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ATPase | ATP synthase, whole enzyme

320 €

AS08 370  |  clonality: polyclonal  |  host: rabbit  |  reactivity: Ch. reinhardtii, E. opiuroides, S. oleracea, P.sativum, P.vaginatum, Ch. reinhardtii

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AS08 370

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product information
background  

ATP synthase produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have two components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.

immunogen  

purified native protein from spinach

antibody format  

rabbit;

polyclonal;

serum;

lyophilized

quantity  

100 µl

- for reconstitution add 100 µl of sterile water

To get the best possible dissolution please keep it at +4° ON.

storage  

store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

tested applications  

Western blot (WB)

related products  

AS08 304 | anti-ATP synthase subunit alpha antibody

AS03 030 | anti-ATP synthase subunit beta hen antibody

AS08 312 | anti-ATP synthase subunit gamma antibody

AS05 071 | anti-ATP synthase subunit c antibody

additional information  

to be added when available

application information
recommended dilution  

1: 10 000 (WB)

expected | apparent MW  

38-58 kDa

confirmed reactivity  

subunits alpha, beta, gamma, epsilon of Ch. reinhardtii, S. oleracea, P.sativum, perennial grasses: Eremochloa ophiuriudes, Paspalum vaginatum

predicted reactivity  

n. a.

not reactive in  

no confirmed exceptions from predicted reactivity known in the moment

additional information  

the prominent reaction is to a doublet around 55-58 kDa which is alpha and beta and weaker reaction to gamma subunit which is around 38 kDa

selected references  

Liu et al. (2011). Identification of differentially expressed salt-responsive proteins in roots of two perennial grass species contrasting in salinity tolerance. J Plant Physiol. Nov 7

 



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