FKBP2 Human

FK506 Binding Protein 2 Human Recombinant
Cat. No.
BT20433
Source
Escherichia Coli.
Synonyms
FKBP13, FKBP-2, Peptidyl-prolyl cis-trans isomerase FKBP2, PPIase FKBP2, FK506-binding protein 2, Rotamase, Immunophilin FKBP13, 13 kDa FK506-binding protein, 13 kDa FKBP, FKBP-13, FKBP2, PPIase.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 90% 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

FKBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (22-142 a.a.) and having a molecular mass of 13.4 kDa. The FKBP2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
As a member of the immunophilin protein family, FKBP2 plays a role in immunoregulation and fundamental cellular processes such as protein folding and trafficking. This cis-trans prolyl isomerase exhibits binding affinity for the immunosuppressant drugs FK506 and rapamycin. Functionally, FKBP2 acts as an ER chaperone and participates in the formation of membrane cytoskeletal scaffolds.
Description
Recombinant human FKBP2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 122 amino acids (residues 22-142) and has a molecular weight of 13.4 kDa. The purification of FKBP2 is achieved through proprietary chromatographic techniques.
Physical Appearance
The product is a sterile-filtered solution, clear and colorless in appearance.
Formulation
The FKBP2 solution is formulated in a buffer containing 20mM Tris-HCl at pH 8.0, 1mM DTT (dithiothreitol), and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Repeated freeze-thaw cycles should be avoided.
Biological Activity
The specific activity of the enzyme is determined to be greater than 270 nmoles per minute per microgram. This is defined as the enzyme's capacity 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, utilizing chymotrypsin.
Purity
Analysis by SDS-PAGE indicates a purity greater than 90%.
Synonyms
FKBP13, FKBP-2, Peptidyl-prolyl cis-trans isomerase FKBP2, PPIase FKBP2, FK506-binding protein 2, Rotamase, Immunophilin FKBP13, 13 kDa FK506-binding protein, 13 kDa FKBP, FKBP-13, FKBP2, PPIase.
Source
Escherichia Coli.
Amino Acid Sequence
MATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK IPGGATLVFE VELLKIERRT EL.

Product Science Overview

Introduction

FK506 Binding Protein 2 (FKBP2), also known as FKBP13, is a member of the FK506-binding protein family. These proteins are peptidyl-prolyl cis-trans isomerases (PPIases) that play a crucial role in protein folding and immunoregulation. FKBP2 is particularly significant due to its involvement in various cellular processes, including protein folding within the endoplasmic reticulum (ER).

Structure and Function

FKBP2 is characterized by its ability to bind to the immunosuppressive drugs FK506 (tacrolimus) and rapamycin. This binding inhibits the activity of calcineurin, a phosphatase involved in T-cell activation, thereby exerting immunosuppressive effects. FKBP2 contains a PPIase domain, which catalyzes the cis-trans isomerization of proline residues in polypeptides, facilitating proper protein folding.

Role in Protein Folding

Within the ER, FKBP2 assists in the folding of newly synthesized proteins. It is particularly involved in the folding of proinsulin, a precursor to insulin. FKBP2 interacts with proinsulin and its chaperone GRP94, ensuring correct folding and preventing the formation of misfolded protein complexes . This function is critical for maintaining cellular homeostasis and preventing ER stress.

Clinical Significance

The immunosuppressive properties of FKBP2 have therapeutic implications, particularly in organ transplantation and autoimmune diseases. By inhibiting calcineurin, FKBP2 helps prevent the rejection of transplanted organs and reduces the activity of the immune system in autoimmune conditions. Additionally, FKBP2’s role in protein folding makes it a potential target for treating diseases associated with protein misfolding and ER stress.

Research and Applications

Recent studies have explored the broader implications of FKBP2 in various biological processes and diseases. For instance, FKBP2 has been implicated in the regulation of calcium signaling pathways through its interaction with ryanodine receptors . This interaction is crucial for maintaining calcium homeostasis in cells, which is essential for numerous physiological functions.

Moreover, FKBP2’s involvement in the Notch signaling pathway highlights its potential role in developmental processes and cancer . Understanding the molecular mechanisms of FKBP2 can lead to the development of novel therapeutic strategies targeting these pathways.

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