Recombinant Zebrafish Heat Shock Protein Hsp 90-Alpha 1 (HSP90A.1) Protein (His&Myc)

Name: Recombinant Zebrafish Heat Shock Protein Hsp 90-Alpha 1 (HSP90A.1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-05089P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Zebrafish Heat Shock Protein Hsp 90-Alpha 1 (HSP90A.1) Protein (His&Myc) is produced by our Baculovirus expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q90474
Target Symbol	HSP90A.1
Synonyms	hsp90a.1; hsp90; hsp90a; hsp90aa1; zgc:86652Heat shock protein HSP 90-alpha 1
Species	Danio rerio (Zebrafish) (Brachydanio rerio)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	HNDDEQYIWESAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEVAAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIK
Expression Range	151-355aa
Protein Length	Partial
Mol. Weight	27.9 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.
Subcellular Location	Melanosome. 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.
Protein Families	Heat shock protein 90 family
Database References	KEGG: dre:30591 STRING: 7955.ENSDARP00000022302 UniGene: Dr.75834
Tissue Specificity	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 ca

Gene Functions References

The study shows that a conserved tryptophan in the middle domain senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-pi interaction with a neighboring lysine. PMID: 29662162
The transcriptional up-regulation of unc45b, hsp90aa1.1 and smyd1b is specific to zebrafish mutants with myosin folding defects, and is not triggered in other zebrafish myopathy models PMID: 26631063
Data indicate that heat shock protein 90alpha (Hsp90alpha1) function in myosin thick filament organization is potentially regulated by post-translational modification (PTM) involving phosphorylation and acetylation. PMID: 26562659
The chaperone proteins Ahsa1 and Hsp90 promote severe craniofacial phenotypes in zebrafish model of HDR syndrome. PMID: 23720234
Perturbation of the HSP70-HSP90 heat-shock protein axis stimulates degradation of endothelial VEGFR2. PMID: 23139789
studies indicate that the hsp90alpha1 mutant phenotype is not simply due to disruption of myosin folding and assembly, suggesting that Hsp90alpha1 may play a role in the assembly and organization of other sarcomeric structures PMID: 20049323
Mild perturbation of Hsp90 function at critical developmental stages may underpin the variable penetrance and expressivity of many developmental anomalies where the interaction between genotype and environment plays a major role. PMID: 17397257
Steif/Unc-45b interacts with the chaperone Hsp90a in vitro. The two genes are co-expressed in the skeletal musculature. PMID: 17586488
Embryonic heat shock reveals latent hsp90 translation in zebrafish. PMID: 18033674
Loss of Hsp90a function leads to the downregulation of genes encoding sarcomeric proteins and upregulation of hsp90a and several other genes encoding proteins that may act with Hsp90a during sarcomere assembly. PMID: 18256191
In response to stress or damage to the myofiber, Unc45b and Hsp90a dissociate from the Z line and transiently associate with myosin. PMID: 18347070

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.