Recombinant Human NDUFB6 Protein, N-His-SUMO & C-Strep

Reference: YHB53601
Product nameRecombinant Human NDUFB6 Protein, N-His-SUMO & C-Strep
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight21.86 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeThr2-Ser68
Aliases /SynonymsNDUFB6, NADH-ubiquinone oxidoreductase B17 subunit, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6, Complex I-B17, CI-B17
ReferenceYHB53601
NoteFor research use only.

Description of Recombinant Human NDUFB6 Protein, N-His-SUMO & C-Strep

Introduction

Recombinant proteins have become an essential tool in various fields of research, including biotechnology, medicine, and biochemistry. These proteins are produced by genetically engineering a specific gene into a host organism, typically a bacterial or mammalian cell, to produce large quantities of the desired protein. One such protein is Recombinant Human NDUFB6, which plays a crucial role in the structure and function of the respiratory chain complex I. In this article, we will explore the structure, activity, and application of Recombinant Human NDUFB6 Protein.

Structure of Recombinant Human NDUFB6 Protein

Recombinant Human NDUFB6 Protein is a subunit of the NADH:ubiquinone oxidoreductase, also known as complex I, which is the first enzyme in the mitochondrial respiratory chain. The gene encoding NDUFB6 is located on chromosome 9 and consists of 6 exons that span over 10 kb. The protein has a molecular weight of approximately 18 kDa and is composed of 161 amino acids. The primary structure of NDUFB6 contains a conserved N-terminal domain, a transmembrane domain, and a C-terminal domain. The N-terminal domain is essential for the stability and assembly of complex I, while the transmembrane domain plays a role in the interaction with other subunits of the complex. The C-terminal domain is responsible for the binding of NADH and the transfer of electrons to the respiratory chain.

Activity of Recombinant Human NDUFB6 Protein

Recombinant Human NDUFB6 Protein is a critical component of the respiratory chain complex I, which is responsible for the transfer of electrons from NADH to ubiquinone, generating a proton gradient across the mitochondrial inner membrane. This gradient is then used to produce ATP, the energy currency of the cell. NDUFB6 is involved in the initial steps of electron transfer, where it accepts electrons from NADH and transfers them to the next subunit of the complex. This process is crucial for the proper functioning of the respiratory chain and the production of energy in the form of ATP.

Application of Recombinant Human NDUFB6 Protein

Recombinant Human NDUFB6 Protein has various applications in both research and medicine. In research, it is used in the study of mitochondrial function and dysfunction, particularly in the context of complex I deficiency, which is associated with various human diseases. Recombinant NDUFB6 has also been used in the production of monoclonal antibodies for the detection of complex I subunits in various tissues and cell types. In medicine, NDUFB6 has been identified as a potential therapeutic target for the treatment of complex I-related diseases, such as Parkinson’s disease and Leber’s hereditary optic neuropathy. Additionally, recombinant NDUFB6 has been used in the development of diagnostic tests for the detection of complex I deficiencies in patients.

Conclusion

In summary, Recombinant Human NDUFB6 Protein is an essential component of the respiratory chain complex I, playing a crucial role in the transfer of electrons and the production of ATP. Its structure, activity, and applications make it a valuable tool for research and potential therapeutic target for various diseases. Further studies on the function and regulation of NDUFB6 may lead to a better understanding of complex I-related disorders and the development of new treatments.

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