Recombinant Mouse Pin1 His Protein Summary
| Description |
A bioactive recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 1-165 of Mouse Pin1 Source: E.coli Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MGSMADEEKL PPGWEKRMSR SSGRVYYFNH ITNASQWERP SGGSTVGGSS KNGQGEPAKV RCSHLLVKHS QSRRPSSWRQ EKITRSKEEA LELINGYIQK IKSGEEDFES LASQFSDCSS AKARGDLGPF SRGQMQKPFE DASFALRTGE MSGPVFTDSG IHIILRTE |
| Details of Functionality |
Specific activity is > 1,200 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAPF-pNA per minute at 37C in Tris-HCl pH 8.0 using chymotrypsin. |
| Source |
E. coli |
| Protein/Peptide Type |
Recombinant Protein |
| Gene |
PIN1 |
| Purity |
>95%, by SDS-PAGE |
| Endotoxin Note |
< 1.0 EU per 1 microgram of protein (determined by LAL method) |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
20.8 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
| Buffer |
PBS (pH 7.4), 10% glycerol |
| Preservative |
No Preservative |
| Concentration |
1 mg/ml |
| Purity |
>95%, by SDS-PAGE |
Alternate Names for Recombinant Mouse Pin1 His Protein
Background
Pin-1 is a the peptidylprolyl cis/trans isomerase enzyme which is responsible, as its name suggests, for flipping the proline ring from the cis to the trans conformation. This enzyme is heavily upregulated in tumor cells, so that antibodies to this protein can be used as tumor markers. Pin-1 protein is concentrated in the nucleus in small punctate structures and is particularly obvious in tumor cells.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 1 year from date of receipt.
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