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ATPase | ATP synthase, whole enzyme

345 €

AS08 370  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: C. reinhardtii, E. opiuroides, S. oleracea, P. sativum, P. vaginatum

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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

Host Rabbit
Clonality Polyclonal
Clone
Purity Serum
Format Lyophilized
Quantity 100 ĩl
Reconstitution For reconstitution add 50 ĩl of sterile water. To get the best possible dissolution please keep it at +4°C 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

AS12 1853 | anti-ATP synthase subunit c antibody

Plant and algal protein extraction buffer

Secondary antibodies

Additional information
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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