RPL3 Antibody [H7C5] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000-1:8000 IHC1:50-1:500 IF1:400-1:1600

Application
WB, IHC, IF

Reactivity
Mouse, Rat, Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
46 kDa 46 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
RPL3 Antibody [H7C5] detects endogenous levels of total RPL3 protein.

Clone
H7C5

Synonym(s)
Large ribosomal subunit protein Ul3, 60S ribosomal protein L3, HIV-1 TAR RNA-binding protein B (TARBP-B), RPL3

Background
RPL3 is a conserved component of the large 60S ribosomal subunit and belongs to the uL3 family of ribosomal proteins, where it occupies a central position adjacent to the peptidyl transferase center and contributes directly to the structural and functional integrity of the eukaryotic translation machinery. The protein adopts a globular core with extended “tentacle”-like regions that penetrate deeply into the large subunit rRNA, contacting helices near the peptidyl transferase center and the sarcin–ricin loop, and these contacts stabilize rRNA architecture required for accurate positioning and accommodation of aminoacyl‑tRNA and peptidyl‑tRNA during peptide bond formation. Within pre‑ribosomal particles and mature ribosomes, RPL3 acts as a structural constituent that supports 60S subunit assembly, 80S subunit joining, and maintenance of translational fidelity, and yeast mutational analyses highlight a functionally important region near a conserved histidine and tryptophan “W‑finger” whose perturbation alters peptidyl transferase activity, aa‑tRNA binding, and sensitivity to peptidyl transferase–targeting antibiotics. RPL3 also participates in late steps of pre‑40S maturation by promoting 20S pre‑rRNA cleavage at site D within 80S‑like quality control complexes that contain pre‑40S and mature 60S subunits and the initiation factor eIF5B/Fun12; integrity of the RPL3 W‑finger region is required for stimulation of eIF5B GTPase activity and for productive 18S rRNA 3′‑end processing that licenses pre‑40S subunits for translation. In human cells, RPL3 expression is subject to autoregulation through alternative splicing coupled to nonsense‑mediated decay, and the RPL3 protein can redistribute from ribosomes to the nucleus under ribosomal stress, where it interacts with factors that control p21 expression and cell‑cycle progression in p53‑independent contexts, indicating that RPL3 links ribosome biogenesis status to stress-responsive transcriptional programs. RPL3 expression and integrity are therefore important not only for bulk translation and ribosome assembly but also for ribosomal stress signaling, and dysregulation or mutation in RPL3 has been associated with altered sensitivity to chemotherapeutic agents and with tumor cell proliferation phenotypes.

Background

RPL3 is a conserved component of the large 60S ribosomal subunit and belongs to the uL3 family of ribosomal proteins, where it occupies a central position adjacent to the peptidyl transferase center and contributes directly to the structural and functional integrity of the eukaryotic translation machinery. The protein adopts a globular core with extended “tentacle”-like regions that penetrate deeply into the large subunit rRNA, contacting helices near the peptidyl transferase center and the sarcin–ricin loop, and these contacts stabilize rRNA architecture required for accurate positioning and accommodation of aminoacyl‑tRNA and peptidyl‑tRNA during peptide bond formation. Within pre‑ribosomal particles and mature ribosomes, RPL3 acts as a structural constituent that supports 60S subunit assembly, 80S subunit joining, and maintenance of translational fidelity, and yeast mutational analyses highlight a functionally important region near a conserved histidine and tryptophan “W‑finger” whose perturbation alters peptidyl transferase activity, aa‑tRNA binding, and sensitivity to peptidyl transferase–targeting antibiotics. RPL3 also participates in late steps of pre‑40S maturation by promoting 20S pre‑rRNA cleavage at site D within 80S‑like quality control complexes that contain pre‑40S and mature 60S subunits and the initiation factor eIF5B/Fun12; integrity of the RPL3 W‑finger region is required for stimulation of eIF5B GTPase activity and for productive 18S rRNA 3′‑end processing that licenses pre‑40S subunits for translation. In human cells, RPL3 expression is subject to autoregulation through alternative splicing coupled to nonsense‑mediated decay, and the RPL3 protein can redistribute from ribosomes to the nucleus under ribosomal stress, where it interacts with factors that control p21 expression and cell‑cycle progression in p53‑independent contexts, indicating that RPL3 links ribosome biogenesis status to stress-responsive transcriptional programs. RPL3 expression and integrity are therefore important not only for bulk translation and ribosome assembly but also for ribosomal stress signaling, and dysregulation or mutation in RPL3 has been associated with altered sensitivity to chemotherapeutic agents and with tumor cell proliferation phenotypes.

References
https://pubmed.ncbi.nlm.nih.gov/26826131/ https://pubmed.ncbi.nlm.nih.gov/24603549/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%