ATP synthase subunit beta, mitochondrial (Atp5b), mouse, recombinant

Organism: Mus musculus (Mouse). Source: E.coli. Expression Region: 47-529aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: AAQASAAPKA GTATGRIVAV IGAVVDVQFD EGLPPILNAL EVQGRDSRLV LEVAQHLGES TVRTIAMDGT EGLVRGQKVL DSGAPIKIPV GPETLGRIMN VIGEPIDERG PIKTKQFAPI HAEAPEFIEM SVEQEILVTG IKVVDLLAPY AKGGKIGLFG GAGVGKTVLI MELINNVAKA HGGYSVFAGV GERTREGNDL YHEMIESGVI NLKDATSKVA LVYGQMNEPP GARARVALTG LTVAEYFRDQ EGQDVLLFID NIFRFTQAGS EVSALLGRIP SAVGYQPTLA TDMGTMQERI TTTKKGSITS VQAIYVPADD LTDPAPATTF AHLDATTVLS RAIAELGIYP AVDPLDSTSR IMDPNIVGNE HYDVARGVQK ILQDYKSLQD IIAILGMDEL SEEDKLTVSR ARKIQRFLSQ PFQVAEVFTG HMGKLVPLKE TIKGFQQILA GEYDHLPEQA FYMVGPIEEA VAKADKLAEE HGS. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. 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. 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 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. 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. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Mitochondrial mbrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the mbrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extrambraneous catalytic core, and F0 - containing the mbrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Reference: Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.