NDUFB4 Human

NADH Dehydrogenase 1 Beta Subcomplex 4 Human Recombinant
Cat. No.
BT13039
Source
E.Coli
Synonyms
B15, CI-B15, Complex I-B15, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4, NADH-ubiquinone oxidoreductase B15 subunit.
Appearance
Sterile Filtered 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

NDUFB4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87) and having a molecular mass of 12.6kDa.
NDUFB4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
NADH Dehydrogenase 1 Beta Subcomplex 4 (NDUFB4) is a protein that is part of Complex I, the first enzyme complex in the mitochondrial electron transport chain. This complex is responsible for transferring electrons from NADH to ubiquinone. NDUFB4 itself does not have catalytic activity and is considered a structural subunit.
Description
This product consists of the human NDUFB4 protein, recombinantly produced in E. coli. It is a single polypeptide chain of 110 amino acids (including a 23 amino acid His-tag at the N-terminus for purification) with a molecular weight of 12.6 kDa. The protein is not glycosylated. It has been purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The NDUFB4 protein is supplied at a concentration of 1 mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 0.4M Urea, and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the product frozen at -20°C. Adding a carrier protein such as HSA or BSA (0.1%) is advisable for long-term storage. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of the NDUFB4 protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
B15, CI-B15, Complex I-B15, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4, NADH-ubiquinone oxidoreductase B15 subunit.
Source
E.Coli
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSFPKYK PSSLRTLPET LDPAEYNISP ETRRAQAERL AIRAQLKREY LLQYNDPNRR GLIENPALLR WAYARTINVY PNFRPTPKNS.

Product Science Overview

Structure and Function

NDUFB4 is an accessory subunit of Complex I, which is the first enzyme complex in the mitochondrial electron transport chain. Complex I is responsible for transferring electrons from NADH to ubiquinone, a process that is essential for ATP synthesis through oxidative phosphorylation . Although NDUFB4 is not directly involved in the catalytic activity of Complex I, it is believed to play a role in the structural stability and functional assembly of the complex .

Genetic Information

The NDUFB4 gene is located on chromosome 3 and encodes a protein that is approximately 15 kDa in size . The gene has several aliases, including NADH:Ubiquinone Oxidoreductase Subunit B4, Complex I-B15, and CI-B15 . The protein is expressed in various tissues and is essential for normal mitochondrial function .

Clinical Significance

Mutations or dysfunctions in the NDUFB4 gene can lead to mitochondrial diseases and other disorders. For example, it has been associated with Hantavirus Hemorrhagic Fever with Renal Syndrome and other mitochondrial-related diseases . Understanding the role of NDUFB4 in these conditions can provide insights into potential therapeutic targets.

Recombinant NDUFB4

Recombinant human NDUFB4 protein is often used in research to study its function and role in the mitochondrial respiratory chain. It is typically expressed in Escherichia coli and purified to a high degree of purity (>90%) for use in various biochemical assays . The recombinant protein is useful for studying the structural and functional aspects of Complex I, as well as for developing potential therapeutic interventions .

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