|Application ||WB, IHC|
|Calculated MW||350687 Da|
|Other Names||Serine-protein kinase ATM, Ataxia telangiectasia mutated, A-T mutated, ATM|
|Target/Specificity||A synthetic peptide corresponding to residues surrounding serine 1981 of human ATM was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||ATM Antibody Phospho (pS1981) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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/H2AFX 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, RAD9 and DCLRE1C. 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.|
|Cellular Location||Nucleus. Cytoplasmic vesicle. Note=Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin|
|Tissue Location||Found in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain, heart, spleen, thymus, testis, ovary, small intestine, colon and leukocytes|
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ATM is a nuclear phosphoprotein involved in Ataxia-telangiectasia (A-T) an autosomal recessive disorder characterized by cerebellar ataxia, immune deficiencies, increased cancer predisposition, chromosomal instability and radiation sensitivity (1-2). This large protein (370 kDa) is involved in genome stability, cellular responses to DNA damage and cell cycle control. Autophosphorylation at serine 1981 on ATM is required during ATM kinase activation initiated by double strand breaks in the genome. After serine 1981 autophosphorylation, ATM phosphorylates downstream proteins (e.g. p53, Chk2), leading to cell cycle arrest and DNA repair (3). More than 100 mutations have been identified so far and are expected to inactivate the ATM protein by truncation or large deletions (4). Defects in ATM contribute to various B-cell and T-cell leukemias (5).
1. Harnden, D.G.; Int. J. Radiat. Biol. 66:S13-S19, 1994.
2. Lavin MF, Shiloh,Y. Ann. Rev. Imm. 15:177-202, 1997
3. Goldstine JV, et al. DNA Repair, 5:432-443, 2006.
4. Savitsky K et al. Hum. Mol. Gen. 4:2025-2032, 1995.
5. Stankovic T.et al. Lancet 353:26-29., 1999.
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