Anti-ATM

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Ataxia telangiectasia mutated,also known as TEL1 or TELO1, is a serine/threonine protein kinase that is recruited and activated by DNA double-strand breaks. The protein is a member of the phosphatidylinositol 3-kinase family of proteins that respond to DNA damage by phosphorylating key substrates involved in DNA repair and/or cell cycle control. Linkage analysis of ataxia-telangiectasia led to mapping of the gene to chromosome 11q22.3. Using an antiserum developed to a peptide corresponding to the deduced amino acid sequence of ATM, the protein is a single, high molecular weight protein predominantly confined to the nucleus of human fibroblasts, although it is present in both nuclear and microsomal fractions from human lymphoblast cells and peripheral blood lymphocytes. Overexpression of ATM cDNA in AT cells enhanced their survival after radiation exposure, decreased radiation-induced chromosome aberrations, reduced radioresistant DNA synthesis, and partially corrected defective cell cycle checkpoints and induction of stress-activated protein kinase. ATM has an essential role in the reconstitutive capacity of hematopoietic stem cells but is not as important for the proliferation or differentiation of progenitors, in a telomere-independent manner. It functions directly in the repair of chromosomal DNA double-stranded breaks by maintaining DNA ends in repair complexes generated during lymphocyte gene assembly. Protein function: Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]- Q. Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed:9843217, PubMed:9733515, PubMed:10550055, PubMed:10766245, PubMed:10839545, PubMed:10910365, PubMed:10802669, PubMed:10973490, PubMed:11375976, PubMed:12086603, PubMed:15456891, PubMed:19965871, PubMed:30612738, PubMed:30886146). May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response. Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878). [The UniProt Consortium]