Key features and details
- Rabbit polyclonal to Prostaglandin D Synthase (Lipocalin)/PDS
- Suitable for: WB, ELISA, IHC-P
- Reacts with: Human
- Isotype: IgG
Product nameAnti-Prostaglandin D Synthase (Lipocalin)/PDS antibody
See all Prostaglandin D Synthase (Lipocalin)/PDS primary antibodies
DescriptionRabbit polyclonal to Prostaglandin D Synthase (Lipocalin)/PDS
Tested applicationsSuitable for: WB, ELISA, IHC-Pmore details
Species reactivityReacts with: Human
Predicted to work with: Mouse
Recombinant fragment corresponding to Human Prostaglandin D Synthase (Lipocalin)/PDS.
Database link: P41222
- Human gastric cancer tissue.
This product was previously labelled as Prostaglandin D Synthase (Lipocalin)
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferpH: 7.30
Preservative: 0.05% Sodium azide
Constituents: 50% Glycerol, 49% PBS
PBS without Mg2+ and Ca2+
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab182784 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/200 - 1/1000. Predicted molecular weight: 21 kDa.|
|ELISA||1/1000 - 1/5000.|
|IHC-P||1/15 - 1/100.|
FunctionCatalyzes 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.
Tissue specificityAbundant in the brain and CNS, where it is expressed in tissues of the blood-brain barrier and secreted into the cerebro-spinal fluid. Abundantly expressed in the heart. In the male reproductive system, it is expressed in the testis, epididymis and prostate, and is secreted into the seminal fluid. Expressed in the eye and secreted into the aqueous humor. Lower levels detected in various tissue fluids such as serum, normal urine, ascitic fluid and tear fluid. Also found in a number of other organs including ovary, fimbriae of the fallopian tubes, kidney, leukocytes.
Sequence similaritiesBelongs to the calycin superfamily. Lipocalin family.
Developmental stageExpression in the amniotic fluid increases dramatically during weeks 12 to 25 of pregnancy. Levels decrease slowly after 25 weeks.
DomainForms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
modificationsBoth N-glycosylation recognition sites are almost quantitatively occupied by N-glycans of the biantennary complex type, with a considerable proportion of structures bearing a bisecting GlcNAc. Agalacto structure as well as sialylated and nonsialylated oligosaccharides bearing alpha2-3- and/or alpha2-6-linked NeuNAc are present.
Cellular localizationRough 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.
- Information by UniProt
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ab182784 has not yet been referenced specifically in any publications.