PPIL4 Human

Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant
Cat. No.
BT4271
Source
Escherichia Coli.
Synonyms
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
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. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

PPIL4 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 512 amino acids (1-492 a.a.) and having a molecular mass of 59.4kDa. The PPIL4 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
PPIL4, a member of the cyclophilin-type PPIase protein family, is found in various tissues, especially the kidney. It primarily resides in the nucleus and possesses several domains: a PPIase cyclophilin-type domain, a lysine-rich domain, two bipartite nuclear targeting sequences, and an RNA recognition motif (RRM) domain. The combination of the RRM domain and nuclear targeting sequences suggests PPIL4's potential role in regulating transcription.
Description
Recombinant human PPIL4, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 59.4 kDa. It consists of 512 amino acids, including a 20 amino acid His tag at the N-terminus (1-492 a.a.). Purification is achieved through proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The PPIL4 solution is provided at a concentration of 0.5 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 10% glycerol, 2mM DTT, and 0.1M NaCl.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
SDS-PAGE analysis indicates a purity greater than 85%.
Biological Activity
The specific activity, determined by measuring the enzyme's ability to cleave suc-AAFP-pNA at 25°C in Tris-Hcl pH 8.0 using chymotrypsin, is greater than 190 nmoles/min/mg. This represents the amount of enzyme needed to cleave 1 µmole of suc-AAFP-pNA per minute.
Synonyms
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR.

Product Science Overview

Introduction

Peptidylprolyl isomerases (PPIases) are a family of enzymes that catalyze the cis-trans isomerization of proline imidic peptide bonds in proteins, which is a critical step in protein folding. Cyclophilins are a subset of PPIases and are known for their role in protein folding, immunosuppression, and various cellular processes.

Cyclophilin-Like 4 (CYP4)

Cyclophilin-Like 4 (CYP4) is a member of the cyclophilin family. While the specific functions of CYP4 are not as well-characterized as other cyclophilins, it shares the common structural and functional features of the family. Cyclophilins, including CYP4, are involved in protein folding, trafficking, and immune regulation.

Human Recombinant Cyclophilin-Like 4

Recombinant proteins are proteins that are artificially produced through recombinant DNA technology. Human recombinant Cyclophilin-Like 4 (CYP4) is produced by inserting the gene encoding CYP4 into an expression system, such as bacteria or yeast, which then produces the protein. This allows for the study and utilization of CYP4 in various research and therapeutic applications.

Biological Functions

Cyclophilins, including CYP4, play a role in:

  • Protein Folding: Catalyzing the cis-trans isomerization of proline residues, which is essential for proper protein folding.
  • Immunosuppression: Cyclophilins are known to bind to immunosuppressive drugs like cyclosporin A, which inhibits calcineurin and prevents T-cell activation.
  • Cellular Processes: Involvement in various cellular processes such as signal transduction, apoptosis, and cell proliferation.
Expression and Tissue Distribution

Cyclophilins are ubiquitously expressed in various tissues. The expression patterns of CYP4 specifically are not well-documented, but it is likely to be expressed in multiple tissues similar to other cyclophilins.

Research and Therapeutic Applications

Recombinant human CYP4 can be used in research to study its structure, function, and interactions with other proteins. It may also have potential therapeutic applications, such as in the development of immunosuppressive therapies or treatments for diseases involving protein misfolding.

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