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hsp90a.1 Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q90474 |
| Reactivity | Zebrafish |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Clone/Animal Names | RB47443 |
| Calculated MW | 83319 Da |
| Antigen Region | 229-263 aa |
| Gene ID | 30591 |
|---|---|
| Other Names | Heat shock protein HSP 90-alpha 1, hsp90a1, hsp90, hsp90a, hsp90aa1 |
| Target/Specificity | This hsp90a.1 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 229-263 amino acids from the Central region of human (DANRE) hsp90a.1. |
| Dilution | WB~~1:2000 IHC-P~~1:25 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | hsp90a.1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | hsp90a.1 |
|---|---|
| Synonyms | hsp90, hsp90a, hsp90aa1 |
| Function | 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. 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 (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly (PubMed:10364427, PubMed:17586488, PubMed:18182494, PubMed:18256191). |
| Cellular Location | Melanosome {ECO:0000250|UniProtKB:P07900}. Cytoplasm, myofibril, sarcomere, Z line Cytoplasm, myofibril, sarcomere, A band Cytoplasm, perinuclear region Note=Expressed at the Z line and in the perinuclear region of myofibrils. Shuttles between the Z line and A band in response to stress conditions and fibril damage |
| Tissue Location | Strongly expressed in the early embryos within the somitic slow muscle progenitors, the adaxial cells that lie on either side of the notochord but not the notochord. Also expressed during the early differentiation of fast fibers. Detected in developing cardiac muscles and pectoral fin primordia. Not detected in mature muscle fibers. |
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Provided below are standard protocols that you may find useful for product applications.
Background
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 (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.
References
Lele Z.,et al.Dev. Biol. 210:56-70(1999).
Etard C.,et al.Dev. Biol. 308:133-143(2007).
Etard C.,et al.J. Cell Biol. 180:1163-1175(2008).
Howe K.,et al.Nature 496:498-503(2013).
Krone P.H.,et al.Biochem. Biophys. Res. Commun. 204:746-752(1994).
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