Recombinant Human RPL5 protein is a Human Full Length protein, in the 1 to 297 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs (PubMed:12962325, PubMed:19061985, PubMed:23636399, PubMed:24120868). It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53 (PubMed:24120868).
MSTP030, RPL5, Large ribosomal subunit protein uL18, 60S ribosomal protein L5
Recombinant Human RPL5 protein is a Human Full Length protein, in the 1 to 297 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab183222 was purified using conventional chromatography techniques.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs (PubMed:12962325, PubMed:19061985, PubMed:23636399, PubMed:24120868). It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53 (PubMed:24120868).
Belongs to the universal ribosomal protein uL18 family.
RPL5 also known as ribosomal protein L5 or uL18 is a component of the large 60S subunit of ribosomes. Its molecular weight is approximately 34 kDa. This protein plays an important role in protein synthesis by facilitating the assembly of the 5S ribonucleoprotein complex. RPL5 is expressed ubiquitously across various tissues indicating its role in essential cellular processes.
The actions of RPL5 include its involvement in the incorporation of the 5S rRNA into the ribosomal subunit in cooperation with other ribosomal proteins. RPL5 is part of the ribosomal complex which is fundamental for translating mRNA into polypeptides. By binding with 5S rRNA RPL5 ensures the structural integrity and functional competence of the ribosome which are important for gene expression and cellular homeostasis.
RPL5 plays a critical role in the ribosome biogenesis pathway and indirectly influences the p53 pathway. It interacts with RPL11 to regulate the p53 response during ribosomal stress which connects RPL5 to the ribosomal stress checkpoint pathway. Deviations in ribosomal assembly or function can influence processes linked to cell cycle regulation and apoptosis.
Alterations in RPL5 have a link to Diamond-Blackfan anemia a disorder characterized by failed ribosome biogenesis affecting erythropoiesis. Mutations in RPL5 in association with failures in the RPL11 gene contribute to this condition by disrupting the proper assembly of ribosomes leading to impaired red blood cell production. Additionally dysregulation of the p53 pathway through RPL5 interaction may have implications in cancer development as it can affect cell growth control and apoptosis.
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15% SDS-PAGE analysis of ab183222 (3μg).
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