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Antibodies
Anti-ATP5L2 Antibody
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产品名称:
Anti-ATP5L2 Antibody
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简单介绍
Anti-ATP5L2
Antibody
Anti-ATP5L2 Antibody
的详细介绍
Overview
Name:
Anti-ATP5L2
Antibody
See all ATP5L2 primary antibodies
Description:
Rabbit polyclonal antibody to ATP5L2
Specificity:
The antibody detects endogenous levels of total ATP5L2 protein.
Applications:
WB, IF
Reactivity:
Human
Immunogen:
Synthesized peptide derived from internal of human ATP5L2.
Host:
Rabbit
Clonality:
Polyclonal
Conjugate:
Unconjugated
Purification:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration:
1.0mg / ml
Formulation:
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Storage:
Store at -20˚C
Target
Function:
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(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Sequence Similarities:
Belongs to the ATPase g subunit family.
Cellular Location:
Mitochondrion membrane.
Database Links:
Entrez Gene: 10632 Human
Entrez Gene: 267020 Human
SwissProt: O75964 Human
SwissProt: Q7Z4Y8 Human
Synonyms:
ATP synthase subunit g 2, mitochondrial Antibody
ATP synthase subunit g, mitochondrial Antibody
ATP5K2 Antibody
ATP5L Antibody
ATP5L2 Antibody
ATP5L2 + ATP5L [EPR15636] Antibody
ATPase subunit g Antibody
ATPase subunit g 2 Antibody
Information:
Target information shown above is from the UniProt Consortium.
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