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ATP5D, Recombinant, Human, aa23-168, His-tag (ATP Synthase Subunit delta, Mitochondrial, F-ATPase delta Subunit)

Cat no: A4000-46C

ATP5D, Recombinant, Human, aa23-168, His-tag (ATP Synthase Subunit delta, Mitochondrial, F-ATPase delta Subunit)

ATP5D, also known as F-ATPase delta subunit, catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This protein is the delta subunit of the catalytic core. Alternatively spliced transcript variants encoding the same isoform have been identified. Purified by using conventional chromatography.\n\nSource:\nRecombinant corresponding to aa23-168 of human ATP5D, fused to His-tag at N-terminus, expressed in E.coli.\n\nAA Sequence:\nMGSSHHHHHH SSGLVPRGSH MAEAAAAPAA ASGPNQMSFT FASPTQVFFN GANVRQVDVP TLTGAFGILA AHVPTLQVLR PGLVVVHAED GTTSKYFVSS GSIAVNADSS VQLLAEEAVT LDMLDLGAAK ANLEKAQAEL VGTADEATRA EIQIRIEANE ALVKALE \n\nMolecular Weight: \n~17.3kD (167aa), confirmed by MALDI-TOF\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

A4000-46C

Size

10ug

Form

Supplied as a liquid in 20mM Tris-HCl buffer, pH8, 0.1M sodium chloride, 20% glycerol.

Purity

~95% (SDS-PAGE)

References

Jordan E.M., et al. (1992) Biochim. Biophys. Acta 1130:123-126 Grimwood J., et al. (2004) Nature. 428:529-535.

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