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- Antibody Data
- Antigen structure
- References [8]
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- Validations
- Western blot [3]
- Immunohistochemistry [1]
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- Product number
- ABIN263944 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody
- Antibody type
- Monoclonal
- Antigen
- Recombinant human hsp90 beta.
- Description
- Affinity Chromatography on Protein G
- Reactivity
- Human, Rat, Canine, Chicken/Avian, Rabbit
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- H90-10
- Vial size
- 50 μg
- Concentration
- 1.0 mg/mL
- Storage
- Store the antibody at -20°C. Shelf life: one year from despatch.
Submitted references Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress.
Structure, function, and mechanism of the Hsp90 molecular chaperone.
Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes.
Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome.
The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors.
Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis.
Steroid receptor interactions with heat shock protein and immunophilin chaperones.
Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90.
Arlander SJ, Eapen AK, Vroman BT, McDonald RJ, Toft DO, Karnitz LM
The Journal of biological chemistry 2003 Dec 26;278(52):52572-7
The Journal of biological chemistry 2003 Dec 26;278(52):52572-7
Structure, function, and mechanism of the Hsp90 molecular chaperone.
Pearl LH, Prodromou C
Advances in protein chemistry 2001;59:157-86
Advances in protein chemistry 2001;59:157-86
Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes.
Barent RL, Nair SC, Carr DC, Ruan Y, Rimerman RA, Fulton J, Zhang Y, Smith DF
Molecular endocrinology (Baltimore, Md.) 1998 Mar;12(3):342-54
Molecular endocrinology (Baltimore, Md.) 1998 Mar;12(3):342-54
Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome.
Loo MA, Jensen TJ, Cui L, Hou Y, Chang XB, Riordan JR
The EMBO journal 1998 Dec 1;17(23):6879-87
The EMBO journal 1998 Dec 1;17(23):6879-87
The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors.
Pratt WB
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) 1998 Apr;217(4):420-34
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) 1998 Apr;217(4):420-34
Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis.
Nemoto T, Sato N, Iwanari H, Yamashita H, Takagi T
The Journal of biological chemistry 1997 Oct 17;272(42):26179-87
The Journal of biological chemistry 1997 Oct 17;272(42):26179-87
Steroid receptor interactions with heat shock protein and immunophilin chaperones.
Pratt WB, Toft DO
Endocrine reviews 1997 Jun;18(3):306-60
Endocrine reviews 1997 Jun;18(3):306-60
Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90.
Minami Y, Kawasaki H, Miyata Y, Suzuki K, Yahara I
The Journal of biological chemistry 1991 Jun 5;266(16):10099-103
The Journal of biological chemistry 1991 Jun 5;266(16):10099-103
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- Experimental details
- Image(s): Western Blotting
- Submitted by
- antibodies-online (provider)
- Main image
- Experimental details
- Image(s): Western Blotting
- Submitted by
- antibodies-online (provider)
- Main image
- Experimental details
- Image(s): Western Blotting
Supportive validation
- Submitted by
- antibodies-online (provider)
- Main image
- Experimental details
- Image(s): Immunohistochemistry
