ATP5EP2 antibody (AA 19-52)
ATP5EP2
Reactivity: Human
WB
Host: Rabbit
Polyclonal
RB53889
unconjugated
1 image
-
- Target
- ATP5EP2 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, epsilon Subunit Pseudogene 2 (ATP5EP2))
- Binding Specificity
- AA 19-52
- Reactivity
- Human
- Host
- Rabbit
- Clonality
- Polyclonal
- Application
- Western Blotting (WB)
- Purification
- This antibody is purified through a protein A column, followed by peptide affinity purification.
- Immunogen
- This ATP5EP2 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 19-52 amino acids from the Central region of human ATP5EP2.
- Clone
- RB53889
- Isotype
- Ig Fraction
-
- Application Notes
- WB: 1:2000
- Restrictions
- For Research Use only
-
- Format
- Liquid
- Buffer
- Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
- Preservative
- Sodium azide
- Precaution of Use
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Storage
- 4 °C,-20 °C
- Expiry Date
- 6 months
-
- Target
- ATP5EP2 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, epsilon Subunit Pseudogene 2 (ATP5EP2))
- Alternative Name
- ATP5EP2
- Synonyms
- ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit pseudogene 2 antibody, ATP5EP2 antibody
- Background
- Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity).
- Molecular Weight
- 5807
- UniProt
- Q5VTU8
-
You are here:
