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- Antigen structure
- References [5]
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- Western blot [1]
- Immunohistochemistry [1]
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- Product number
- ABIN2484840 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Transcript Similar p23 antibody (Atto 488)
- Antibody type
- Monoclonal
- Description
- Protein G Purified
- Reactivity
- Human, Mouse
- Host
- Mouse
- Conjugate
- Green dye
- Isotype
- IgG
- Antibody clone number
- Tsp232A
- Vial size
- 100 μg
- Storage
- -20°C
Submitted references In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins.
Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone.
An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function.
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.
Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.
Hu J, Toft D, Anselmo D, Wang X
Journal of virology 2002 Jan;76(1):269-79
Journal of virology 2002 Jan;76(1):269-79
Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone.
Weaver AJ, Sullivan WP, Felts SJ, Owen BA, Toft DO
The Journal of biological chemistry 2000 Jul 28;275(30):23045-52
The Journal of biological chemistry 2000 Jul 28;275(30):23045-52
An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function.
Weikl T, Abelmann K, Buchner J
Journal of molecular biology 1999 Oct 29;293(3):685-91
Journal of molecular biology 1999 Oct 29;293(3):685-91
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.
Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF
Cell stress & chaperones 1996 Dec;1(4):237-50
Cell stress & chaperones 1996 Dec;1(4):237-50
Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.
Johnson JL, Beito TG, Krco CJ, Toft DO
Molecular and cellular biology 1994 Mar;14(3):1956-63
Molecular and cellular biology 1994 Mar;14(3):1956-63
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Supportive validation
- Submitted by
- antibodies-online (provider)
- Main image
- Experimental details
- IHC
