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LearnABIN361711
antibody from antibodies-online
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
- ABIN361711 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN361711, RRID:AB_10772266
- Product name
- anti-Heat Shock Protein 90 (HSP90) antibody
- Antibody type
- Monoclonal
- Antigen
- Heat shock protein 900 from the water mold Achyla ambisexualis
- Description
- Protein G Purified
- Reactivity
- Human, Rat, Chicken/Avian, Rabbit
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- AC-16
- Vial size
- 50 μg
- Concentration
- 1 mg/mL
- Storage
- -20°C
Submitted references 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.
Steroid receptor interactions with heat shock protein and immunophilin chaperones.
Steroid receptor interactions with heat shock protein and immunophilin chaperones.
Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.
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
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
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
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
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