and proper metabolic function.
PHD2 has connections with conditions such as cancer and chronic kidney disease. Its role in cancer is linked to its regulation of HIF where dysregulation can lead to abnormal cell growth and angiogenesis. In chronic kidney disease the insights into PHD2's function offer potential therapeutic targets particularly since HIF stabilization can ameliorate anemia frequently associated with this condition. Interactions between PHD2 and other proteins in these disease pathways make it a significant focal point for research aimed at developing new treatments.
We have tested this species and application combination and it works. It is covered by our product promise.
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
U-87 MG cells stained for PHD2 (green) using ab226890 at 1/500 dilution in ICC/IF.
IV9 rat E18 primary cortical neuron cells stained for PHD2 (green) using ab226890 at 1/500 dilution in ICC/IF.
Frozen-sectioned adult mouse cerebellum tissue stained for PHD2 / prolyl hydroxylase using ab226890 at 1/250 dilution in immunohistochemical analysis.
Red: NF-H, stained by NF-H antibody diluted at 1/500.
Blue: DAPI.
10% SDS-PAGE gel.
All lanes: Western blot - Anti-PHD2 / prolyl hydroxylase antibody - C-terminal (ab226890) at 1/2000 dilution
Lane 1: Untreated HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell extract at 30 µg
Lane 2: HeLa (human epithelial cell line from cervix adenocarcinoma) treated with 200 µM cobalt (II) chloride for 24 hours whole cell extract at 30 µg
Predicted band size: 46 kDa
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com