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AB131739

Recombinant Human ATM protein (GST tag N-Terminus)

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Recombinant Human ATM protein (GST tag N-Terminus) is a Human Fragment protein, in the 1 to 138 aa range, expressed in Wheat germ, with >80%, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

Serine-protein kinase ATM, Ataxia telangiectasia mutated, A-T mutated, ATM

1 Images
SDS-PAGE - Recombinant Human ATM protein (GST tag N-Terminus) (AB131739)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human ATM protein (GST tag N-Terminus) (AB131739)

12.5% SDS-PAGE using ab131739 stained with Coomassie Blue.

Key facts

Purity

>80%

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

WB, ELISA, SDS-PAGE

applications

Biologically active

No

Accession

Q13315

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MTLHEPANSSASQSTDLCDFSGDLDPAPNPPHFPSHVVKATFAYISNCHKTKLKSILEILSKSPDSYQKILLAICEQAAETNNVYKKHRILKIYHLFVSLLLKDIKSGLGGAWAFVLRDVIYTLIHYINQRKLTIFSQ","proteinLength":"Fragment","predictedMolecularWeight":"40.81 kDa","actualMolecularWeight":null,"aminoAcidEnd":138,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q13315","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ATM also known as Ataxia Telangiectasia Mutated is a protein kinase with a molecular weight of approximately 370 kDa. ATM protein primarily resides in the cell nucleus and functions as a critical regulator of the cell cycle. It plays a significant role in the detection of DNA damage and initiation of repair processes. As part of its mechanical functions ATM phosphorylates serine and threonine residues on various substrates most notably in response to double-strand breaks in DNA. This activity is important for maintaining genomic stability.
Biological function summary

ATM acts as a coordinator in cellular response to DNA damage highly interacting with multiple components of the DNA repair machinery. It forms a complex with proteins like NBS1 and MRN complex facilitating repair by recruiting and activating other proteins involved in homologous recombination and non-homologous end joining pathways. ATM also modulates p53 activity a primary response factor in cellular stress management linking ATM to control of cell cycle arrest and apoptosis. This positions ATM as an integral part of maintaining cellular integrity in face of genomic insult.

Pathways

ATM integrates neatly within the DNA damage response and cell cycle control pathways. ATM's operative relationship with the MRN complex and its role in the PI3K-related protein kinase family helps initiate appropriate repair processes upon DNA damage detection. Additionally ATM regulates the activity of proteins such as Chk2 which further propagates signals to p53 influencing decisions between cell cycle arrest and apoptosis. These interactions link ATM closely to essential processes like DNA repair and cell survival highlighting its role in genomic maintenance.

ATM mutations or dysregulation leads to Ataxia Telangiectasia an autosomal recessive disorder characterized by neurodegeneration immune deficiencies and cancer predisposition. ATM dysfunction also connects to cancer development particularly breast cancer where it transmits signals involving BRCA1 contributing to DNA repair through homologous recombination. Understanding ATM dynamics and related pathways has important implications for developing therapeutic strategies to manage or mitigate effects associated with its dysfunction.

Specifications

Form

Liquid

Additional notes

Glutathione Sepharose

General info

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 (PubMed : 10550055, PubMed : 10839545, PubMed : 10910365, PubMed : 12556884, PubMed : 14871926, PubMed : 15064416, PubMed : 15448695, PubMed : 15456891, PubMed : 15790808, PubMed : 15916964, PubMed : 17923702, PubMed : 21757780, PubMed : 24534091, PubMed : 35076389, PubMed : 9733514). Recognizes the substrate consensus sequence [ST]-Q (PubMed : 10550055, PubMed : 10839545, PubMed : 10910365, PubMed : 12556884, PubMed : 14871926, PubMed : 15448695, PubMed : 15456891, PubMed : 15916964, PubMed : 17923702, PubMed : 24534091, PubMed : 9733514). Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism (By similarity). 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, FBXW7, FANCD2, NFKBIA, BRCA1, CREBBP/CBP, RBBP8/CTIP, MRE11, nibrin (NBN), RAD50, RAD17, PELI1, TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed : 10550055, PubMed : 10766245, PubMed : 10802669, PubMed : 10839545, PubMed : 10910365, PubMed : 10973490, PubMed : 11375976, PubMed : 12086603, PubMed : 15456891, PubMed : 19965871, PubMed : 21757780, PubMed : 24534091, PubMed : 26240375, PubMed : 26774286, PubMed : 30612738, PubMed : 30886146, PubMed : 30952868, PubMed : 38128537, PubMed : 9733515, PubMed : 9843217). 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 (PubMed : 19965871). Phosphorylates ATF2 which stimulates its function in DNA damage response (PubMed : 15916964). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed : 29203878). Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (PubMed : 15448695). Also involved in pexophagy by mediating phosphorylation of PEX5 : translocated to peroxisomes in response to reactive oxygen species (ROS), and catalyzes phosphorylation of PEX5, promoting PEX5 ubiquitination and induction of pexophagy (PubMed : 26344566).

Sequence similarities

Belongs to the PI3/PI4-kinase family. ATM subfamily.

Post-translational modifications

Phosphorylated by NUAK1/ARK5 (PubMed:12409306). Autophosphorylation on Ser-367, Ser-1893, Ser-1981 correlates with DNA damage-mediated activation of the kinase (PubMed:12556884, PubMed:15790808, PubMed:16141325, PubMed:16858402, PubMed:21144835, PubMed:27664052). During the late stages of DNA damage response, dephosphorylated following deacetylation by SIRT7, leading to ATM deactivation (PubMed:30944854).. Acetylation, on DNA damage, is required for activation of the kinase activity, dimer-monomer transition, and subsequent autophosphorylation on Ser-1981 (PubMed:12556884, PubMed:16141325, PubMed:16858402, PubMed:17923702, PubMed:21144835). Acetylated in vitro by KAT5/TIP60 (PubMed:16141325). Deacetylated by SIRT7 during the late stages of DNA damage response, promoting ATM dephosphorylation and subsequent deactivation (PubMed:30944854).

Subcellular localisation

Nucleus

Product protocols

Target data

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 (PubMed : 10550055, PubMed : 10839545, PubMed : 10910365, PubMed : 12556884, PubMed : 14871926, PubMed : 15064416, PubMed : 15448695, PubMed : 15456891, PubMed : 15790808, PubMed : 15916964, PubMed : 17923702, PubMed : 21757780, PubMed : 24534091, PubMed : 35076389, PubMed : 9733514). Recognizes the substrate consensus sequence [ST]-Q (PubMed : 10550055, PubMed : 10839545, PubMed : 10910365, PubMed : 12556884, PubMed : 14871926, PubMed : 15448695, PubMed : 15456891, PubMed : 15916964, PubMed : 17923702, PubMed : 24534091, PubMed : 9733514). Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism (By similarity). 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, FBXW7, FANCD2, NFKBIA, BRCA1, CREBBP/CBP, RBBP8/CTIP, MRE11, nibrin (NBN), RAD50, RAD17, PELI1, TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed : 10550055, PubMed : 10766245, PubMed : 10802669, PubMed : 10839545, PubMed : 10910365, PubMed : 10973490, PubMed : 11375976, PubMed : 12086603, PubMed : 15456891, PubMed : 19965871, PubMed : 21757780, PubMed : 24534091, PubMed : 26240375, PubMed : 26774286, PubMed : 30612738, PubMed : 30886146, PubMed : 30952868, PubMed : 38128537, PubMed : 9733515, PubMed : 9843217). 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 (PubMed : 19965871). Phosphorylates ATF2 which stimulates its function in DNA damage response (PubMed : 15916964). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed : 29203878). Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (PubMed : 15448695). Also involved in pexophagy by mediating phosphorylation of PEX5 : translocated to peroxisomes in response to reactive oxygen species (ROS), and catalyzes phosphorylation of PEX5, promoting PEX5 ubiquitination and induction of pexophagy (PubMed : 26344566).
See full target information ATM

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