Rabbit Anti-TUTase Polyclonal Antibody#abs140573

Rabbit Anti-TUTase Polyclonal Antibody#abs140573

Please note that the price stated is for reference only. If you require more detailed information regarding pricing, please reach out to our seller, Vecent. Western blot analysis TUTase using 3T3 whole cell lysates This product is for research use only, not for use in diagnostic prodecures or in...

Description

Catalog-specificationDelivery timeUSD price

abs140573-100ug

1-2 Weeks

301.0

abs140573-50ug

1-2 Weeks

201.0

Please note that the price stated is for reference only. If you require more detailed information regarding pricing, please reach out to our seller, Vecent.


Overview

catalog

abs140573
Other names1. The alpha regulated poly(A) polymerase, also known as PAPD2 or Star-PAP, is a nuclear speckle targeted enzyme that is involved in the regulation of polyadenylation. It is a protein encoded by the RBM21 gene and belongs to the family of RNA-binding motif proteins.
2. The nuclear speckle targeted phosphatidylinositol 4 phosphate 5 kinase type I, or PIPK1A, is another enzyme that interacts with PAPD2 in the nuclear speckles. It plays a role in regulating the synthesis of phosphatidylinositol 4,5-bisphosphate, an important lipid signaling molecule.
3. PAPD2 contains a domain called the poly(A) polymerase associated domain, which is involved in mediating protein-protein interactions. This domain is crucial for the proper functioning of PAPD2 in the regulation of polyadenylation.
4. PAPD2 has been shown to be specifically associated with the U6 small nuclear RNA (snRNA), a component of the spliceosome machinery. It acts as a terminal uridylyl transferase, adding uridine residues to the 3' end of the U6 snRNA molecule.
5. The U6 snRNA specific terminal uridylyltransferase 1, or TUT1, is another name for PAPD2. It is responsible for the addition of uridine residues to the U6 snRNA, a process called uridylation. This modification is critical for the biogenesis and stability of the U6 snRNA.
6. The interaction between PAPD2 and PIPK1A in the nuclear speckles suggests a coordinated regulation of polyadenylation and phosphatidylinositol metabolism. This may indicate a potential link between RNA processing and lipid signaling pathways in the nucleus.
7. Understanding the functional significance of PAPD2 and its interactions with other proteins in the nuclear speckles could provide valuable insights into the regulation of RNA processing and its impact on cellular processes such as gene expression and cell signaling.
SourceRabbit
SpecificityThe TUTase Antibody is capable of identifying the presence of total TUTase at its natural levels within an organism. By rearranging the information from the original text, a highly similar content can be generated.
Species ReactivityHuman
Predictive reaction speciesRabbit;Dog;Horse
AntigenTUTase
ApplicationWB 1:1000, ELISA(peptide) 1:20000-1:40000
ImmunogenA synthesized peptide derived from human TUTase.
MW95kDa
Properties

Concentration

1mg/ml

purificationSulfoLink™ Coupling Resin was employed to purify the antiserum through peptide affinity chromatography.
ClonalityPolyclonal Antibody
Stability & StorageStore at -20 °C for one year. Avoid repeated freeze/thaw cycles
Storage bufferRabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.

Target

Background

Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.

Tissue specificityWidely expressed.
Posttranslational modificationPhosphorylated by CK1 in the proline-rich (Pro-rich) region.
Celluar localizationCytosol;Nucleus;
UniPortQ9H6E5


Western blot analysis TUTase using 3T3 whole cell lysates


This product is for research use only, not for use in diagnostic prodecures or in human.


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