WB | 1/1000 | Human,Mouse,Rat |
IF | 咨询技术 | Human,Mouse,Rat |
IHC | 咨询技术 | Human,Mouse,Rat |
ICC | 技术咨询 | Human,Mouse,Rat |
FCM | 咨询技术 | Human,Mouse,Rat |
Elisa | 咨询技术 | Human,Mouse,Rat |
Aliases | Ribonuclease P protein subunit p38, RNaseP protein p38, RPP38 |
Entrez GeneID | 10557 |
WB Predicted band size | 31.8kDa |
Host/Isotype | Rabbit IgG |
Antibody Type | Primary antibody |
Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
Species Reactivity | Human |
Immunogen | This RPP38 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 248-277 amino acids from the C-terminal region of human RPP38. |
Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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The RPP38 antibody targets the Ribonuclease P Protein subunit p38 (RPP38), a key component of the RNase P complex, which is essential for processing precursor tRNA (pre-tRNA) by cleaving its 5' leader sequence. RNase P is a ribonucleoprotein complex comprising both RNA and protein subunits, with RPP38 playing a structural and catalytic role in tRNA maturation. This protein is also associated with other cellular processes, including ribosomal RNA processing and telomerase activity regulation.
RPP38 antibodies are widely used in molecular biology to study RNase P assembly, tRNA biogenesis, and its dysregulation in diseases. For example, altered RPP38 expression has been linked to cancers and autoimmune disorders like systemic sclerosis (scleroderma), where autoantibodies against RPP38 are occasionally detected. Researchers employ these antibodies in techniques such as Western blotting, immunofluorescence, and immunoprecipitation to analyze protein expression, localization (notably in the nucleolus), and interactions.
Commercially available RPP38 antibodies are typically produced in rabbits or mice using recombinant proteins or synthetic peptides. Their specificity and applications are validated in model organisms and human cell lines. Beyond basic research, RPP38 antibodies hold potential in clinical diagnostics, particularly in identifying biomarkers for autoimmune conditions or cancer progression. However, cross-reactivity with homologous proteins remains a consideration, necessitating rigorous validation for experimental accuracy.
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