MilliporeSigma™ phospho-ATM (Ser1981), Mouse, Unlabeled, Clone: 10H11.E12,
Manufacturer: MilliporeSigma™
Select a Size
| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| Each of 1 | MAB3806CMI-Each-of-1 | In Stock | ₹ 40,292.08 |
MAB3806CMI - Each of 1
In Stock
Quantity
1
Base Price: ₹ 40,292.08
GST (18%): ₹ 7,252.574
Total Price: ₹ 47,544.654
Antigen
phospho-ATM (Ser1981)
Classification
Monoclonal
Concentration
Please refer to lot specific datasheet.
Formulation
Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1M Tris-Glycine (pH 7.4), 150mM NaCl with 0.05% Sodium Azide.
Gene Accession No.
Q13315
Immunogen
Synthetic peptide corresponding to a.a. 1974-1988 of human ATM with phosphorylated Ser1981 (SLAFEEG[pS]QSTTISS).
Quantity
100 μg
Research Discipline
Epigenetics & Nuclear Function
Gene ID (Entrez)
NP_000042
Target Species
Human
Form
Purified
Applications
Immunocytochemistry, Immunoprecipitation, Western Blot
Clone
10H11.E12
Conjugate
Unconjugated
Gene
ATM, AT
Host Species
Mouse
Purification Method
Protein G Purified
Regulatory Status
RUO
Primary or Secondary
Primary
Test Specificity
Reacts with ATM Kinase phosphorylated at serine 1981. Clone 10H11.E12 is covered by US patent No. 6,916,627 and 7,108,992.
Content And Storage
Stable for 1 year at 2°-8°C from date of receipt.
Isotype
IgG1 κ
Related Products
Description
- Serine-protein kinase ATM (EC 2.7.11.1; UniProt Q13315; also known as A-T mutated, Ataxia telangiectasia mutated) is encoded by the ATM (also known as AT) gene (Gene ID 472) in human
- Ataxia telangiectasia mutated kinase (ATM) and ataxia telangiectasia and Rad3-related kinase (ATR) are related kinases that regulate cell cycle checkpoints and DNA repair
- Mutation in the ATM gene results in the autosomal recessive disease ataxia telangiectasia (AT)
- Known ATM substrates include p53, p95/NBS1, MDM2, Chk2, BRCA1, CtIP, 4E-BP1, and Chk1
- The S/TQ sequence constitutes the essential substrates phosphorylation site motif
- Hydrophobic amino acids at positions -3 and -1, and negatively charged amino acids at position +1 are positive determinants for substrate phosphorylation, while positively charged residues surrounding the S/TQ are negative determinants
- The complex phenotypes of cells derived from patients with AT suggests that ATM has additional cellular substrates
- ATM is present as an inactive homodimer or multimer prior to activation
- DNA double-stranded breaks induced by ionizing radiation (IR) cause rapid ATM autophosphorylation at Ser1981 in human or the Ser1987 equivalent in mouse.