Analytical Data
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Gene name
Prostatic acid Phosphatase/ACPP
- Application
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Alternative Names
PSAP; ACPP; ACP3; PAPf39; 5'-NT; Prostatic Specific Acid Phosphatase; Ecto-5'-Nucleotidase
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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
P15309
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Expression Region
Ser217~Asp386
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Molecular Weight
20kDa
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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
Prostatic acid phosphatase (PAP), also known as acid phosphatase-related protein (ACPP), is an enzyme predominantly expressed in the prostate and has garnered attention due to its potential role in prostate cancer diagnosis and therapy. Historically, elevated levels of PAP in serum have been associated with metastatic prostate cancer, making it a valuable biomarker for clinicians. Recent research has focused on the recombinant production of PAP/ACPP protein to facilitate studies regarding its enzymatic properties, physiological roles, and pathological implications. Advances in recombinant DNA technology allow for the efficient expression and purification of PAP/ACPP, enabling detailed investigations into its structure-function relationships, substrate specificity, and interactions with other proteins. Understanding these aspects could lead to the development of novel therapeutic strategies and diagnostic tools for prostate cancer. Furthermore, exploring the modulation of PAP activity may provide insights into its role in tumor microenvironments and contribute to the identification of prognostic markers. The research surrounding recombinant PAP/ACPP is instrumental in advancing our knowledge of prostate cancer biology and could have significant implications for patient management and treatment options.
