SOMAmer® anti‐ATP synthase subunit beta, mitochondrial Reagent DESCRIPTION
SOMAmer Reagent No. Protein Target Target UniProt ID Species Reactivity 5’ Functional Mod. Target Source Formulation
B‐4965‐27_1 ATP synthase subunit beta, mitochondrial P06576 Human Biotinylated Synthetic Oligonucleotide Poly‐His tagged Buffered SOMAmer reagent delivered at 10 μM in 5 mM HEPES, 1 mM EDTA, pH 8 ACTIVITY SOMAmer reagents have been qualified for target affinity capture in conjunction with numerous downstream applications. Specific protocols should be determined for the intended use. General application notes are available on our website (http://www.somalogic.com/resources/app-notes/). Specificity No closely related human proteins were available for specificity testing. Affinity The Kd for ATP synthase subunit beta, mitochondrial binding to the SOMAmer reagent, measured by Zorbax Affinity method, is typically 5 x 10-9 M. See Certificate of Analysis for details. HANDLING and STORAGE
Handling Shipping Stability & Storage Heat/cool treatment on material ready for use (not stocks) is recommended (e.g. heat the reagent to 95 °C for 5 minutes, then cool to assay temperature). The product is shipped frozen. Upon receipt, store it immediately at the temperature recommended below. For long term use, aliquotting is recommended to avoid freeze‐thaw cycles.  2 years from date of receipt at ‐20 °C to ‐70 °C, as supplied
 3 months at 4 °C
TARGET 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. (Source: The UniProt Consortium, Activities at the Universal Protein Resource (UniProt), Nucleic Acids Res. 42: D191‐
D198 (2014).) SomaLogic, Inc. • 2945 Wilderness Place Boulder, CO 80301 • www.somalogic.com Technical Support 800‐324‐0783 • Main Number 303‐625‐9000 570‐00006, Rev 0, DCN 16‐083
Effective Date: 4/19/2016  2015 SomaLogic, Inc. 1 of 1