Analytical Data
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Gene name
MYH9
- Application
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Alternative Names
MYH9；Myosin-9
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35579
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Expression Region
2-241aa
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AA Sequence
AQQAADKYLYVDKNFINNPLAQADWAAKKLVWVPSDKSGFEPASLKEEVGEEAIVELVENGKKVKVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI
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Molecular Weight
54.2kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
MYH9, or Myosin Heavy Chain 9, is a critical gene that encodes a non-muscle myosin heavy chain involved in various cellular processes, including cell motility, cytokinesis, and cytoskeletal organization. Mutations in the MYH9 gene have been associated with several human disorders, such as May-Hegglin anomaly, Fechtner syndrome, and Sebastian syndrome, which primarily manifest as hematological abnormalities and platelet dysfunction. Research into MYH9 recombinant proteins has gained momentum due to their potential utility in understanding the molecular mechanisms underlying these conditions and for developing therapeutic strategies. By producing and analyzing MYH9 recombinant proteins, scientists can explore the functional consequences of specific mutations, investigate protein interactions, and assess the impact of MYH9 on cellular dynamics. Furthermore, the recombinant proteins can serve as valuable tools for drug testing and the development of targeted therapeutics. Given the critical roles of MYH9 in various biological processes, the study of its recombinant forms not only enhances our understanding of related pathologies but also lays the groundwork for potential advances in treatment approaches for MYH9-related diseases.
