Analytical Data
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Gene name
PPAP2B
- Application
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Alternative Names
Dri42; LPP3; PAP-2b; PAP2-b; PAP2-beta; VCIP; Lipid phosphate phosphohydrolase 3; Vascular endothelial growth factor and type I collagen-inducible protein
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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 90% as determined by SDS-PAGE.
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Uniprot
O14495
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Expression Region
Ser57~Ser194
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Molecular Weight
19.3kDa
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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
PPAP2B, also known as Phosphatidate Phosphatase 2B, is a crucial enzyme involved in lipid metabolism and cellular signaling processes. It plays a significant role in regulating levels of lysophosphatidic acid (LPA) and phosphatidic acid (PA), both of which are essential lipid mediators in cellular functions, including proliferation, survival, and differentiation. Dysregulation of PPAP2B is linked to various pathological conditions, including cancer, cardiovascular diseases, and metabolic disorders. Given its importance, researchers have focused on investigating the structure and function of PPAP2B through recombinant protein expression systems. These studies aim to provide insights into the enzyme's biochemical properties, optimal activity conditions, and potential regulatory mechanisms. Moreover, utilizing recombinant PPAP2B allows for detailed analyses of its interactions with cellular substrates and signaling pathways, which can enhance the understanding of its roles in health and disease. The ongoing research on PPAP2B is expected to pave the way for the development of targeted therapeutic strategies that can modulate its activity, offering new avenues for treating diseases associated with its dysregulation.
