Prostaglandin E Synthase 3 (Cytosolic) (PTGES3) antibody

Details for Product No. ABIN263974
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Antigen
Synonyms PTGES3, P23, TEBP, cPGES, 5730442A20Rik, Ptges, Tebp, p23, sid3177, RGD1561913, CPGES
Reactivity
Chicken, Guinea Pig, Human, Mouse (Murine), Rabbit, Yeast (Saccharomyces cerevisiae)
(80), (20), (18), (15), (12), (12), (12), (2), (2), (1), (1), (1), (1)
Host
Mouse
(48), (32)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(4), (4), (3), (3), (3), (3), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Enzyme Immunoassay (EIA), Immunoprecipitation (IP), Immunohistochemistry (Frozen Paraffin-embedded Sections) (IHC (frpe)), Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
(71), (39), (23), (14), (10), (8), (4), (2), (2), (2)
Pubmed 8 references available
Quantity 0.1 mg
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Catalog No. ABIN263974
324.50 $
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Immunogen Recombinant Human full length p23 protein
Clone JJ6
Isotype IgG1
Specificity This antibody detects ~23 kDa p23.
Characteristics Synonyms: Prostaglandin E synthase 3, cPGES, P23, Cytosolic prostaglandin E2 synthase,Telomerase-binding protein p23, Hsp90 co-chaperone, Progesterone receptor complex p23
Purification Protein G Affinity Chromatography
Alternative Name PTGES3 / TEBP
Background P23 is a highly conserved ubiquitous protein, known to have an important function as a cochaperone for the hsp90 chaperoning system (1). Studies have revealed that p23 is a small protein (18 to 25 kDa) with a simple structure (2, 3). p23 does not have any structural homology with any other known proteins (1). p23 was first discovered as a part of the Hsp90-progesterone receptor complex along with hsp70, p54 and p50 (1). p23 is a phosphor-protein, which is highly acidic and has an aspartic acid-rich c-terminal domain (1). Numerous studies have found p23 to be associated with other client proteins like Fes tyrosine kinase (4), the heme regulated kinase HRI (5), hsf1 transcription factor (4), aryl hydrocarbon receptor (4), telomerase (6), and Hepadnavirus reverse transcriptase (7). In spite of several years of study, the exact functional significance of p23 is still not clear (8). p23 is thought to be involved in the adenosine triphosphate-mediated hsp90 binding of client proteins (8). Since many hsp90 client proteins are involved in oncogenic survival signaling, a recent study has concluded p23 to be a promising target in leukemic apoptosis (9). Hsp90 and its co-chaperone p23 are certainly among the emerging anti-tumor targets in oncology.Synonyms: Cytosolic prostaglandin E2 synthase, Hsp90 co-chaperone, P23, Progesterone receptor complex p23, Prostaglandin E synthase 3, Telomerase-binding protein p23, cPGES
Gene ID 10728
UniProt Q15185
Application Notes Western blot (1: 2000). Immunprecipitation. ELISA.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Concentration 1.0 mg/mL
Buffer PBS in 50 % Glycerol, 0.09 % Sodium Azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Store the antibody at 2 - 8 °C up to one month or (in aliquots) at -20 °C for longer. Avoidrepeated freezing and thawing.
Shelf life: one year from despatch.
Expiry Date 12 months
Supplier Images
anti-Prostaglandin E Synthase 3 (Cytosolic) (PTGES3) antibody anti-Prostaglandin E Synthase 3 (Cytosolic) (PTGES3) antibody
Background publications Felts, Toft: "p23, a simple protein with complex activities." in: Cell stress & chaperones, Vol. 8, Issue 2, pp. 108-13, 2003 (PubMed).

Hu, Toft, Anselmo et al.: "In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins." in: Journal of virology, Vol. 76, Issue 1, pp. 269-79, 2001 (PubMed).

Weaver, Sullivan, Felts et al.: "Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone." in: The Journal of biological chemistry, Vol. 275, Issue 30, pp. 23045-52, 2000 (PubMed).

Weikl, Abelmann, Buchner: "An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function." in: Journal of molecular biology, Vol. 293, Issue 3, pp. 685-91, 1999 (PubMed).

Holt, Aisner, Baur et al.: "Functional requirement of p23 and Hsp90 in telomerase complexes." in: Genes & development, Vol. 13, Issue 7, pp. 817-26, 1999 (PubMed).

Nair, Toran, Rimerman et al.: "A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor." in: Cell stress & chaperones, Vol. 1, Issue 4, pp. 237-50, 1997 (PubMed).

Pingoud, Jeltsch: "Recognition and cleavage of DNA by type-II restriction endonucleases." in: European journal of biochemistry / FEBS, Vol. 246, Issue 1, pp. 1-22, 1997 (PubMed).

Johnson, Beito, Krco et al.: "Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes." in: Molecular and cellular biology, Vol. 14, Issue 3, pp. 1956-63, 1994 (PubMed).

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