Analytical Data
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Gene name
ACTL7A
- Application
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Alternative Names
Actin-like-7-alpha
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y615
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Expression Region
1-435aa
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Molecular Weight
64.6 kDa
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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
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Protein Description
ACTL7A, also known as actin-like protein 7A, is a member of the actin superfamily that plays a critical role in various cellular processes, including muscle contraction, cell motility, and intracellular transport. Its unique structural characteristics and expression patterns suggest that it may be involved in specific cellular mechanisms distinct from conventional actins. In recent years, there has been increasing interest in studying recombinant ACTL7A protein to elucidate its functional properties and physiological relevance. Various research efforts have focused on the recombinant production of ACTL7A in heterologous systems, which allows for detailed analyses of its biophysical and biochemical properties, including polymerization kinetics and binding interactions. Understanding ACTL7A's role in cellular dynamics could provide insights into its involvement in diseases where actin regulation is disrupted, such as cancer and muscular disorders. Furthermore, ACTL7A's unique properties make it a potential target for biotechnological applications, including the development of novel biomaterials or therapeutic strategies. Overall, the study of recombinant ACTL7A protein holds promise for advancing our understanding of actin-related functions in health and disease, while also exploring its potential utility in various biotechnological applications.











