PET117 Human

PET117 Human Recombinant
Cat. No.
BT6558
Source
Escherichia Coli.
Synonyms
Protein PET117 homolog, mitochondrial, PET117, UNQ607/PRO1194.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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

PET117 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 82 amino acids (23-81) and having a molecular mass of 9.5kDa.
PET117 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
The PET117 gene, found on chromosome V near the HIS1 gene in S. cerevisiae, is essential for the formation of functional cytochrome c oxidase. Interestingly, despite its crucial role, the gene products are not part of the final cytochrome c oxidase complex.
Description
Recombinant human PET117, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 82 amino acids (residues 23-81), resulting in a molecular weight of 9.5 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus, and proprietary chromatographic techniques are employed.
Physical Appearance
The product is a sterile, colorless solution that has been filtered for sterility.
Formulation
The PET117 solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.2 M NaCl, 50% glycerol, and 2 mM DTT.
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 such as 0.1% HSA or BSA is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
SDS-PAGE analysis indicates a purity greater than 90%.
Synonyms
Protein PET117 homolog, mitochondrial, PET117, UNQ607/PRO1194.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVHVKQQW DQQRLRDGVI RDIERQIRKK ENIRLLGEQI ILTEQLEAER EKMLLAKGSQ KS.

Product Science Overview

Gene and Protein Structure

PET117 is located on chromosome V near the HIS1 gene in yeast. The human recombinant version of PET117 is expressed in Escherichia coli and is typically fused with a His-tag at the N-terminus for purification purposes. The recombinant protein corresponds to the amino acids 23-81 of the human PET117 sequence .

The amino acid sequence of the recombinant human PET117 protein is as follows:

MGSSHHHHHH SSGLVPRGSH MGSVHVKQQW DQQRLRDGVI RDIERQIRKK ENIRLLGEQI ILTEQLEAER EKMLLAKGSQ KS

The theoretical molecular weight of this protein is approximately 9.5 kDa, although the observed molecular weight may vary due to post-translational modifications and other experimental factors .

Expression and Purification

The recombinant human PET117 protein is expressed in Escherichia coli and purified using conventional chromatography techniques. The purity of the protein is greater than 90%, as determined by SDS-PAGE . The protein is typically stored in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.2 M NaCl, 50% glycerol, and 2 mM DTT to maintain its stability .

Functional Role

In yeast, PET117 is required for the assembly of active cytochrome c oxidase, an essential component of the mitochondrial electron transport chain. This enzyme complex is responsible for the final step in the mitochondrial respiratory chain, where electrons are transferred to oxygen, resulting in the formation of water. The proper assembly and function of cytochrome c oxidase are critical for cellular respiration and energy production .

Applications

Recombinant human PET117 protein is primarily used in research settings to study its role in mitochondrial function and its potential implications in human health and disease. The protein can be utilized in various applications, including SDS-PAGE and mass spectrometry (MS), to investigate its structure, function, and interactions with other proteins .

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