ATP Synthase Subunit Gamma, Mitochondrial (ATP5F1C) Peptide

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Description
ATP Synthase Subunit Gamma, Mitochondrial (ATP5F1C) Peptide is a synthetic peptide.
Documents del producto
Product specifications
Category | Proteins and Peptides |
Immunogen Target | ATP Synthase Subunit Gamma, Mitochondrial (ATP5F1C) |
Host | Synthetic |
Recommended Dilution | BL (predicted): 0.5 mg/ml. Optimal dilutions/concentrations should be determined by the end user. |
Conjugation | Unconjugated |
Observed MW | Sequence Fragment: C-Terminus: C-TLTFNRTRQAVITKE |
Size 1 | 100 µg |
Form | Lyophilized Reconstitute in deionized water. |
Tested Applications | P-ELISA |
Buffer | Prior to lyophilization: Deionized water. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
Gene ID | 509, 11949, 116550 |
NCBI Accession | NP_005165.1, NP_001001973.1 |
Background | Protein ATP5F1C |
Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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ATP5F1C antibody
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 the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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.
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ATP5F1C antibody
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 the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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.
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