EXOSC4 Polyclonal Antibody (E-AB-19187)

For research use only.
Verified Samples |
Verified Samples in WB: 293T, L-O2, Hela, Jurkat Verified Samples in IHC: Human thyroid cancer |
Dilution | WB 1:500-1:2000, IHC 1:50-1:200 |
Isotype | IgG |
Host | Rabbit |
Reactivity | Human, Mouse |
Applications | WB, IHC |
Clonality | Polyclonal |
Immunogen | Fusion protein of human EXOSC4 |
Abbre | EXOSC4 |
Synonyms | EXOSC 4, Exosome complex component RRP41, Exosome complex exonuclease RRP41, Exosome component 4 , Exosome component Rrp41 , FLJ20591 , RRP 41, RRP41, RRP41A , Ribosomal RNA processing protein 41, Rrp41p , SKI 6, SKI6 , Ski6p, hRrp41p, p12A |
Swissprot | |
Calculated MW | 26 kDa |
Observed MW |
Refer to figures
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
Cellular Localization | Cytoplasm. Nucleus, nucleolus. |
Concentration | 0.84 mg/mL |
Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
Purification Method | Antigen affinity purification |
Research Areas | Epigenetics and Nuclear Signaling |
Conjugation | Unconjugated |
Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
background | 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. EXOSC4 binds to ARE-containing RNAs. |
Other Clones
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Unconjugated
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