Immunohistochemistry (IHC)
(Immunohistochemistry analysis using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone K41220A. Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative and paraffin-embedded. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Epidermis.)
Mouse Hsp90 alpha/beta Monoclonal Antibody | anti-HSP90AB1 antibody
Hsp90 alpha/beta Antibody: Biotin
Gene Names
HSP90AB1; HSP84; HSPC2; HSPCB; D6S182; HSP90B
Reactivity
Human, Rat, S. cerevisiae, S. pombe. Limited or no reactivity to mice or P.caudatum
Applications
Western Blot, ELISA, Immunohistochemistry
Synonyms
Hsp90 alpha/beta; Monoclonal Antibody; Hsp90 alpha/beta Antibody: Biotin; Hsp86; Hsp89A; Hsp90AA1; Hsp90Alpha; HspC1; HSPCA; HspCAL3; Hsp84; Hsp90B; HspC2; HspCB; D6S182; FLJ26985; anti-HSP90AB1 antibody
Host
Mouse
Reactivity
Human, Rat, S. cerevisiae, S. pombe. Limited or no reactivity to mice or P.caudatum
Clonality
Monoclonal
Isotype
IgG2a
Clone Number
Hyb-K41220A
Form/Format
Protein G Purified
Concentration
1mg/mL (varies by lot)
Sequence Length
724
Applicable Applications for anti-HSP90AB1 antibody
Western Blot (WB), ELISA (EIA), Immunohistochemistry (IHC)
Application Notes
1ug/ml was sufficient for detection of hsp90alphabeta by Western Blot in 20ug of HeLa lysate.
Conjugate
Biotin
Storage Buffer
PBS pH7.2, 50% glycerol, 0.09% sodium azide
Preparation and Storage
-20 degree C
Immunohistochemistry (IHC)
(Immunohistochemistry analysis using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone K41220A. Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative and paraffin-embedded. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Epidermis.)
Immunohistochemistry (IHC)
(Immunohistochemistry analysis using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone K41220A. Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative and paraffin-embedded. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Epidermis.)
Western Blot (WB)
(Western Blot analysis of Human Cell lysates showing detection of Hsp90 alpha protein using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone K41220A. Load: 15 ug. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.)
Western Blot (WB)
(Western Blot analysis of Human Cell lysates showing detection of Hsp90 alpha protein using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone K41220A. Load: 15 ug. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.)
Related Product Information for anti-HSP90AB1 antibody
Background Info: Detects 90kD proteins corresponding to the molecular mass of hsp90 alpha or beta.
Scientific Background: HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer.(2) From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions - including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5 When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function (9).
Scientific Background: HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer.(2) From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions - including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5 When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function (9).
Product Categories/Family for anti-HSP90AB1 antibody
References
1. Nemoto, T. et al. (1997) J.Biol Chem. 272, 26179-26187. 2. Minami, Y, et al. (1991), J.Biol Chem. 266, 10099-10103. 3. Arlander SJH, et al. (2003) J Biol Chem 278, 52572-52577. 4. Pearl H, et al. (2001) Adv Protein Chem 59,157-186. 5. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 6. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 7. Pratt W, Toft D. (1997) Endocr Rev 18,306-360. 8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217, 420-434. 9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91, 8324-8328. 10. Kishimoto J, et al. (2005). Cell Stress and Chaperones. 10 (4), 296-311.
1. Horvat, N. K., et al. (2014). A mutation in the catalytic loop of Hsp90 specifically impairs ATPase stimulation by Aha1p, but not Hch1p. J Mol Biol. pii: S0022-2836(14)00176-4. doi: 10.1016/j.jmb.2014.04.002
1. Horvat, N. K., et al. (2014). A mutation in the catalytic loop of Hsp90 specifically impairs ATPase stimulation by Aha1p, but not Hch1p. J Mol Biol. pii: S0022-2836(14)00176-4. doi: 10.1016/j.jmb.2014.04.002
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
Molecular Weight
83,264 Da
NCBI Official Full Name
heat shock protein HSP 90-beta isoform a
NCBI Official Synonym Full Names
heat shock protein 90kDa alpha (cytosolic), class B member 1
NCBI Official Symbol
HSP90AB1
NCBI Official Synonym Symbols
HSP84; HSPC2; HSPCB; D6S182; HSP90B
NCBI Protein Information
heat shock protein HSP 90-beta; HSP90-beta; heat shock 84 kDa; heat shock 90kD protein 1, beta
UniProt Protein Name
Heat shock protein HSP 90-beta
Protein Family
UniProt Gene Name
HSP90AB1
UniProt Synonym Gene Names
HSP90B; HSPC2; HSPCB; HSP 90; HSP 84; HSP84
UniProt Entry Name
HS90B_HUMAN
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Product Notes
The HSP90AB1 hsp90ab1 (Catalog #AAA803665) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. The Hsp90 alpha/beta Antibody: Biotin reacts with Human, Rat, S. cerevisiae, S. pombe. Limited or no reactivity to mice or P.caudatum and may cross-react with other species as described in the data sheet. AAA Biotech's Hsp90 alpha/beta can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), ELISA (EIA), Immunohistochemistry (IHC). 1ug/ml was sufficient for detection of hsp90alphabeta by Western Blot in 20ug of HeLa lysate. Researchers should empirically determine the suitability of the HSP90AB1 hsp90ab1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "Hsp90 alpha/beta, Monoclonal Antibody" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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