Recombinant Human NDUFB9 protein (denatured) is a Human Full Length protein, in the 1 to 179 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
Amino acid sequence
M G S S H H H H H H S S G L V P R G S H M G S M A F L A S G P Y L T H Q Q K V L R L Y K R A L R H L E S W C V Q R D K Y R Y F A C L M R A R F E E H K N E K D M A K A T Q L L K E A E E E F W Y R Q H P Q P Y I F P D S P G G T S Y E R Y D C Y K V P E W C L D D W H P S E K A M Y P D Y F A K R E Q W K K L R R E S W E R E V K Q L Q E E T P P G G P L T E A L P P A R K E G D L P P L W W Y I V T R P R E R P M
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Alternative names
LYRM3, UQOR22, NDUFB9, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9, Complex I-B22, LYR motif-containing protein 3, NADH-ubiquinone oxidoreductase B22 subunit, CI-B22
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Recombinant Human NDUFB9 protein (denatured) is a Human Full Length protein, in the 1 to 179 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- Q9Y6M9-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl
Sequence info
Amino acid sequence
- M G S S H H H H H H S S G L V P R G S H M G S M A F L A S G P Y L T H Q Q K V L R L Y K R A L R H L E S W C V Q R D K Y R Y F A C L M R A R F E E H K N E K D M A K A T Q L L K E A E E E F W Y R Q H P Q P Y I F P D S P G G T S Y E R Y D C Y K V P E W C L D D W H P S E K A M Y P D Y F A K R E Q W K K L R R E S W E R E V K Q L Q E E T P P G G P L T E A L P P A R K E G D L P P L W W Y I V T R P R E R P M
- Accession
- Q9Y6M9
- Protein length
- Full Length
- Predicted molecular weight
- 24.2 kDa
- Amino acids
- 1 to 179
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Liquid
General info
- Function
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
- Sequence similarities
Belongs to the complex I LYR family.
- Subcellular localisation
- Mitochondrion inner membrane
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage conditions
- -20°C
- Appropriate long-term storage conditions
- -20°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
The protein NDUFB9 also known as NADH:ubiquinone oxidoreductase subunit B9 is a part of the mitochondrial respiratory chain. This protein has a molecular mass of approximately 22 kDa. NDUFB9 is expressed in the mitochondria of many tissues serving as an accessory subunit of complex I the first enzyme in the electron transport chain. It does not participate in catalysis but assists in maintaining the integrity and stability of the complex.
- Biological function summary
NDUFB9 plays a role in mitochondrial energy production. As a component of complex I which is the largest of the five mitochondrial complexes NDUFB9 contributes to the process of oxidative phosphorylation. This complex transfers electrons from NADH to ubiquinone facilitating the pumping of protons across the inner mitochondrial membrane. This proton gradient drives ATP production vital for energy metabolism in cells.
- Pathways
The function of NDUFB9 is critical in cellular respiration and energy production pathways. It is integral to the pathway of oxidative phosphorylation closely associated with aerobic energy metabolism. Through its role in complex I NDUFB9 interacts with other mitochondrial proteins such as NDUFA1 and NDUFS1 which are also part of the same complex and contribute to electron transport and energy conservation.
- Associated diseases and disorders
NDUFB9 mutations have been linked to mitochondrial disorders including Leigh syndrome a severe neurological disorder characterized by progressive loss of mental and movement abilities. NDUFB9 dysfunction can also contribute to Complex I deficiency which leads to a range of metabolic syndromes. This protein's interaction with other complex I proteins like NDUFS2 is important for maintaining proper mitochondrial function and disturbances can lead to broader mitochondrial pathologies.
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1 product image
SDS-PAGE - Recombinant Human NDUFB9 protein (denatured) (ab171600)
15% SDS-PAGE analysis of 3µg ab171600.
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