You are viewing an incomplete version of our website. Please click to reload the website as full version.

Tsp23 antibody

Details for Product No. ABIN863111, Supplier: Log in to see
Human, Mouse (Murine)
Clonality (Clone)
Monoclonal ()
Antibody Array (AA), Immunohistochemistry (IHC), Western Blotting (WB)
Log in to see
Supplier Product No.
Log in to see

Get this product for free

It's quick and easy to submit your validation proposal. I want to validate this product

Learn more

Available images

Immunogen Recombinant tsp23
Clone Tsp232A
Isotype IgG1 kappa
Specificity Detects ~19 kDa. Detects Tsp23, no cross-reactivity to p23.
Sensitivity 1 µg/mL of SMC-194 was sufficient for detection of tsp23 in 20 µg of transiently transfected Hela cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
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 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. Specifically TSP23 (transcript similar p23) displays 44 % and 17 % amino acid identity with p23 and Sba1p respectively (10).
Gene ID 80755
NCBI Accession NP_001136126
UniProt B9A003
Application Notes
  • WB (1:1000)
  • IHC (1:1000)
  • optimal dilutions for assays should be determined by the user.

1 μg/ml of SMC-194 was sufficient for detection of tsp23 in 20 μg of transiently transfected Hela cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 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 -20 °C
Supplier Images
Western Blotting (WB) image for anti-Tsp23 antibody (ABIN863111) Tsp23 HS Hela 20ug 1 in 1000 Western Blotting.
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, Wang: "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, Owen, Toft: "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, Tesmer, Dy, Ouellette, Trager, Morin, Toft, Shay, Wright, White: "Functional requirement of p23 and Hsp90 in telomerase complexes." in: Genes & development, Vol. 13, Issue 7, pp. 817-26, 1999 (PubMed).

Nair, Toran, Rimerman, Hjermstad, Smithgall, Smith: "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, Toft: "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).