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AB93731

Recombinant human PPIL2 protein

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Recombinant human PPIL2 protein is a Human Full Length protein, in the 1 to 527 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.

View Alternative Names

RING-type E3 ubiquitin-protein ligase PPIL2, CYC4, Cyclophilin-60, Probable inactive peptidyl-prolyl cis-trans isomerase-like 2, Rotamase PPIL2, Cyclophilin-like protein Cyp-60, Cyp60, hCyP-60, PPIase, PPIL2

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SDS-PAGE - Recombinant human PPIL2 protein (AB93731)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PPIL2 protein (AB93731)

15% SDS Page of 3ug ab93731

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific activity is > 290 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 μmole of suc-AAPF-pNA per minute at 37°C in Tris-Hcl pH8.0 using chymotrypsin.

Activity Assay

Prepare 170 μl assay buffer into a suitable container and pre-chill on ice before use: The final concentrations are 200 mM Tris-Hcl, pH 8.0, and 20nM chymotrypsin. Add 10 μl of recombinant PPIL2 protein with 1 μg in assay buffer. Mix by inversion and equilibrate to 1°C and monitor the A405nm until the value is constant using a spectrophotometer. Add 20 μl pre-chilled 5mM suc-AAFP-pNA. (Substrate was dissolved in TFE that contained 460mM LiCl to a concentration of 3 mM) Record the increase in A405 nm for 30 minutes at 25°C.

Accession

Q13356

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGKRQHQKDKMYITCAEYTHFYGGKKPDLPQTNFRRLPFDHCSLSLQPFVYPVCTPDGIVFDLLNIVPWLKKYGTNPSNGEKLDGRSLIKLNFSKNSEGKYHCPVLFTVFTNNTHIVAVRTTGNVYAYEAVEQLNIKAKNFRDLLTDEPFSRQDIITLQDPTNLDKFNVSNFYHVKNNMKIIDPDEEKAKQDPSYYLKNTNAETRETLQELYKEFKGDEILAATMKAPEKKKVDKLNAAHYSTGKVSASFTSTAMVPETTHEAAAIDEDVLRYQFVKKKGYVRLHTNKGDLNLELHCDLTPKTCENFIRLCKKHYYDGTIFHRSIRNFVIQGGDPTGTGTGGESYWGKPFKDEFRPNLSHTGRGILSMANSGPNSNRSQFFITFRSCAYLDKKHTIFGRVVGGFDVLTAMENVESDPKTDRPKEEIRIDATTVFVDPYEEADAQIAQERKTQLKVAPETKVKSSQPQAGSQGPQTFRQGVGKYINPAATEQQRKSPQPVPLSPCPRRSPVGVLGTSAPGSSRLPDDH","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":527,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q13356","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Cyclophilin-like 2 (PPIL2) is a protein encoded by the PPIL2 gene. It possesses peptidyl-prolyl cis-trans isomerase activity which facilitates protein folding. PPIL2 with a molecular mass of approximately 64 kDa is involved in various cellular processes. It gets expressed in many tissues such as the brain and testis. Scientists often study it using models like human cell lines to better grasp its functions in different contexts.
Biological function summary

The protein interacts with elements of the spliceosome complex contributing to pre-mRNA processing. PPIL2 partners with other molecular chaperones to regulate protein folding and quality control within the endoplasmic reticulum. These interactions influence how proteins fold stabilize and function. The protein's role in chaperone-mediated processes highlights its impact on maintaining cellular protein homeostasis.

Pathways

PPIL2 participates in the mRNA splicing pathway where it influences gene expression. It interacts with various splicing factors such as Cyclophilin A which aids in assembling and modulating spliceosome components. Another important pathway involving PPIL2 is protein processing in the endoplasmic reticulum. PPIL2 interacts with specific proteins like U-box E3 ubiquitin ligases to manage protein degradation further controlling cellular mechanisms.

Researchers associate PPIL2 with neurodegenerative diseases and cancer. Aberrations in PPIL2's function or expression can lead to the accumulation of misfolded proteins contributing to neurodegenerative conditions like Alzheimer's disease. In cancer its interaction with various oncogenic pathways can affect tumorigenesis. PPIL2's relationship with proteins like p53 in these disorders underlines its potential role in disease progression and presents it as a target for therapeutic strategies.
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Specifications

Form

Liquid

Additional notes

Purified using conventional chromatography techniques.

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General info

Function

Has a ubiquitin-protein ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation (PubMed : 11435423). May also function as a chaperone, playing a role in transport to the cell membrane of BSG/Basigin for instance (PubMed : 15946952). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed : 20676357). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable).

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Has a ubiquitin-protein ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation (PubMed : 11435423). May also function as a chaperone, playing a role in transport to the cell membrane of BSG/Basigin for instance (PubMed : 15946952). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed : 20676357). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable).
See full target information RING-type E3 ubiquitin-protein ligase PPIL2
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