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LearnNBP1-97529
antibody from Novus Biologicals
Targeting: HSP90AA1
FLJ31884, Hsp89, Hsp90, HSP90N, HSPC1, HSPCA
Western blotAntibody data
- Antibody Data
- Antigen structure
- References [8]
- Comments [0]
- Validations [0]
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- Product number
- NBP1-97529 - Provider product page
- Provider
- Novus Biologicals
- Proper citation
- Novus Cat#NBP1-97529, RRID:AB_11188853
- Product name
- Mouse Monoclonal Hsp90A/B Antibody
- Antibody type
- Monoclonal
- Description
- Protein G purified. Recognizes human, mouse and rabbit HSP90 alpha and HSP90 beta.
- Reactivity
- Human, Mouse, Rabbit
- Host
- Mouse
- Isotype
- IgG
- Vial size
- 0.1 mg
- Concentration
- 1.0 mg/ml
- Storage
- Store at -20C. Avoid freeze-thaw cycles.
Submitted references A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells.
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress.
The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR.
The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties.
The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties.
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.
Zhang T, Hamza A, Cao X, Wang B, Yu S, Zhan CG, Sun D
Molecular cancer therapeutics 2008 Jan;7(1):162-70
Molecular cancer therapeutics 2008 Jan;7(1):162-70
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
Chadli A, Graham JD, Abel MG, Jackson TA, Gordon DF, Wood WM, Felts SJ, Horwitz KB, Toft D
Molecular and cellular biology 2006 Mar;26(5):1722-30
Molecular and cellular biology 2006 Mar;26(5):1722-30
Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress.
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
The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR.
Donzé O, Abbas-Terki T, Picard D
The EMBO journal 2001 Jul 16;20(14):3771-80
The EMBO journal 2001 Jul 16;20(14):3771-80
The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties.
Felts SJ, Owen BA, Nguyen P, Trepel J, Donner DB, Toft DO
The Journal of biological chemistry 2000 Feb 4;275(5):3305-12
The Journal of biological chemistry 2000 Feb 4;275(5):3305-12
The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties.
Felts SJ, Owen BA, Nguyen P, Trepel J, Donner DB, Toft DO
The Journal of biological chemistry 2000 Feb 4;275(5):3305-12
The Journal of biological chemistry 2000 Feb 4;275(5):3305-12
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
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