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AB179933

Anti-DIS3 antibody

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(2 Publications)

Rabbit Polyclonal DIS3 antibody. Suitable for WB, IHC-P and reacts with Mouse, Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human DIS3 aa 300-350 conjugated to Keyhole Limpet Haemocyanin.

View Alternative Names

KIAA1008, RRP44, DIS3, Exosome complex exonuclease RRP44, Protein DIS3 homolog, Ribosomal RNA-processing protein 44

2 Images
Western blot - Anti-DIS3 antibody (AB179933)
  • WB

Supplier Data

Western blot - Anti-DIS3 antibody (AB179933)

All lanes:

Western blot - Anti-DIS3 antibody (ab179933) at 1/1000 dilution

All lanes:

Mouse bladder lysate at 15 µg

Predicted band size: 109 kDa

false

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-DIS3 antibody (AB179933)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-DIS3 antibody (AB179933)

Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human skin tissue labelling DIS3 with ab179933 at 5μg/ml.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

WB, IHC-P

applications

Immunogen

Synthetic Peptide within Human DIS3 aa 300-350 conjugated to Keyhole Limpet Haemocyanin. The exact immunogen used to generate this antibody is proprietary information.

Q9Y2L1

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.09% Sodium azide Constituents: 99% PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
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.

DIS3 also known as RRP44 is an exoribonuclease and an essential component of the RNA degradation machinery. It possesses a molecular mass of approximately 110 kDa and functions as an RNA helicase and 3'-5' exoribonuclease. DIS3 is expressed in various tissues including the bone marrow and lymphoid tissues. The protein acts to degrade defective RNA molecules and regulate RNA levels ensuring accurate gene expression and proper cellular function.
Biological function summary

DIS3 participates in the RNA exosome complex a multi-protein complex responsible for processing and degrading RNA. This complex processes a wide range of RNA substrates including pre-rRNA snRNA and snoRNA. DIS3 performs its function by catalyzing the exonucleolytic cleavage of these RNA molecules regulating their abundance and contributing to RNA quality control. As a critical member of the exosome DIS3 is essential for cellular RNA homeostasis and plays a role in maintaining the stability of the transcriptome.

Pathways

RNA metabolism and degradation significantly involve DIS3 impacting mRNA surveillance and decay pathways. It notably contributes to the Nonsense-Mediated mRNA Decay (NMD) pathway which detects and degrades mRNAs containing premature stop codons. DIS3 interacts with other exosome components such as RRP6 and MTR4 facilitating the processing of diverse RNA species. The protein’s role is integral to overall RNA turnover and quality control ensuring effective removal of defective RNA transcripts and preventing inappropriate protein synthesis.

Mutations or dysregulation of DIS3 relate to multiple myeloma and acute myeloid leukemia. In these conditions aberrant RNA degradation may contribute to the pathogenesis by altering normal RNA processing and expression profiles. DIS3 mutations can lead to impaired function of the exosome enhancing the survival and proliferation of malignant cells. Additionally proteins such as RRP6 are connected with DIS3 through their roles in the exosome machinery suggesting combined involvement in RNA processing-related diseases.

Product protocols

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

Target data

Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. DIS3 has both 3'-5' exonuclease and endonuclease activities.
See full target information DIS3

Publications (2)

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

Journal of Cancer 14:2001-2014 PubMed37497407

2023

CAVIN2/SDPR Functioned as a Tumor Suppressor in Lung Adenocarcinoma from Systematic Analysis of Caveolae-Related Genes and Experimental Validation.

Applications

Unspecified application

Species

Unspecified reactive species

Keyun Zhu,Baichuan Wang,Yingxi Li,Yue Yu,Zhaohui Chen,Haoran Yue,Qingxiang Meng,Dongchen Tian,Xiaofeng Liu,Weiyu Shen,Yao Tian

Genes & development 33:1381-1396 PubMed31488579

2019

, the nuclear exosome targeting component, is mutated in familial pulmonary fibrosis and is required for telomerase RNA maturation.

Applications

Unspecified application

Species

Unspecified reactive species

Dustin L Gable,Valeriya Gaysinskaya,Christine C Atik,C Conover Talbot,Byunghak Kang,Susan E Stanley,Elizabeth W Pugh,Nuria Amat-Codina,Kara M Schenk,Murat O Arcasoy,Cory Brayton,Liliana Florea,Mary Armanios
View all publications

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