Anti-HSP90 Alpha antibody
Specifications
| Product Cat#: | AB-06-2286 |
| Product type: | Primary antibody |
| Antigen: | HSP90 Alpha |
| Immunogen: | Recombinant protein |
| Species immunized: | Rabbit |
| Isotype: | IgG |
| Applications: | Immunofluorescence; Western Blot (1:800-1:2000); Immunohistochemistry (1:60-1:200); Immunocytochemistry (1:60-1:200) |
| Reactivity: | Mouse, Rat and Human |
| Clonality (clone number): | Monoclonal （SY14-06） |
| Form: | Liquid |
| Buffer: | Tris-HCl buffer (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide. |
| Concentration: | 1 mg/ml |
| Purity: | Protein A affinity purified |
| Storage: | Aliquot and freeze at -20℃. Avoid multiple freeze/thaw cycles. |
| Alternative names: | EL52 antibody |
| Epididymis luminal secretory protein 52 antibody | |
| Heat shock 86 kDa antibody | |
| Heat shock 90kD protein 1, alpha antibody | |
| Heat shock 90kD protein 1, alpha like 4 antibody | |
| Heat shock 90kD protein, alpha-like 4 antibody | |
| Heat shock 90kDa protein 1 alpha antibody | |
| Heat shock protein 90kDa alpha (cytosolic) class A member 1 antibody | |
| Heat shock protein HSP 90-alpha antibody | |
| HS90A_HUMAN antibody | |
| HSP 86 antibody | |
| HSP86 antibody | |
| Hsp89 antibody | |
| HSP89A antibody | |
| Hsp90 antibody | |
| HSP90A antibody | |
| HSP90AA1 antibody | |
| HSP90ALPHA antibody | |
| HSP90N antibody | |
| HSPC1 antibody | |
| HSPCA antibody | |
| HSPCAL1 antibody | |
| HSPCAL4 antibody | |
| HSPN antibody | |
| LAP 2 antibody | |
| LAP2 antibody | |
| Lipopolysaccharide-associated protein 2 antibody | |
| LPS-associated protein 2 antibody | |
| Renal carcinoma antigen NY-REN-38 antibody |
Target information
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).
Provider
Erpantech Laboratory
