Product Pathways - Motif Antibodies
PTMScan® Phospho-AMPK Substrate Motif (LXRXXS*/T*) Immunoaffinity Beads
|Consenus Site||Cell or Tissue Type||Study No.||Modified Peptides Identified|
|(L/M)XRXX(S*/T*), RXX(S*/T*)||Human non-small cell lung cancer (H1650) cell line||157 PDF|
This product is not for individual sale. It is only available as a component of the PTMScan® Proteomics System. PTMScan® Proteomics System orders must be priced out individually. Please email us at email@example.com to receive the most accurate pricing.
PTMScan® Immunoaffinity Beads are custom preparations of motif antibodies coupled to protein A beads. They are intended only for use for PTMScan® and are available as components of the PTMScan® Proteomics System.
Specificity / Sensitivity
PTMScan® AMPK Substrate Motif (LXRXXS*/T*) (D72H3G8/D78G9) Immunoaffinity Beads detect and capture endogenous levels of peptide derived from protease digested cellular proteins containing phospho-Ser/Thr preceded by Arg at positions -3 and Leu at positon -5; It also cross reacts with proteins and peptides that only harbor RXXS*/T* motif. (U.S. Patent No's.: 6,441,140; 6,982,318; 7,259,022; 7,344,714; U.S.S.N. 11,484,485; and all foreign equivalents.)
AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).
AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1), through phosphorylating many of its substrates. AMPK phosphorylates consensus motif (L/M)XRXX(s/t)XXXL (8). Antibody recognizing LXRXX(s/t) motif is very useful to identify AMPK substrate since many of them are still unknown.
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For Research Use Only. Not For Use In Diagnostic Procedures.