Analytical Data
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Gene name
PPIL2
- Application
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Alternative Names
PPIL2;RING-type E3 ubiquitin-Protein ligase PPIL2
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Species
Human
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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
Q13356
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Expression Region
1-520aa
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AA Sequence
MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV GKYINPAATK RAAEEEPSTS ATVPMSKKKP SRGFGDFSSW
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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
PPIL2 (peptidyl-prolyl isomerase-like 2) is a member of the cyclophilin family, which plays a crucial role in protein folding and post-translational modifications. Research into PPIL2 has garnered attention due to its potential implications in various biological processes, including cellular signaling, cell cycle regulation, and responses to stress. Its isomerase activity is essential for the proper conformation of proteins, influencing critical cellular functions. Dysregulation of PPIL2 has been linked to several diseases, including cancer and neurodegenerative disorders, suggesting that it may be a valuable target for therapeutic intervention. Furthermore, PPIL2's interactions with other proteins and involvement in molecular pathways highlight its importance in maintaining cellular homeostasis. Understanding the structure and function of recombinant PPIL2 can provide insights into its role in health and disease, paving the way for research into novel treatments that modulate its activity. By investigating the biochemical properties and potential applications of recombinant PPIL2, researchers aim to elucidate its contribution to various physiological processes and its perturbations in pathological conditions, thereby laying the groundwork for future studies focused on harnessing its therapeutic potential.
