Analytical Data
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Gene name
Acylphosphatase-2/ACYP2
- Application
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Alternative Names
ACYM; ACYP; Acylphosphatase, muscle type isozyme; Acylphosphatase 2, Muscle; Acylphosphate phosphohydrolase 2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P14621
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Expression Region
Ser2~Tyr99
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Molecular Weight
15kDa
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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
Acylphosphatase-2 (ACYP2) is an enzyme that plays a significant role in various biological processes, including cellular signaling and energy metabolism. It is involved in the hydrolysis of acyl-phosphates, which are critical intermediates in metabolic pathways. Research has shown that ACYP2 exhibits a distinct expression pattern in different tissue types and is associated with several physiological functions, such as muscle contraction and neuronal signaling. The study of recombinant ACYP2 proteins has gained attention due to their potential applications in therapeutic scenarios and their role in understanding metabolic diseases. The ability to produce ACYP2 in a recombinant form allows for advanced biochemical studies, enzyme kinetics, and structural analysis, providing insights into its functional mechanisms. Furthermore, investigating the structure-function relationship of ACYP2 can reveal its involvement in disorders linked to metabolism and potentially aid in the development of novel therapeutic strategies. Overall, the exploration of ACYP2 and its recombinant forms not only enhances our understanding of its biological significance but also opens avenues for biomedical applications in managing metabolic-related diseases.











