Anti-NDUFB10 antibody [EPR16230]
- RabMAb
- Recombinant
- What is this?
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(2 Publications)
Rabbit Recombinant Monoclonal NDUFB10 antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 2 publications.
View Alternative Names
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10, Complex I-PDSW, NADH-ubiquinone oxidoreductase PDSW subunit, CI-PDSW, NDUFB10
- ICC/IF
Supplier Data
Immunocytochemistry/ Immunofluorescence - Anti-NDUFB10 antibody [EPR16230] (AB192245)
Immunofluorescent analysis of 4% paraformaldehyde-fixed 0.1% tritonX-100 permeabilized HeLa cells labeling NDUFB10 with ab192245 at 1/50 dilution ( 6 μg/ml) followed by Goat anti rabbit IgG (Alexa Fluor® 555) secondary antibody (ab150078) at 1/500 dilution. Nuclear counter stain Dapi (blue).
The two negative controls are ab192245 at 1/50 dilution followed by (Goat anti mouse IgG (Alexa Fluor®488) secondary antibody at 1/200 dilution.
- WB
Supplier Data
Western blot - Anti-NDUFB10 antibody [EPR16230] (AB192245)
Blocking/Dilution buffer : 5% NFDM /TBST.
All lanes:
Western blot - Anti-NDUFB10 antibody [EPR16230] (ab192245) at 1/5000 dilution
Lane 1:
HeLa cell lysate at 20 µg
Lane 2:
HepG2 cell lysate at 20 µg
Lane 3:
Jurkat cell lysate at 20 µg
Lane 4:
Human fetal kidney lysate at 20 µg
Secondary
All lanes:
Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/1000 dilution
Predicted band size: 21 kDa
Observed band size: 21 kDa
false
Related conjugates and formulations (1)
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Anti-NDUFB10 antibody [EPR16230] - BSA and Azide free
Reactivity data
Product details
Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free batch production
For more information, read more on recombinant antibodies.
Properties and storage information
Form
Purification technique
Storage buffer
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
NDUFB10 plays a significant role in cellular energy production by being a subunit of complex I in the mitochondrial electron transport chain. As part of this large enzyme complex NDUFB10 contributes to the overall stability and function of complex I facilitating ATP production by driving the conversion of energy derived from nutrients into a usable form. Its presence in the mitochondrial inner membrane highlights its essential role in maintaining efficient energy metabolism and cellular respiration.
Pathways
The electron transport chain pathway incorporates NDUFB10 as a vital component. This pathway plays a major role in oxidative phosphorylation where NDUFB10 interacts closely with other mitochondrial proteins like NDUFS1 and NDUFA1 within complex I. Besides serving in ATP synthesis these interactions help in maintaining overall cellular bioenergetics and proper mitochondrial function demonstrating the integrated role NDUFB10 plays alongside other proteins in energy metabolism.
Product protocols
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Target data
Publications (2)
Recent publications for all applications. Explore the full list and refine your search
The Journal of neuroscience : the official journal of the Society for Neuroscience 41:3331-3343 PubMed33707295
2021
Applications
Unspecified application
Species
Unspecified reactive species
EMBO reports 21:e48833 PubMed31721420
2019
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
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