Analytical Data
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Gene name
PRL2A1
- Application
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Alternative Names
PRL2A1；Prlpm；Prolactin-2A1
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Species
Rat
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9JII3
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Expression Region
30-228aa
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AA Sequence
V PTCLVRNGRC FASLEEMLER AVGLSEEISK QALQLFTEFD NQYAQSKQLI NKNFKKCHTS SLELPKPSST SVQTHPITLL KIASKLLSAW KVPLNDLVNN LPSLKDIHPN ILSKAREIEA KSAGLLEGVK SILIQMQNGD TEDENYPGWS GLASLQSENE DDRLFAYYNM IRCEGRETQK VETALKMVKC KISNENNC
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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
PRL2A1, a member of the phosphatase of regenerating liver (PRL) family, is an important protein implicated in various cellular processes, including cellular signaling, proliferation, and differentiation. Research has highlighted PRL2A1's role in tumorigenesis, where its dysregulation can contribute to cancer progression. The protein is known to possess dual specificity phosphatase activity, which allows it to dephosphorylate a variety of substrates, thus influencing multiple signaling pathways. Recent studies have indicated that PRL2A1 may interact with key oncogenic pathways, making it a potential biomarker for cancer diagnostics and a target for therapeutic interventions. Additionally, understanding the three-dimensional structure of PRL2A1 through recombinant protein techniques can provide insights into its functional mechanisms and interactions within the cell. As a result, the study of PRL2A1 as a recombinant protein is crucial for elucidating its biological roles and exploring its potential in clinical applications, particularly in cancer biology. By investigating the expression, purification, and functional characterization of PRL2A1, researchers aim to develop novel strategies for targeted therapies that can improve patient outcomes in cancer treatment.
