Alternative Name(s):

Gastric H(+)/K(+) ATPase subunit beta Proton pump beta chain

Species: (Organism)

Homo sapiens (Human)

Gene Names:

ATP4B

Tag info:

Tag-Free

Target Protein AA Sequence:

CLYVLMQTVDPYTPDYQDQLRSPGVTLRPDVYGEKGLEIVYNVSDNRTWADLTQTLHAFLAGYSPAAQEDSINCTSEQYFFQESFRAPNHTKFSCKFTADMLQNCSGLADPNFGFEEGKPCFIIKMNRIVKFLPSNGSAPRVDCAFLDQPRELGQPLQVKYYPPNGTFSLHYFPYYGKKAQPHYSNPLVAAKLLNIPRNAEVAIVCKVMAEHVTFNNPHDPYEGKVEFKLKIEK

Expression Region:

58-291aa

Subcellular Location:

Cell membrane, Single-pass type II membrane protein

Tissue Specificity:

Protein Length:

Extracellular Domain

Pathway:

OxidativePhosphorylation

Mol. Weight:

26.6 kDa

Purity:

Greater than 85% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Signal Transduction

Function:

Required for stabilization and maturation of the catalytic proton pump alpha subunit and may also involved in cell adhesion and establishing epithelial cell polarity.

Involvement in disease:

Relevance:

Required for stabilization and maturation of the catalytic proton pump alpha subunit and may also involved in cell adhesion and establishing epithelial cell polarity.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

X(+)/potassium ATPases subunit beta family

Reference:

"A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase resembles cell adhesion molecules." Bab-Dinitz E., Albeck S., Peleg Y., Brumfeld V., Gottschalk K.E., Karlish S.J. Biochemistry 48:8684-8691(2009)