Where to get ATM (phospho-Ser1981) Polyclonal Antibody?

Ataxia telangiectasia mutated (ATM) is a serine/threonine protein kinase that is recruited and activated by DNA double-strand breaks. It phosphorylates several key proteins that admit activation of the DNA accident checkpoint, arch to corpuscle aeon arrest, DNA adjustment or apoptosis. Several of these targets, including p53, CHK2 and H2AX are bump suppressors.
The protein is alleged for the ataxia Ataxia telangiectasia acquired by mutations of ATM.
The ATM gene codes for a 350 kDa protein consisting of 3056 amino acids. ATM belongs to the superfamily of Phosphatidylinositol 3-kinase-related kinases (PIKKs). The PIKK superfamily comprises six Ser/Thr-protein kinases that appearance a arrangement affinity to phosphatidylinositol 3-kinases (PI3Ks). This protein kinase ancestors includes amidst others ATR (ATM- and RAD3-related), DNA-PKcs (DNA-dependent protein kinase catalytic subunit) and mTOR (mammalian ambition of rapamycin). Characteristic for ATM are 5 domains. These are from N-Terminus to C-Terminus the HEAT echo domain, the FRAP-ATM-TRRAP (FAT) domain, the kinase area (KD), the PIKK-regulatory area (PRD) and the FAT-C-terminal (FATC) domain. The HEAT repeats anon bind to the C-terminus of NBS1. The FAT area interacts with ATM's kinase area to balance the C-terminus arena of ATM itself. The KD area resumes kinase activity, while the PRD and the FATC area adapt it. Although no anatomy for ATM has been solved, the all-embracing appearance of ATM is actual agnate to DNA-PKcs and is composed of a arch and a continued arm that is anticipation to blanket about double-stranded DNA afterwards a conformational change. The absolute N-terminal area calm with the FAT area are predicted to adobt an α-helical structure, which was begin by arrangement analysis. This α-helical anatomy is believed to anatomy a tertiary structure, which has a curved, tubular appearance present for archetype in the Huntingtin protein, which aswell contains HEAT repeats. FATC is the C-terminal area with a breadth of about 30 amino acids. It is awful conserved and consists of an α-helix followed by a aciculate turn, which is counterbalanced by a disulfide bond.
Function
A trimeric circuitous of the three proteins Mre11, RAD50 and NBS1 (Xrs2 in yeast), alleged the MRN circuitous in humans, recruits ATM to bifold fiber break (DSBs) and holds the two ends together. ATM anon interacts with the NBS1 subunit and phosphorylates the histone alternative H2AX on Ser139.This phosphorylation generates bounden sites for adaptor proteins with a BRCT domain. These adaptor proteins again recruit altered factors including the effector protein kinase CHK2 and the bump suppressor p53. The ATM-mediated DNA accident acknowledgment consists of a accelerated and a delayed response. The effector kinase CHK2 is phopsphorylated and thereby activated by ATM. Activated CHK2 phophorylates phosphatase CDC25A which is base thereupon and can no best dephosphororylate CDK2-Cyclin consistent in cell-cycle arrest. If the DSB can not be repaired during this accelerated response, ATM additionally phophorylates MDM2 and p53 at Ser15. p53 is aswell phosphorylated by the effector kinase CHK2. These phosphorylation contest advance to stabilization and activation of p53 and consecutive archetype of abundant p53 ambition genes including Cdk inhibitor p21 which advance to abiding cell-cycle arrest or even apoptosis.
More about: ATM (phospho-Ser1981) Polyclonal Antibody sale
Read more: phospho antibody