Gene ID Number
1ug per 1ul
Human, Mouse, Rat
ALEXA FLUOR® 488
Purified by Protein A.
Conjugated Primary Antibodies
Rabbit (Oryctolagus cuniculus)
Anti-ATP5G2 PAb ALEXA FLUOR 488
This is a highly specific antibody against ATP5G2.
ATP5G2 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated
Due to limited amount of testing and knowledge, not every possible cross-reactivity is known.
This antibody was obtained by immunization of the host with KLH conjugated synthetic peptide derived from human ATP5G2
Store this antibody in aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Keep refrigerated at 2 to 8 degrees Celcius for up to one year.
ATP5A; ATP synthase F(0) complex subunit C2, mitochondrial; ATP synthase lipid-binding protein; ATP synthase proteolipid P2; ATP synthase proton-transporting mitochondrial F(0) complex subunit C2; ATPase protein 9; ATPase subunit c; ATP5G2; PSEC0033
For facs or microscopy Alexa 1 conjugate.Alexa Fluor 488 has the same range to that of fluorescein isothiocyanate (FITC), yet the Anti-ATP5G2 has a very high photo stability. As a result of this photo stability, it has turned into an antibody for fluorescent microscopy and FACS FLOW cytometry. It is distinguished in the FL1 of a FACS-Calibur or FACScan. Also Alexa Fluor 488 is pH stable.If you buy Antibodies supplied by Bioss Primary Conjugated Antibodies. ALEXA FLUOR they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.
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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.