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AB152135

Anti-DOM3Z antibody

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(2 Publications)

Rabbit Polyclonal DOM3Z antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human DXO aa 1-250.

View Alternative Names

DOM3L, DOM3Z, NG6, DXO, Decapping and exoribonuclease protein, 5'-3' exoribonuclease DXO, Dom-3 homolog Z, NAD-capped RNA hydrolase DXO, DeNADding enzyme DXO

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-DOM3Z antibody (AB152135)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-DOM3Z antibody (AB152135)

Immunofluorescent analysis of methanol-fixed HeLa cells labeling DOM3Z with ab152135 at 1/200 dilution. Lower panel co-stained with Hoechst 33342.

Western blot - Anti-DOM3Z antibody (AB152135)
  • WB

Unknown

Western blot - Anti-DOM3Z antibody (AB152135)

10% SDS PAGE

All lanes:

Western blot - Anti-DOM3Z antibody (ab152135) at 1/500 dilution

Lane 1:

MOLT4 whole cell lysate at 30 µg

Lane 2:

Raji whole cell lysate at 30 µg

Predicted band size: 45 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ICC/IF, WB

applications

Immunogen

Recombinant Fragment Protein within Human DXO aa 1-250. The exact immunogen used to generate this antibody is proprietary information.

O77932

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: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
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.

DOM3Z also known as exosome component 1 or hDOM3Z is a protein involved in RNA processing and degradation. It has a molecular mass of about 28 kDa. This protein is present in various tissues with higher expression levels seen in the heart and skeletal muscle. DOM3Z localizes to the nucleus where it plays an important role in maintaining RNA quality control. The protein acts within the RNA exosome complex which is a multi-protein complex essential for RNA decay.
Biological function summary

DOM3Z forms part of the RNA exosome complex working in concert with other components to remove defective or unnecessary RNA molecules. This activity is essential for regulating RNA homeostasis and ensuring the fidelity of RNA populations within the cell. By interacting with exosome core components and exosome co-factors DOM3Z facilitates the degradation of a wide range of RNA substrates including messenger RNA and non-coding RNA. The proper function of DOM3Z within the exosome complex assures accuracy in gene expression regulation.

Pathways

The RNA degradation pathway heavily relies on functions executed by DOM3Z. It interacts with related proteins such as RRP6 and RRP44 within the exosome assembly. Another significant pathway involving DOM3Z is the non-coding RNA processing pathway where its involvement ensures the correct biogenesis and maturation of small nuclear RNAs and small nucleolar RNAs. This involvement of DOM3Z and its associated proteins highlights its central role in maintaining cellular RNA integrity and gene expression equilibrium.

Abnormalities in DOM3Z function correlate with neuromuscular disorders reflecting its higher expression levels in muscle tissues. Mutations or misregulation that affect DOM3Z can also relate to certain types of cancer where disrupted RNA processing leads to uncontrolled cell proliferation. In the context of these conditions DOM3Z interacts with several proteins like DIS3L2 which play roles in disease mechanisms. Understanding and investigating these associations may offer new avenues for therapeutic strategies targeting RNA metabolism disorders.

Product protocols

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

Target data

Decapping enzyme for NAD-capped RNAs : specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed : 28283058). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (PubMed : 28283058). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (PubMed : 28283058). Preferentially acts on NAD-capped transcripts in response to environmental stress (PubMed : 31101919). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation (By similarity). Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed : 29601584). In contrast to canonical decapping enzymes DCP2 and NUDT16, which cleave the cap within the triphosphate linkage, the decapping activity releases the entire cap structure GpppN and a 5'-end monophosphate RNA (By similarity). Also has 5'-3' exoribonuclease activities : The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs (PubMed : 29601584). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity). Exhibits decapping activity towards FAD-capped RNAs (PubMed : 32374864). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
See full target information DXO

Publications (2)

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The Journal of clinical investigation 133: PubMed37022795

2023

Long noncoding RNA HIKER regulates erythropoiesis in Monge's disease via CSNK2B.

Applications

Unspecified application

Species

Unspecified reactive species

Priti Azad,Dan Zhou,Hung-Chi Tu,Francisco C Villafuerte,David Traver,Tariq M Rana,Gabriel G Haddad

Cerebral cortex (New York, N.Y. : 1991) 27:4060-4072 PubMed27552836

2016

Prefrontal Cortical GABAergic Dysfunction Contributes to Aberrant UP-State Duration in APP Knockout Mice.

Applications

Unspecified application

Species

Unspecified reactive species

Qingwei Huo,Ming Chen,Quansheng He,Jiajia Zhang,Bo Li,Kai Jin,Xi Chen,Cheng Long,Li Yang
View all publications

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