PIN1 Mouse
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
PIN1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 20.8kDa. PIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Recombinant Mouse PIN1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 188 amino acids, with the PIN1 sequence comprising amino acids 1-165, and has a molecular weight of 20.8 kDa. The protein includes an N-terminal 23 amino acid His-tag and is purified using proprietary chromatographic techniques.
The PIN1 protein solution is provided at a concentration of 1 mg/ml in a buffer consisting of phosphate-buffered saline (pH 7.4) and 10% glycerol.
The specific activity of the PIN1 protein is greater than 1,200 nmol/min/mg. This is measured as the amount of enzyme required to cleave 1 nmole of the substrate suc-AAFP-PNA per minute at a temperature of 37°C in Tris-HCl buffer at pH 8.0 using chymotrypsin.
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.
MGSSHHHHHH SSGLVPRGSH MGSMADEEKL PPGWEKRMSR SSGRVYYFNH ITNASQWERP SGGSTVGGSS KNGQGEPAKV RCSHLLVKHS QSRRPSSWRQ EKITRSKEEA LELINGYIQK IKSGEEDFES LASQFSDCSS AKARGDLGPF SRGQMQKPFE DASFALRTGE MSGPVFTDSG IHIILRTE.
Product Science Overview
PIN1 is a member of the peptidyl-prolyl cis/trans isomerase (PPIase) family, which is known for its ability to catalyze the isomerization of peptide bonds at proline residues . This specific isomerase interacts with phosphorylated serine/threonine-proline motifs, inducing conformational changes in its substrates . These conformational changes are critical for regulating the activity, stability, and function of various proteins involved in cell growth, stress responses, immune response, and neuronal differentiation .
The conformational regulation catalyzed by PIN1 has profound impacts on key proteins involved in several cellular processes . For instance, PIN1 is known to play a pivotal role in the regulation of cell growth, genotoxic stress responses, and the immune response . Additionally, it is involved in the induction and maintenance of pluripotency, germ cell development, and neuronal survival .
PIN1 has been implicated in the pathogenesis of several diseases, including Alzheimer’s disease and various cancers . In cancer, PIN1 is often overexpressed, driving oncogenesis by modulating the activity of oncogenes and tumor suppressors . The enzyme’s ability to regulate the post-phosphorylation conformation of its substrates makes it a potential target for therapeutic intervention .
Recent research has focused on developing specific inhibitors for PIN1 to explore its therapeutic potential . For example, a potent and specific covalent PIN1 inhibitor, Sulfopin, has been identified and shown to reduce tumor progression and increase survival in mouse models of cancer . This highlights the potential of targeting PIN1 in cancer therapy and other diseases where PIN1 plays a critical role .
