Recombinant Human PPIL1 Protein

Name: Recombinant Human PPIL1 Protein
Brand: Beta LifeScience
SKU: BLA-7119P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Synonym	CGI 124 CGI-124 CGI124 Cyclophilin related gene 1 cyclophilin-related gene 1 cyclophilinrelated gene 1 CYPL1 hCyPX MGC678 peptidyl-prolyl cis-trans isomerase Peptidyl-prolyl cis-trans isomerase-like 1 Peptidylprolyl isomerase (cyclophilin) like 1 peptidylprolyl isomerase (cyclophilin)-like 1 peptidylprolyl isomerase (cyclophilin)like 1 peptidylprolyl isomerase (cyclophilin)like1 peptidylprolyl isomerase like 1 PPIase PPIL1 PPIL1_HUMAN rotamase Rotamase PPIL1
Description	Recombinant Human PPIL1 Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNG TKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAM ANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQ DRPVDDVKIIKAYPSGLEHHHHHH
Purity	>95% purity as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 µmole of suc-AAFP-pNA per minute at 25°C in Tris-Hcl pH8.0 using chymotrypsin.Activity AssayPrepare 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 PPIL1 protein with 1 µg in assay buffer. Mix by inversion and equilibrate to 1deg;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.
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycle.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.