RPL5 Antibody / 60S ribosomal protein L5

Overview

60S ribosomal protein L5 is a protein that in humans is encoded by the RPL5 gene. Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of four RNA species and approximately 80 structurally distinct proteins. This gene encodes a member of the L18P family of ribosomal proteins and component of the 60S subunit. The encoded protein binds 5S rRNA to form a stable complex called the 5S ribonucleoprotein particle (RNP), which is necessary for the transport of nonribosome-associated cytoplasmic 5S rRNA to the nucleolus for assembly into ribosomes. The encoded protein may also function to inhibit tumorigenesis through the activation of downstream tumor suppressors and the downregulation of oncoprotein expression. Mutations in this gene have been identified in patients with Diamond-Blackfan Anemia (DBA). This gene is co-transcribed with the small nucleolar RNA gene U21, which is located in its fifth intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed throughout the genome.

This anti-RPL5 antibody is supplied as Antigen affinity purified (Rabbit, Polyclonal (rabbit origin), Rabbit IgG, Unconjugated) and is designed to support common target-detection workflows after the on-page specifications.

Key elements and design rationale

• Target: RPL5
• Format: Antigen affinity purified
• Species reactivity: Human
• Applications (listed): WB, FACS, Direct ELISA
• Conjugate: Unconjugated
• Clone and antibody class: Polyclonal (rabbit origin), Rabbit IgG

Because antibody performance can depend on epitope context, sample preparation, and biological state, interpret signals using appropriate controls and orthogonal evidence when possible.

Biological background

RPL5 is referenced in public gene/protein resources (e.g., UniProt and NCBI Gene), which provide curated names/synonyms, protein features, and pathway context. When designing assays, consider potential isoforms, post-translational modifications, and cell-type specific expression that may influence observed signal.

Research relevance and current trends

• Profiling RPL5 expression across model systems, perturbations, and time points to support mechanistic hypotheses.
• Combining antibody-based detection with multi-omics or imaging readouts to link RPL5 signal with phenotype.
• Using well-matched controls (isotype controls, genetic perturbations, or independent reagents) to strengthen interpretation of target-associated signal.

Common research applications

• WB
• FACS
• Direct ELISA

Use the listed applications as a starting point and tailor experimental design to your sample type and readout requirements.

Notes for experimental interpretation

• Specificity considerations: closely related family members, isoforms, or PTMs can affect apparent specificity; confirm with independent approaches when critical.
• Controls: include negative controls and, when feasible, genetic or pharmacologic perturbations to support target attribution in your system.
• Species and sample context: differences in sequence, expression, fixation, or extraction conditions can change signal behavior across models.

Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.