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Anti-HSP90 (2D11B9) Antibody (OAED00192)
Datasheets/Manuals | Printable datasheet for Anti-HSP90 (2D11B9) Antibody (OAED00192) (OAED00192) |
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Predicted Species Reactivity | Dog|Drosophila|Fish|Guinea Pig|Hamster|Horse|Human|Monkey|Mouse|Porcine|Rat|Sheep |
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Product Format | Liquid. PBS containing 50% glycerol and 0.09% sodium azide |
Clonality | Monoclonal |
Clone | 2D11B9 |
Isotype | IgG1 |
Host | Mouse |
Application | Western blot |
Reconstitution and Storage | Store at -20°C. Avoid freeze/thaw cycles. |
Immunogen | Recombinant human Hsp90 |
Purification | Protein G affinity purified |
Concentration | 1 mg/ml |
Application Info | WB: (1 μg/ml, colorimetric) Detects a band of ~92kDa by Western blot. Optimal dilutions should be determined by the end user. |
Description |
Gene Symbol | HSP90AA1|HSP90AB1 |
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Gene Full Name | heat shock protein 90 alpha family class A member 1|heat shock protein 90 alpha family class B member 1 |
Alias Symbols | D6S182;EL52;epididymis luminal secretory protein 52;epididymis secretory sperm binding protein Li 65p;heat shock 84 kDa;heat shock 86 kDa;heat shock 90kD protein 1, alpha;heat shock 90kD protein 1, alpha-like 4;heat shock 90kD protein 1, beta;heat shock 90kD protein, alpha-like 4;heat shock 90kDa protein 1, alpha;heat shock protein 90 kDa;heat shock protein 90kDa alpha (cytosolic), class A member 1;heat shock protein 90kDa alpha (cytosolic), class B member 1;heat shock protein 90kDa alpha family class A member 1;heat shock protein 90kDa alpha family class B member 1;heat shock protein HSP 90-alpha;heat shock protein HSP 90-beta;HEL-S-65p;HSP 86;Hsp103;HSP84;HSP86;Hsp89;HSP89A;Hsp90;HSP90A;HSP90B;HSP90-beta;HSP90N;HSPC1;HSPC2;HSPCA;HSPCAL1;HSPCAL4;HSPCB;HSPN;LAP2;LAP-2;lipopolysaccharide-associated protein 2;LPS-associated protein 2;renal carcinoma antigen NY-REN-38. |
NCBI Gene Id | 3320|3326 |
Protein Name | Heat shock protein HSP 90-alpha|Heat shock protein HSP 90-beta |
Description of Target | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385).|Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). |
Uniprot ID | P07900|P08238 |
Molecular Weight | 90 kDa |
- Protocol:
- Reconstitution & Storage Instructions
- Western Blotting/Immunoblotting (WB/IB) Protocol
- Immunohistochemistry (IHC) Protocol
- Immunocytochemistry (ICC) Protocol
- Enzyme-Linked ImmunoSorbent Assay (ELISA) Protocol
- Blocking Peptide Competition Protocol (BPCP)
- Immunoprecipitation (IP) Protocol
- Antibody Array (AA) Protocol
- Tips Information:
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See our General FAQ page.
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What is the species homology for "Anti-HSP90 (2D11B9) Antibody (OAED00192)"?
The tested species reactivity for this item is "". This antibody is predicted to have homology to "Dog|Drosophila|Fish|Guinea Pig|Hamster|Horse|Human|Monkey|Mouse|Porcine|Rat|Sheep".
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How long will it take to receive "Anti-HSP90 (2D11B9) Antibody (OAED00192)"?
This item is available "Domestic: within 1-2 week delivery | International: 1-2 week".
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What buffer format is "Anti-HSP90 (2D11B9) Antibody (OAED00192)" provided in?
This item is provided in "Liquid. PBS containing 50% glycerol and 0.09% sodium azide".
Additional format options may be available. For more information please contact info@avivasysbio.com. -
What are other names for "Anti-HSP90 (2D11B9) Antibody (OAED00192)"?
This target may also be called "D6S182;EL52;epididymis luminal secretory protein 52;epididymis secretory sperm binding protein Li 65p;heat shock 84 kDa;heat shock 86 kDa;heat shock 90kD protein 1, alpha;heat shock 90kD protein 1, alpha-like 4;heat shock 90kD protein 1, beta;heat shock 90kD protein, alpha-like 4;heat shock 90kDa protein 1, alpha;heat shock protein 90 kDa;heat shock protein 90kDa alpha (cytosolic), class A member 1;heat shock protein 90kDa alpha (cytosolic), class B member 1;heat shock protein 90kDa alpha family class A member 1;heat shock protein 90kDa alpha family class B member 1;heat shock protein HSP 90-alpha;heat shock protein HSP 90-beta;HEL-S-65p;HSP 86;Hsp103;HSP84;HSP86;Hsp89;HSP89A;Hsp90;HSP90A;HSP90B;HSP90-beta;HSP90N;HSPC1;HSPC2;HSPCA;HSPCAL1;HSPCAL4;HSPCB;HSPN;LAP2;LAP-2;lipopolysaccharide-associated protein 2;LPS-associated protein 2;renal carcinoma antigen NY-REN-38." in publications.
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What is the shipping cost for "Anti-HSP90 (2D11B9) Antibody (OAED00192)"?
The shipping cost for this item is $40 within the US. Please contact us for specific shipping prices for international orders.
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What is the guarantee for "Anti-HSP90 (2D11B9) Antibody (OAED00192)"?
All Aviva products have been through rigorous validations and carry 100% satisfaction guarantee.
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Can I get bulk pricing for "Anti-HSP90 (2D11B9) Antibody (OAED00192)"?
You can get bulk pricing for this item by going here.
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What is the molecular weight of the protein?
The molecular weight reported by Uniprot for this item is "90 kDa".
Please note observed molecular weights in western blot applications may differ depending on a variety of protein characteristics. -
What protocols are available for "Anti-HSP90 (2D11B9) Antibody (OAED00192)"?
We may have detailed protocol data avaialble for this item. To learn more, please view the "Protocols & Data" tab on the product page.
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What are positive controls for "HSP90AA1|HSP90AB1"?
We have listed RNA Seq and gene expression data in the "Target Info" tab. You may be able to find adequate positive controls there.
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What are negative controls for "HSP90AA1|HSP90AB1"?
We have listed RNA Seq and gene expression data in the "Target Info" tab. You may be able to find adequate positive controls there.
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What other proteins interact with "HSP90AA1|HSP90AB1"?
This protein has been reported to interact with "Protein Interactions". Please view the "Related Categories" tab on the product page for more information.
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What biological processes are associated with "HSP90AA1|HSP90AB1"?
This protein has been associated with "Biological Processes". Please view the "Related Categories" tab on the product page for more information.
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What cellular components are associated with "HSP90AA1|HSP90AB1"?
This protein has been associated with "Cellular Components". Please view the "Related Categories" tab on the product page for more information.
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What protein functions are associated with "HSP90AA1|HSP90AB1"?
This protein has been associated with "Protein Functions". Please view the "Related Categories" tab on the product page for more information.