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AB79665

Recombinant human PARP9 protein (GST N-Terminus + His tag C-Terminus)

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(2 Publications)

Recombinant human PARP9 protein (GST N-Terminus + His tag C-Terminus) is a Human Full Length protein, in the 1 to 854 aa range, expressed in Baculovirus infected Sf9 cells, with >80%, suitable for SDS-PAGE, FuncS.

View Alternative Names

BAL, BAL1, PARP9, Protein mono-ADP-ribosyltransferase PARP9, ADP-ribosyltransferase diphtheria toxin-like 9, B aggressive lymphoma protein, Poly [ADP-ribose] polymerase 9, ARTD9, PARP-9

1 Images
SDS-PAGE - Recombinant human PARP9 protein (GST N-Terminus + His tag C-Terminus) (AB79665)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PARP9 protein (GST N-Terminus + His tag C-Terminus) (AB79665)

SDS-PAGE showing ab79665 at approximately 119kDa (4μg).

Key facts

Purity

>80% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus His tag C-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific Activity: 196 U/mg.

Accession

Q8IXQ6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 50% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.395% Tris HCl, 0.05% Sorbitan monolaurate, ethoxylated, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Recombinant human PARP3/IRT1 protein (GST tag N-Terminus)

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Primary Antibodies

AB53796

Anti-PARP9 antibody

Western blot - Anti-PARP9 antibody (AB53796)

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AB271651

Recombinant human PARP7 protein (DDDDK tag N-Terminus)

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Reactivity data

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

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":854,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q8IXQ6","tags":[{"tag":"GST","terminus":"N-Terminus"},{"tag":"His","terminus":"C-Terminus"}]}]
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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
True
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Supplementary information

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

PARP9 also known as ADP-ribosyltransferase diphtheria toxin-like 9 is a protein involved in cellular DNA repair and immune response. The protein has a molecular mass of approximately 88 kDa. It is notably expressed in various tissues including lymphoid tissues and immune cells suggesting a role in the immune system. PARP9 possesses domains that may facilitate interactions with other proteins playing a part in regulating cellular repair processes.
Biological function summary

PARP9 enhances DNA repair mechanisms and modulates the immune response. It may work as part of larger protein complexes coordinating with other proteins to maintain genomic stability and regulate transcription. Its involvement in these complexes indicates a supportive role in cellular defense ensuring the integrity of genetic information and proper immune function. Moreover PARP9 may influence signal transduction pathways related to inflammation and cell survival.

Pathways

PARP9 participates in critical networks that govern DNA damage response and immune signaling. It aligns with the NF-kB pathway which controls transcription of DNA cytokine production and cell survival. Additionally PARP9 associates with the innate immune response pathway influencing processes driven by related proteins like STAT1 enhancing the cellular response to external stressors. These interactions reflect its contribution to cellular adaptation and resilience.

PARP9 links to conditions with underlying inflammatory or immune-related components. Its dysregulation associates with autoimmune diseases where it may influence abnormal immune activity. Additionally PARP9 has connections to certain cancers potentially through interactions with proteins like STAT3 which influences cell proliferation and survival. Understanding PARP9's role in these conditions could guide therapeutic strategies targeting abnormal protein interactions and signaling.
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Specifications

Form

Liquid

Additional notes

Affinity purified.

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General info

Function

ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses (PubMed : 16809771, PubMed : 23230272, PubMed : 26479788, PubMed : 27796300). Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP-ribose) (PubMed : 28525742). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones (PubMed : 28525742). During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1 (PubMed : 23230272). Subsequent PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed : 23230272, PubMed : 28525742). In response to DNA damage, PARP9-DTX3L complex is required for efficient non-homologous end joining (NHEJ); the complex function is negatively modulated by PARP9 activity (PubMed : 28525742). Dispensable for B-cell receptor (BCR) assembly through V(D)J recombination and class switch recombination (CSR) (By similarity). In macrophages, positively regulates pro-inflammatory cytokines production in response to IFNG stimulation by suppressing PARP14-mediated STAT1 ADP-ribosylation and thus promoting STAT1 phosphorylation (PubMed : 27796300). Also suppresses PARP14-mediated STAT6 ADP-ribosylation (PubMed : 27796300).

Sequence similarities

Belongs to the ARTD/PARP family.

Post-translational modifications

ADP-ribosylated by PARP14.

Subcellular localisation

Nucleus

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Product protocols

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Target data

ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses (PubMed : 16809771, PubMed : 23230272, PubMed : 26479788, PubMed : 27796300). Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP-ribose) (PubMed : 28525742). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones (PubMed : 28525742). During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1 (PubMed : 23230272). Subsequent PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed : 23230272, PubMed : 28525742). In response to DNA damage, PARP9-DTX3L complex is required for efficient non-homologous end joining (NHEJ); the complex function is negatively modulated by PARP9 activity (PubMed : 28525742). Dispensable for B-cell receptor (BCR) assembly through V(D)J recombination and class switch recombination (CSR) (By similarity). In macrophages, positively regulates pro-inflammatory cytokines production in response to IFNG stimulation by suppressing PARP14-mediated STAT1 ADP-ribosylation and thus promoting STAT1 phosphorylation (PubMed : 27796300). Also suppresses PARP14-mediated STAT6 ADP-ribosylation (PubMed : 27796300).
See full target information PARP9
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Publications (2)

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

Nature communications 12:2681 PubMed33976210

2021

Identification of poly(ADP-ribose) polymerase 9 (PARP9) as a noncanonical sensor for RNA virus in dendritic cells.

Applications

Unspecified application

Species

Unspecified reactive species

Junji Xing,Ao Zhang,Yong Du,Mingli Fang,Laurie J Minze,Yong-Jun Liu,Xian Chang Li,Zhiqiang Zhang

Science advances 6: PubMed32948590

2020

Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases.

Applications

Unspecified application

Species

Unspecified reactive species

Chatrin Chatrin,Mads Gabrielsen,Lori Buetow,Mark A Nakasone,Syed F Ahmed,David Sumpton,Gary J Sibbet,Brian O Smith,Danny T Huang
View all publications
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