Prostaglandin D Synthase (Lipocalin)/PDS peptide (ab188544)
Key features and details
- Suitable for: Blocking
Description
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Product name
Prostaglandin D Synthase (Lipocalin)/PDS peptide
See all Prostaglandin D Synthase (Lipocalin)/PDS proteins and peptides -
Accession
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Animal free
No -
Nature
Synthetic -
Associated products
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Corresponding Antibody
Specifications
Our Abpromise guarantee covers the use of ab188544 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Blocking - Blocking peptide for Anti-Prostaglandin D Synthase (Lipocalin)/PDS antibody [EP12357] (ab182141)
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Form
Liquid -
Additional notes
- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions.
- If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
- Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
- Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
- Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.This product was previously labelled as Prostaglandin D Synthase (Lipocalin)
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at -20°C.
General Info
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Alternative names
- Beta trace protein
- Beta-trace protein
- Cerebrin 28
see all -
Function
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. -
Tissue specificity
Abundant 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 similarities
Belongs to the calycin superfamily. Lipocalin family. -
Developmental stage
Expression in the amniotic fluid increases dramatically during weeks 12 to 25 of pregnancy. Levels decrease slowly after 25 weeks. -
Domain
Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. -
Post-translational
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 localization
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. - Information by UniProt
Images
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Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab188544 has not yet been referenced specifically in any publications.