Analytical Data
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Gene name
MINPP1
- Application
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Alternative Names
2,3-bisphosphoglycerate 3-phosphatase (EC:3.1.3.80) ;2,3-BPG phosphataseInositol (1,3,4,5)-tetrakisphosphate 3-phosphatase ;Ins(1,3,4,5)P(4) 3-phosphatase
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UNW1
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Expression Region
31-487aa
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Molecular Weight
79.1 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
MINPP1, also known as multiple inositol polyphosphate phosphatase 1, is an enzyme that plays a crucial role in cellular signaling and phosphoinositide metabolism. It dephosphorylates various inositol phosphates, which are critical secondary messengers involved in a multitude of cellular processes, including cell growth, differentiation, and apoptosis. The study of MINPP1 has gained attention due to its implications in various diseases, including cancer and neurodegenerative disorders. Dysregulation of MINPP1 activity has been linked to abnormal cellular signaling pathways, prompting researchers to investigate its functional roles and regulatory mechanisms further. As a recombinant protein, MINPP1 can be produced in controlled laboratory settings, allowing for detailed biochemical studies to elucidate its enzymatic properties, substrate specificity, and interaction with other cellular components. Understanding these aspects of MINPP1 can provide insights into its potential as a therapeutic target and its involvement in disease pathogenesis, making it a topic of significant interest in the fields of molecular biology and biochemistry.











