Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system.
Subcellular Location:
Rough endoplasmic reticulum
Nucleus membrane
Golgi apparatus
Cytoplasm
perinuclear region
Secreted
Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted.
Monoclonal Antibody for Human Prostaglandin-H2 D-isomerase
Monoclonal Antibody for Human Prostaglandin-H2 D-isomerase
Monoclonal Antibody for Human Prostaglandin-H2 D-isomerase
Monoclonal Antibody for Human Prostaglandin-H2 D-isomerase
Monoclonal Antibody for Human Prostaglandin-H2 D-isomerase
Monoclonal Antibody for Human Prostaglandin-H2 D-isomerase
Protein for Human Prostaglandin-H2 D-isomerase
Protein for Human Prostaglandin-H2 D-isomerase
Protein for Human Prostaglandin-H2 D-isomerase
Protein for Human Prostaglandin-H2 D-isomerase
Protein for Human Prostaglandin-H2 D-isomerase
Protein for Human Prostaglandin-H2 D-isomerase
R&D Technical Data
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s
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s
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Precision
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Intra-assay Precision (Precision within an assay):Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.
Intra-Assay CV: ≤5.4%
Inter-assay Precision (Precision between assays):Three samples of known concentration were tested in five separate assays to assess inter-assay precision.
Inter-Assay CV: ≤11.3%
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Intra-assay Precision (Precision within an assay):Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.
Intra-Assay CV: ≤3.9%
Inter-assay Precision (Precision between assays):Three samples of known concentration were tested in five separate assays to assess inter-assay precision.
Inter-Assay CV: ≤7.7%
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Recovery
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Recovery was determined by spiking various levels of PTGDS into serum and plasma .
Sample Type
Average(%)
Recovery Range(%)
Serum
98
92-102
Plasma
99
96-104
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Recovery was determined by spiking various levels of ACE into serum and plasma .
Sample Type
Average(%)
Recovery Range(%)
Serum
99
91-103
Plasma
98
93-106
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Linearity
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The linearity of the kit was assayed by testing samples spiked with appropriate concentration of PTGDS and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.
Sample
1:2
1:4
1:8
1:16
serum(n=5)
92-105%
92-103%
92-104%
94-102%
EDTA plasma(n=5)
91-106%
93-105%
96-101%
95-100%
heparin plasma(n=5)
94-101%
91-104%
95-102%
93-105%
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The linearity of the kit was assayed by testing samples spiked with appropriate concentration of ACE and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.
Sample
1:2
1:4
1:8
1:16
serum(n=5)
92-105%
90-101%
95-105%
92-109%
EDTA plasma(n=5)
89-95%
93105%
89-94%
90-106%
heparin plasma(n=5)
93-104%
94-110%
101-111%
91-110%
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: SEQUENCE REVISION TO 12; 16; 19; 36; 56; 73; 77; 99; 100; 127 AND 176
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PROTEIN SEQUENCE OF 23-190;GLYCOSYLATION AT ASN-51 AND ASN-78
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PROTEIN SEQUENCE OF 23-37; 67-77; 117-126 AND 169-178;TISSUE SPECIFICITY;GLYCOSYLATION
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PROTEIN SEQUENCE OF 23-38;FUNCTION;TISSUE SPECIFICITY
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PROTEIN SEQUENCE OF 23-35;TISSUE SPECIFICITY;USE AS A MARKER FOR BRAIN TUMOR
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PROTEIN SEQUENCE OF 30-44;DEVELOPMENTAL STAGE;EXPRESSION IN ABNORMAL PREGNANCIES
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PROTEIN SEQUENCE OF 58-73 AND 123-140;TISSUE SPECIFICITY
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: SUBCELLULAR LOCATION;TISSUE SPECIFICITY;USE AS A MARKER FOR MENINGIOMA
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: TISSUE SPECIFICITY;USE AS A MARKER FOR RENAL INJURY IN HYPERTENSION
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Cited for: USE AS A MARKER FOR RENAL INJURY IN DIABETES MELLITUS
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51 AND ASN-78;STRUCTURE OF CARBOHYDRATES
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: GLYCOSYLATION AT ASN-78;STRUCTURE OF CARBOHYDRATES;IDENTIFICATION BY MASS SPECTROMETRY
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: GLYCOSYLATION AT SER-29;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 29-190 OF MUTANT ALA-65 IN COMPLEXES WITH FATTY ACIDS;FUNCTION;CATALYTIC ACTIVITY;SUBUNIT;MUTAGENESIS OF LYS-59; MET-64; CYS-65; LEU-79; PHE-83; LEU-131 AND TYR-149;DOMAIN
36.
"Crystal structure of the human lipocalin-type prostaglandin D synthase crystallised with the substrate analog 9,11-dideoxy-9alpha,11alpha- epoxymethanoprostaglandin f2alpha." Structural genomics consortium (SGC)
Submitted (2010-01) to the PDB data bank
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Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-190 IN COMPLEX WITH SUBSTRATE ANALOG