ITA6186
ITA6186
ITA6186
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$526.00
Price in reward points: 526
- Catalog: ITA6186
- Gene/Protein: HSP90AA1
- Product Description: Immunotag™ HSP90AA1 Antibody
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Description
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Specifications
Antibody Specification Datasheet 
IMPORTANT NOTE This product is custom manufactured with a lead time of 3-4 weeks. Once in production, this item cannot be cancelled from an order and is not eligible for return. Target Protein HSP90AA1 Clonality Polyclonal Storage/Stability -20°C/1 year Application WB,IHC,IF/ICC,ELISA Recommended Dilution WB 1:500-1:2000 IHC 1:50-1:200, IF/ICC 1:100-1:500 Concentration 1 mg/ml Reactive Species Human,Mouse,Rat Host Species Rabbit Immunogen N term -peptideof human HSP90AA1 Specificity HSP90AA1 Antibody detects endogenous levels of total HSP90AA1 Purification The antiserum was purified by peptide affinity chromatography. Form Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt Gene Name HSP90AA1 Accession No. P07900 Alternate Names EL52; epididymis luminal secretory protein 52; Heat shock 86 kDa; heat shock 90kD protein 1, alpha; Heat shock 90kD protein 1, alpha like 4; heat shock 90kD protein, alpha-like 4; Heat shock 90kDa protein 1 alpha; Heat shock protein 90kDa alpha (cytosolic) class A member 1; Heat shock protein HSP 90-alpha; HS90A_HUMAN; HSP 86; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90AA1; HSP90ALPHA; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP 2; LAP2; lipopolysaccharide-associated protein 2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38; Description 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). Cell Pathway/ Category Primary Polyclonal Antibody Protein MW 90kDa Usage For Research Use Only! Not for diagnostic or therapeutic procedures. - Reviews
| Antibody Specification | |
| Datasheet |
|
| IMPORTANT NOTE | This product is custom manufactured with a lead time of 3-4 weeks. Once in production, this item cannot be cancelled from an order and is not eligible for return. |
| Target Protein | HSP90AA1 |
| Clonality | Polyclonal |
| Storage/Stability | -20°C/1 year |
| Application | WB,IHC,IF/ICC,ELISA |
| Recommended Dilution | WB 1:500-1:2000 IHC 1:50-1:200, IF/ICC 1:100-1:500 |
| Concentration | 1 mg/ml |
| Reactive Species | Human,Mouse,Rat |
| Host Species | Rabbit |
| Immunogen | N term -peptideof human HSP90AA1 |
| Specificity | HSP90AA1 Antibody detects endogenous levels of total HSP90AA1 |
| Purification | The antiserum was purified by peptide affinity chromatography. |
| Form | Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt |
| Gene Name | HSP90AA1 |
| Accession No. | P07900 |
| Alternate Names | EL52; epididymis luminal secretory protein 52; Heat shock 86 kDa; heat shock 90kD protein 1, alpha; Heat shock 90kD protein 1, alpha like 4; heat shock 90kD protein, alpha-like 4; Heat shock 90kDa protein 1 alpha; Heat shock protein 90kDa alpha (cytosolic) class A member 1; Heat shock protein HSP 90-alpha; HS90A_HUMAN; HSP 86; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90AA1; HSP90ALPHA; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP 2; LAP2; lipopolysaccharide-associated protein 2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38; |
| Description | 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). |
| Cell Pathway/ Category | Primary Polyclonal Antibody |
| Protein MW | 90kDa |
| Usage | For Research Use Only! Not for diagnostic or therapeutic procedures. |