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AB126962

Anti-DIPP antibody

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(1 Publication)

Rabbit Polyclonal DIPP antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human NUDT3 aa 1 to C-terminus.

View Alternative Names

DIPP, DIPP1, NUDT3, Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine hexaphosphate hydrolase, Endopolyphosphatase, Nucleoside diphosphate-linked moiety X motif 3, m7GpppN-mRNA hydrolase, m7GpppX diphosphatase, Ap6A hydrolase, Nudix motif 3

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-DIPP antibody (AB126962)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-DIPP antibody (AB126962)

ab126962, at a dilution of 1/500, staining DIPP in paraffin-embedded Human lung adenocarcinoma tissue by Immunohistochemistry.

Western blot - Anti-DIPP antibody (AB126962)
  • WB

Unknown

Western blot - Anti-DIPP antibody (AB126962)

12% SDS PAGE

All lanes:

Western blot - Anti-DIPP antibody (ab126962) at 1/1000 dilution

All lanes:

IMR32 whole cell lysate at 30 µg

Predicted band size: 19 kDa,37 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Recombinant Fragment Protein within Human NUDT3 aa 1 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

O95989

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

DIPP also known as a Diadenosine triphosphate hydrolase (Ap3Aase) acts mechanically as a nucleoside triphosphate diphosphohydrolase. It hydrolyzes nucleoside diphosphates such as Ap3A. DIPP has a molecular mass of approximately 41 kDa. It expresses in various tissues including the brain kidney and liver suggesting its involvement in essential biochemical processes.
Biological function summary

DIPP regulates the concentration of diadenosine polyphosphates which act as signaling molecules in cellular communication. These molecules control intracellular and extracellular nucleotide levels. DIPP sometimes forms part of a protein complex that modulates signal transduction pathways emphasizing its role in cellular homeostasis and signaling.

Pathways

DIPP integrates into the purinergic signaling pathway and it contributes to the regulation of energy metabolism. This protein interacts with other hydrolases and kinases influencing ATP degradation and synthesis. Through this interaction it plays a role with proteins like NTPDases highlighting its significance in nucleotide management.

DIPP contributes to diseases related to abnormal nucleotide levels such as cancer and neurological disorders. In cancer altered DIPP activity relates to dysregulation of cellular energy balance. Additionally in neurological disorders DIPP's interaction with proteins like Ap3A-binding proteins might affect synaptic transmission and neuronal function illustrating its involvement in neuronal health.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (PubMed : 10585413, PubMed : 12370170, PubMed : 9822604). InsP6 (inositol hexakisphosphate) is not a substrate (PubMed : 9822604). Acts as a negative regulator of the ERK1/2 pathway (By similarity). Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) and diadenosine 5',5'''- P1,P5-pentaphosphate (Ap5A) being the preferred substrates (PubMed : 10419486, PubMed : 12370170). The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A (PubMed : 12370170). Also able to hydrolyze 5-phosphoribose 1-diphosphate (PubMed : 12370170). Acts as a decapping enzyme that modulates the stability of a subset of mRNAs implicated in cell motility (PubMed : 26932476). Hydrolyzes monomethylated capped RNA after both the alpha- and beta-phosphates generating m7GMP + ppRNA and m7GDP + pRNA (PubMed : 32727897). Can hydrolyze unmethylated capped RNAs (By similarity). Divalent cations zinc, magnesium and manganese determine its substrate specificity (PubMed : 34788624). Exhibits diphosphoinositol polyphosphate phosphohydrolase in the presence of magnesium ions, diadenosine hexaphosphate hydrolase activity in the presence of manganese ions and endopolyphosphatase activity in the presence of zinc ions (PubMed : 34788624). Plays an important role in limiting DNA damage and maintaining cell survival upon oxidative stress via its endopolyphosphatase activity (PubMed : 34788624).
See full target information NUDT3

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Nature 619:176-183 PubMed37286593

2023

Epigenetic dysregulation from chromosomal transit in micronuclei.

Applications

Unspecified application

Species

Unspecified reactive species

Albert S Agustinus,Duaa Al-Rawi,Bhargavi Dameracharla,Ramya Raviram,Bailey S C L Jones,Stephanie Stransky,Lorenzo Scipioni,Jens Luebeck,Melody Di Bona,Danguole Norkunaite,Robert M Myers,Mercedes Duran,Seongmin Choi,Britta Weigelt,Shira Yomtoubian,Andrew McPherson,Eléonore Toufektchan,Kristina Keuper,Paul S Mischel,Vivek Mittal,Sohrab P Shah,John Maciejowski,Zuzana Storchova,Enrico Gratton,Peter Ly,Dan Landau,Mathieu F Bakhoum,Richard P Koche,Simone Sidoli,Vineet Bafna,Yael David,Samuel F Bakhoum
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Product promise

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