Did you know that you can buy products from over 140 different suppliers from us?

Tsp23 antibody

Details for Product No. ABIN863111
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Antigen
Reactivity
Human
(1), (1)
Host
Mouse
(1)
Clonality (Clone)
Monoclonal ()
Application
Western Blotting (WB)
(1)
Pubmed 8 references available
Quantity 100 µg
Options
Shipping to United States (Change)
Availability Will be delivered in 3 to 4 Business Days
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Catalog No. ABIN863111
344.30 $
Plus shipping costs $45.00

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen Recombinant tsp23
Clone Tsp232A
Isotype IgG1 kappa
Specificity Detects approx. 19 kDa. Detects Tsp23, no cross-reactivity to p23.
Cross-Reactivity (Details) 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 Synonyms:
Transcript similar p23
p23 is a highly conserved ubiquitous protein, known to have an important function as a cochaperone for the hsp90 chaperoning system. Studies have revealed that p23 is a small protein (18 to 25 kDa) with a simple structure. p23 is a phosphor-protein, which is highly acidic and has an aspartic acid-rich c-terminal domain. Numerous studies have found p23 to be associated with other client proteins like Fes tyrosine kinase, the heme regulated kinase HRI, hsf1 transcription factor, aryl hydrocarbon receptor, telomerase, and Hepadnavirus reverse transcriptase. In spite of several years of study, the exact functional significance of p23 is still not clear. p23 is thought to be involved in the adenosine triphosphate–mediated hsp90 binding of client proteins. 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. 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 % AA identity with p23 and Sba1p respectively.
Gene ID 80755
NCBI Accession NP_001136126.1
UniProt B9A003
Research Area Heat Shock Proteins
Restrictions For Research Use only
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
anti-Tsp23 antibody Tsp23 HS Hela 20ug 1 in 1000 Western Blotting.
Background publications 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).

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).

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).

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).

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).

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).

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).

Felts, Toft: "p23, a simple protein with complex activities." in: Cell stress & chaperones, Vol. 8, Issue 2, pp. 108-13, 2003 (PubMed).

Validation Images
back to top