Analytical Data
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Gene name
PPIH
- Application
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Alternative Names
Cyclophilin H; CYP-20; CypH; Peptidyl prolyl cis trans isomerase H; Peptidyl-prolyl cis-trans isomerase H; Peptidylprolyl isomerase H; PPIase H; PPIH; PPIH_HUMAN; RGD1564921; Rotamase H; Small nuclear ribonucleoprotein particle specific cyclophilin H; Small nuclear ribonucleoprotein particle-specific cyclophilin H; SnuCyp 20; U snRNP associated cyclophilin SnuCyp 20; U-snRNP-associated cyclophilin SnuCyp-20; USA CYP; USA-CYP; USACYP
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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
O43447
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Expression Region
2-177 aa
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AA Sequence
AVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE FRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM
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Molecular Weight
19.20 kDa
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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
PPIH (Peptidyl-prolyl isomerase H) is a member of the cyclophilin family of proteins that play critical roles in various biological processes, including protein folding, cell signaling, and immune response. Research into PPIH has gained significance due to its potential implications in several diseases, such as cancer and neurodegenerative disorders, where protein misfolding and aggregation are key contributors. The structural and functional characterization of PPIH is essential to understand its biological mechanisms and to explore its therapeutic potential. Recent advances in recombinant protein technology allow for the production of PPIH in large quantities, facilitating detailed investigations. By studying the enzymatic activity, binding properties, and interaction networks of PPIH, researchers aim to uncover its role in cellular homeostasis and disease pathology. Furthermore, understanding PPIH's mechanism of action could lead to the development of novel drugs that target misfolded proteins, thus paving the way for innovative treatments in diseases characterized by impaired protein function. The ongoing research on recombinant PPIH not only enhances our basic understanding of protein dynamics but also positions this protein as a potential biomarker or therapeutic target in clinical applications.
