PIN4 Human

Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 4 Human Recombinant

Cat. No.

BT1602

Source

Escherichia Coli.

Synonyms

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

Appearance

Sterile filtered colorless solution.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

PIN4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (1-156 a.a.) and having a molecular mass of 18.8kDa.
PIN4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (PIN4) is a key enzyme involved in cell cycle regulation. It acts as a peptidyl-prolyl cis/trans isomerase (PPIase) and interacts with NIMA. PIN4 exists in two isoforms: PAR14 and PAR17. Additionally, Pin4 protein exhibits the ability to bind to double-stranded DNA under physiological salt conditions.

Description

This product consists of the PIN4 protein produced in E.Coli. It is a single, non-glycosylated polypeptide chain comprising 176 amino acids (with amino acids 1-156 derived from the PIN4 sequence) and possesses a molecular mass of 18.8kDa. The PIN4 sequence is fused to a 20 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.

Physical Appearance

Clear, colorless solution devoid of particulate matter.

Formulation

The PIN4 protein is supplied in a solution at a concentration of 1mg/ml. The solution is buffered with 20mM Tris-HCl at a pH of 8.0 and supplemented with 10% glycerol, 1mM DTT, and 0.1mM PMSF.

Stability

For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Repeated cycles of freezing and thawing should be avoided.

Biological Activity

The specific activity of this product exceeds 300 nmoles/min/mg. Specific activity is defined as the amount of enzyme required to cleave 1 μmole of the substrate suc-AAFP-pNA per minute at a temperature of 25°C in a Tris-HCl buffer at pH 8.0 using chymotrypsin.

Purity

The purity of this product, as assessed by SDS-PAGE analysis, is greater than 85.0%.

Synonyms

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MPMAGLLKGL VRQLERFSVQ QQASKMPPKG KSGSGKAGKG GAASGSDSAD KKAQGPKGGG NAVKVRHILC EKHGKIMEAM EKLKSGMRFN EVAAQYSEDK ARQGGDLGWM TRGSMVGPFQ EAAFALPVSG MDKPVFTDPP VKTKFGYHII MVEGRK.

Product Science Overview

Discovery and Gene Encoding

The PIN4 gene was identified through a search of an expressed sequence tag (EST) database using human PIN1 and Escherichia coli parvulin sequences as probes. This led to the isolation of a cDNA encoding PIN4 from a lung cDNA library. The gene encoding PIN4 is located on the X chromosome and is expressed in various tissues, indicating its fundamental role in cellular processes.

Structure and Function

PIN4 has a unique structure that includes a peptidyl-prolyl isomerase domain, which is responsible for its enzymatic activity. This domain contains a nucleophilic cysteine residue (Cys113) that is crucial for its function. The enzyme catalyzes the cis/trans isomerization of proline residues in polypeptides, a process that is essential for proper protein folding and function.

Biological Role

PIN4 plays a significant role in several cellular processes, including the cell cycle, chromatin remodeling, and ribosome biogenesis. It is involved in the regulation of various signaling pathways by inducing conformational changes in key signaling molecules following proline-directed phosphorylation. This regulation is critical for maintaining cellular homeostasis and function.

Clinical Significance

The deregulation of PIN4 has been implicated in various diseases, particularly cancer. Overexpression of PIN4 has been observed in several types of cancer, including breast, cervical, ovarian, and endometrial cancers. This overexpression promotes cell proliferation and transformation, contributing to tumorigenesis. Targeting PIN4 with specific inhibitors has shown promise in reducing tumor progression and increasing survival in preclinical models.

Research and Therapeutic Potential

Recent research has focused on developing specific inhibitors for PIN4 to explore its therapeutic potential. One such inhibitor, Sulfopin, has demonstrated high affinity binding to PIN4 and inhibition of its catalytic activity. In preclinical studies, Sulfopin treatment led to tumor regression and increased survival in mouse models of cancer. These findings highlight the potential of PIN4 as a therapeutic target for cancer treatment.

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PIN4 Human

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