Mouse Monoclonal CSL4 antibody. Suitable for ELISA and reacts with Human samples. Cited in 2 publications.
pH: 7.2
Preservative: 0.01% Sodium azide
Constituents: 0.88% Sodium chloride, 0.424% Potassium phosphate solution
ELISA | |
---|---|
Human | Expected |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/5000.00000 - 1/20000.00000 | Notes - |
Non-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. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8.
CSL4, CGI-108, EXOSC1, Exosome complex component CSL4, Exosome component 1
Mouse Monoclonal CSL4 antibody. Suitable for ELISA and reacts with Human samples. Cited in 2 publications.
pH: 7.2
Preservative: 0.01% Sodium azide
Constituents: 0.88% Sodium chloride, 0.424% Potassium phosphate solution
This protein A purified mouse monoclonal antibody reacts specifically with p13 in human granulocytes and monocytes residing in lymphoid and non-lymphoid tissues The antibody recognizes a 13 kDa band corresponding to p13. Cross reactivity from other sources has not been determined.
This protein A purified mouse monoclonal antibody reacts specifically with p13 in human granulocytes and monocytes residing in lymphoid and non-lymphoid tissues.
BM3 is an early marker of myeloid differentiation. Immunoprecipitation experiments using S35 methionine labeled human myeloid leukemia cells show that BM3 identifies a 13 kDa protein.
The antibody does not stain tissue after paraffin treatment.
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P13 also known as MAPK-interacting serine/threonine-protein kinase 1 (MNK1) is a protein with a mass of approximately 51 kDa. This protein functions as a kinase meaning it adds phosphate groups to other molecules often regulating their activity. p13 is expressed in various tissues but it shows higher expression in the brain and testes. Like many kinases it modulates cellular processes by phosphorylating substrates which leads to changes in their function and consequently impacts cell signaling pathways.
The kinase activity of p13 influences several processes by participating in the regulation of mRNA translation. It binds to and phosphorylates the eukaryotic translation initiation factor 4E (eIF4E) which is a component of the eIF4F complex responsible for initiating protein synthesis. By phosphorylating eIF4E p13 affects translation rates and potentially influences the production of proteins from specific mRNAs thereby indirectly controlling various cellular functions.
P13 plays roles in the mitogen-activated protein kinase (MAPK) signaling and mammalian target of rapamycin (mTOR) pathways. These pathways regulate cell growth proliferation and survival. In the MAPK pathway p13 can interact with various other kinases such as ERK and integrate signals that influence translation. The mTOR pathway involves complex signaling networks where p13 modulates translation machinery components. Through these pathways p13 interconnects with proteins like RPS6KB1 further illustrating its role in controlling protein synthesis and cellular growth.
P13 has been linked to cancer and neurodegenerative diseases. In cancer its elevated activity may lead to increased protein synthesis and cell proliferation contributing to tumorigenesis. For instance its interplay with eIF4E has been observed in several malignancies suggesting a potential therapeutic target in oncology. In neurodegenerative diseases aberrant signaling involving p13 may alter neuron function or survival possibly involving proteins like mTOR which when dysregulated contribute to the pathophysiology of conditions like Alzheimer's disease.
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