ABIN361664
antibody from antibodies-online
Targeting: HSP90AA1
FLJ31884, Hsp89, Hsp90, HSP90N, HSPC1, HSPCA
Antibody data
- Antibody Data
- Antigen structure
- References [15]
- Comments [0]
- Validations
- Western blot [1]
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- Product number
- ABIN361664 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN361664, RRID:AB_10774750
- Product name
- anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2) antibody
- Antibody type
- Monoclonal
- Description
- Protein G Purified
- Reactivity
- Human, Mouse, Rat
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- 2G5-G3
- Vial size
- 200 μg
- Storage
- -20°C
Submitted references Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells.
17-AAG improves cognitive process and increases heat shock protein response in a model lesion with Aβ25-35.
Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones.
Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.
Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress.
Hsp90 inhibitors as novel cancer chemotherapeutic agents.
Structure, function, and mechanism of the Hsp90 molecular chaperone.
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.
Colipase stabilizes the lid domain of pancreatic triglyceride lipase.
Isoform-specific monoclonal antibodies against HSP90.
Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.
Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90.
Nitric oxide decreases cytosolic free calcium in Balb/c 3T3 fibroblasts by a cyclic GMP-independent mechanism.
Hunter MC, O'Hagan KL, Kenyon A, Dhanani KC, Prinsloo E, Edkins AL
PloS one 2014;9(1):e86842
PloS one 2014;9(1):e86842
17-AAG improves cognitive process and increases heat shock protein response in a model lesion with Aβ25-35.
Ortega L, Calvillo M, Luna F, Pérez-Severiano F, Rubio-Osornio M, Guevara J, Limón ID
Neuropeptides 2014 Aug;48(4):221-32
Neuropeptides 2014 Aug;48(4):221-32
Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones.
Kishimoto J, Fukuma Y, Mizuno A, Nemoto TK
Cell stress & chaperones 2005 Winter;10(4):296-311
Cell stress & chaperones 2005 Winter;10(4):296-311
Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.
Pratt WB, Toft DO
Experimental biology and medicine (Maywood, N.J.) 2003 Feb;228(2):111-33
Experimental biology and medicine (Maywood, N.J.) 2003 Feb;228(2):111-33
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
Hsp90 inhibitors as novel cancer chemotherapeutic agents.
Neckers L
Trends in molecular medicine 2002;8(4 Suppl):S55-61
Trends in molecular medicine 2002;8(4 Suppl):S55-61
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
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
Colipase stabilizes the lid domain of pancreatic triglyceride lipase.
Lowe ME
The Journal of biological chemistry 1997 Jan 3;272(1):9-12
The Journal of biological chemistry 1997 Jan 3;272(1):9-12
Isoform-specific monoclonal antibodies against HSP90.
Nemoto T, Roi R, Matsusaka T, Iwanari H, Yamashita H, Kyakumoto S, Sato N
Biochemistry and molecular biology international 1997 Aug;42(5):881-9
Biochemistry and molecular biology international 1997 Aug;42(5):881-9
Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.
Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM
Proceedings of the National Academy of Sciences of the United States of America 1994 Aug 30;91(18):8324-8
Proceedings of the National Academy of Sciences of the United States of America 1994 Aug 30;91(18):8324-8
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
Nitric oxide decreases cytosolic free calcium in Balb/c 3T3 fibroblasts by a cyclic GMP-independent mechanism.
Garg UC, Hassid A
The Journal of biological chemistry 1991 Jan 5;266(1):9-12
The Journal of biological chemistry 1991 Jan 5;266(1):9-12
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