Product Name: ATP5H Antibody
Species Reactivity: Human
Tested Applications: IHC-P, WB
Applications: For IHC-P starting dilution is: 1:50~100For FACS starting dilution is: 1:10~50For WB starting dilution is: 1:1000
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 18 kDa
Immunogen: This ATP5H antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 68-97 amino acids from the Central region of human ATP5H.
Host Species: Rabbit
Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.
Physical State: Liquid
CAS NO.: 1338545-07-5
Product: OTS-964
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration:
Storage Conditions: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: ATP synthase subunit d, mitochondrial, ATPase subunit d, ATP5H
Accession NO.: O75947
Protein Ino:
Official Symbol: ATP5H
Geneid: 10476
Background: Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the d subunit of the Fo complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. In addition, three pseudogenes are located on chromosomes 9, 12 and 15.
PubMed ID:http://aac.asm.org/content/53/8/3190.abstract
