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ATP4B Protein, Human, Recombinant (GST)

Catalog No. TMPH-01893
Synonyms: Proton pump beta chain, Gastric H(+)/K(+) ATPase subunit beta, ATP4B, Potassium-transporting ATPase subunit beta

The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump. Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle.

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ATP4B Protein, Human, Recombinant (GST)
Pack Size Availability Price/USD Quantity
20 μg 20 days $ 198.00
100 μg 20 days $ 389.00
1 mg 20 days $ 1,680.00
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Biological Description
Technical Params
Product Properties
Description The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump. Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle.
Species Human
Expression System E. coli
Tag N-terminal GST-tagged
Accession Number P51164
Synonyms Proton pump beta chain, Gastric H(+)/K(+) ATPase subunit beta, ATP4B, Potassium-transporting ATPase subunit beta
Amino Acid CLYVLMQTVDPYTPDYQDQLRSPGVTLRPDVYGEKGLEIVYNVSDNRTWADLTQTLHAFLAGYSPAAQEDSINCTSEQYFFQESFRAPNHTKFSCKFTADMLQNCSGLADPNFGFEEGKPCFIIKMNRIVKFLPSNGSAPRVDCAFLDQPRELGQPLQVKYYPPNGTFSLHYFPYYGKKAQPHYSNPLVAAKLLNIPRNAEVAIVCKVMAEHVTFNNPHDPYEGKVEFKLKIEK Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Construction 58-291
Protein Purity > 90% as determined by SDS-PAGE.
Molecular Weight 53.6 kDa (predicted)
Formulation Tris-based buffer,50% glycerol
Reconstitution A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage

Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shipping

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Research Background The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump. Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle.

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Keywords

ATP4B Protein, Human, Recombinant (GST) Proton pump beta chain Gastric H(+)/K(+) ATPase subunit beta ATP4B Potassium-transporting ATPase subunit beta recombinant recombinant-proteins proteins protein

 

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