Product Name: Abltide [KKGEAIYAAPFA-NH2]
Sequence One Letter Code: KKGEAIYAAPFA-NH2
Sequence Three Letter Code: Lys-Lys-Gly-Glu-Ala-Ile-Tyr-Ala-Ala-Pro-Phe-Ala-NH2
Chemical Formula:C60H93N15O15
Molecular Weight: 1264.6
Purity: 95%
Form: Lyophilized
Storage Conditions: - 20 °C
Research Area: peptide substrate
Conjugation: Unconjugated
Code Nacres: NA.26
Application: Abltide is a well-characterized synthetic peptide substrate for the Abl family of protein tyrosine kinases. It is widely used in biochemical kinase assays and phosphorylation studies to measure Abl kinase activity and signaling dynamics. Abl kinases regulate key cellular processes including cytoskeletal organization, cell growth, and stress responses, and are particularly important in oncogenic signaling driven by the BCR-Abl fusion protein in chronic myeloid leukemia. Because of its efficient phosphorylation and reproducible performance, Abltide provides a reliable substrate for evaluating kinase activity and inhibitor potency. The peptide is commonly applied in Western blot–based phosphorylation assays, enzymatic activity measurements, and high-throughput screening workflows. It supports cancer research, kinase inhibitor discovery, and mechanistic studies investigating tyrosine kinase regulation and oncogenic transformation.
Current Research: Introduction to Abl Kinase Research Protein tyrosine kinases are critical regulators of cellular signaling pathways that control growth, differentiation, survival, and stress responses. Among these enzymes, the Abl family of tyrosine kinases plays a significant role in coordinating cytoskeletal organization, DNA damage responses, and intracellular signaling networks. Dysregulation of Abl kinase activity is strongly associated with oncogenic transformation, particularly in hematological malignancies such as chronic myeloid leukemia (CML). To investigate Abl kinase activity and identify therapeutic inhibitors, researchers rely on well-defined peptide substrates that enable accurate measurement of phosphorylation events. Abltide is one of the most widely used synthetic peptide substrates developed specifically for studying the catalytic activity of Abl tyrosine kinases. Abltide as a Synthetic Substrate for Abl Kinases Abltide is a synthetic peptide designed to serve as an efficient phosphorylation substrate for the Abl family kinases, including c-Abl and the oncogenic BCR-Abl fusion protein. The peptide sequence contains a tyrosine residue embedded within a recognition motif that is preferentially phosphorylated by Abl kinases. Because of its optimized sequence and strong compatibility with Abl catalytic domains, Abltide exhibits high phosphorylation efficiency and consistent performance in biochemical assays. This makes it particularly suitable for quantitative measurements of kinase activity in vitro. Unlike complex protein substrates, synthetic peptides such as Abltide provide a simplified system that reduces experimental variability. Researchers can therefore directly evaluate the catalytic function of Abl kinases and monitor phosphorylation kinetics with greater precision. Role of Abl Kinases in Cancer Signaling Abl kinases are involved in a wide range of cellular processes, including regulation of the actin cytoskeleton, cell adhesion, and responses to cellular stress. Under normal physiological conditions, these kinases participate in controlled signaling networks that maintain cellular homeostasis. However, in certain cancers the Abl kinase pathway becomes dysregulated. A well-known example is the BCR-Abl fusion protein, which arises from a chromosomal translocation known as the Philadelphia chromosome. This fusion protein possesses constitutive tyrosine kinase activity that continuously activates downstream signaling pathways, driving uncontrolled cell proliferation and survival in leukemia cells. Because BCR-Abl is a central driver of chronic myeloid leukemia, it has become a major therapeutic target. Many approved targeted therapies, including tyrosine kinase inhibitors, function by suppressing the abnormal activity of this oncogenic kinase. Applications in Kinase Activity and Phosphorylation Assays Abltide is widely used in biochemical kinase assays designed to measure the catalytic activity of Abl family kinases. In these assays, the peptide serves as a substrate that becomes phosphorylated on its tyrosine residue in the presence of active kinase. The phosphorylation reaction can be detected using multiple analytical techniques. For example, researchers may measure phosphorylation using antibody-based detection methods, including Western blot–based phosphotyrosine analysis. These methods allow scientists to quantify phosphorylation levels and evaluate how different experimental conditions influence kinase activity. Because Abltide produces consistent and reproducible phosphorylation signals, it is particularly useful for studying kinase kinetics, substrate specificity, and regulatory mechanisms associated with Abl signaling pathways. Inhibitor Screening and Drug Discovery Another important application of Abltide is in kinase inhibitor screening. Drug discovery programs targeting Abl kinases often rely on peptide substrates that provide reliable readouts of enzymatic activity. In such assays, the kinase is incubated with Abltide in the presence or absence of potential inhibitor compounds. If a compound effectively blocks Abl kinase activity, phosphorylation of the peptide substrate decreases. Measuring this change allows researchers to determine inhibitor potency and evaluate candidate molecules during early-stage drug development. Because peptide-based assays can be adapted to multi-well formats, Abltide is frequently incorporated into high-throughput screening workflows used to test large compound libraries. This approach accelerates the identification of molecules capable of suppressing oncogenic kinase signaling. Supporting Mechanistic Studies of Tyrosine Kinase Regulation Beyond inhibitor discovery, Abltide is also valuable for mechanistic studies investigating tyrosine kinase regulation. Researchers use this peptide to explore how Abl kinases are activated, how they interact with regulatory proteins, and how phosphorylation events influence downstream signaling. By monitoring Abl-mediated phosphorylation in controlled experimental systems, scientists can better understand how kinase activity contributes to cytoskeletal remodeling, cell migration, and cellular stress responses. These insights are particularly relevant in studies examining how abnormal kinase signaling leads to oncogenic transformation. Conclusion Abltide is a well-established synthetic peptide substrate for the Abl family of protein tyrosine kinases and serves as a reliable reagent for measuring kinase activity. Its efficient phosphorylation and reproducible performance make it highly suitable for biochemical assays, phosphorylation studies, and inhibitor screening experiments. Through its applications in Western blot–based assays, enzymatic activity measurements, and high-throughput screening platforms, Abltide supports a wide range of research areas. These include cancer biology, kinase inhibitor discovery, and investigations into the molecular mechanisms governing tyrosine kinase signaling and oncogenic transformation.
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