NCF1 Human

Neutrophil Cytosolic Factor 1 Human Recombinant
Cat. No.
BT18021
Source
Escherichia Coli.
Synonyms
NCF1A, NOXO2, p47phox, SH3PXD1A .
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.
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Description

NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
NCF1, a cytosolic protein, functions as a subunit of the neutrophil NADPH oxidase, an enzyme complex responsible for generating superoxide anions. This multi-component enzyme requires NCF1, along with NCF2 and cytochrome b558 (membrane-bound), for its activation and subsequent superoxide production. Mutations in the NCF1 gene are linked to chronic granulomatous disease.
Description
Recombinant Human NCF1, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 45.7 kDa. It consists of 398 amino acids, with residues 1-390 representing the NCF1 sequence. An 8-amino acid His-tag is fused to the C-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear and colorless solution that has been sterilized by filtration.
Formulation
The solution contains 0.5mg of protein per ml and is formulated in a buffer consisting of 20mM Tris-HCl at pH 8, 1mM DTT, 0.1M NaCl, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the solution can be stored at 4°C. For extended periods, it is recommended to store the protein in frozen aliquots at -20°C. To further enhance stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Repeated freezing and thawing of the protein solution should be avoided.
Purity
Analysis by SDS-PAGE confirms that the purity of the protein is greater than 90%.
Synonyms
NCF1A, NOXO2, p47phox, SH3PXD1A .
Source
Escherichia Coli.
Amino Acid Sequence
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.

Product Science Overview

Structure and Function

NCF1 is a 47 kDa cytosolic subunit of the NADPH oxidase complex . The protein is essential for the activation of the NADPH oxidase complex, which is crucial for the production of superoxide anion . NCF1 cooperates with other subunits, such as NCF2 (p67phox), NCF4 (p40phox), CYBB (gp91phox), and CYBA (p22phox), to form a functional enzyme complex .

Genetic Variability and Associated Diseases

Mutations in the NCF1 gene have been linked to Chronic Granulomatous Disease (CGD), an inherited immunodeficiency disorder characterized by the inability of phagocytes to produce reactive oxygen species . This results in recurrent bacterial and fungal infections. Additionally, genetic variability in the NCF1 gene has been associated with a higher risk of autoimmune diseases such as Sjögren’s syndrome, rheumatoid arthritis, and lupus erythematosus .

Recombinant NCF1

Recombinant NCF1 is produced using E. coli expression systems and is often tagged with a His-tag for purification purposes . The recombinant protein is used in various research applications to study the function and regulation of the NADPH oxidase complex, as well as to investigate the molecular mechanisms underlying diseases associated with NCF1 dysfunction .

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Source
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THE BIOTEK
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