Ribosomal Protein S7 Antibody [E20M7]

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:100-1:1000 IP1:100-1:200 IHC1:50-1:500 IF1:50-1:500

Application
WB, IP, IHC, IF, ELISA

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
22 kDa

Datasheet & SDS

Biological Description

Specificity
Ribosomal Protein S7 Antibody [E20M7] detects endogenous levels of total Ribosomal Protein S7 protein.

Clone
E20M7

Synonym(s)
Small ribosomal subunit protein Es7, 40S ribosomal protein S7, RPS7

Background
Ribosomal protein S7, encoded by RPS7, is a conserved component of the small 40S ribosomal subunit in eukaryotes and belongs to the S7e family of basic RNA‑binding proteins that act both in ribosome biogenesis and in mRNA translation. The protein is predominantly cytoplasmic but participates first in nucleolar assembly steps as part of the small subunit (SSU) processome, where it associates with nascent pre‑rRNA, ribosome biogenesis factors, and additional ribosomal proteins to support rRNA folding, modification, processing, and packaging into the pre‑40S particle. In bacterial and archaeal analogues, S7 sits at the head of the small subunit and contacts the 3′ major domain of small subunit rRNA and tRNAs positioned at the A and P decoding sites; structural analyses define a positively charged surface formed by conserved basic and aromatic residues that binds rRNA and contributes to formation of the decoding center, and these core architectural features are retained in eukaryotic S7e family members. RPS7 therefore contributes to the structural integrity of the small subunit and to the correct positioning of rRNA and tRNA within the decoding center, supporting accurate codon recognition and peptide chain elongation during translation, and is annotated as a structural constituent of the ribosome with additional RNA‑binding activity. Human RPS7 also has extra‑ribosomal functions in stress signaling: it interacts with the E3 ligase MDM2, and this interaction inhibits MDM2 ubiquitin ligase activity and stabilizes both MDM2 and p53, linking perturbed ribosome biogenesis and “ribosomal stress” to activation of the p53 pathway and cell‑cycle arrest or apoptosis. RPS7 behaves as both a regulator and substrate of MDM2, as MDM2 ubiquitinates RPS7 and modulates its levels, creating a feedback loop that couples ribosomal protein homeostasis to p53‑dependent transcriptional programs. Genetic annotations associate RPS7 with Diamond–Blackfan anemia subtypes and other ribosomopathies, consistent with its essential role in rRNA maturation and small-subunit production.

Background

Ribosomal protein S7, encoded by RPS7, is a conserved component of the small 40S ribosomal subunit in eukaryotes and belongs to the S7e family of basic RNA‑binding proteins that act both in ribosome biogenesis and in mRNA translation. The protein is predominantly cytoplasmic but participates first in nucleolar assembly steps as part of the small subunit (SSU) processome, where it associates with nascent pre‑rRNA, ribosome biogenesis factors, and additional ribosomal proteins to support rRNA folding, modification, processing, and packaging into the pre‑40S particle. In bacterial and archaeal analogues, S7 sits at the head of the small subunit and contacts the 3′ major domain of small subunit rRNA and tRNAs positioned at the A and P decoding sites; structural analyses define a positively charged surface formed by conserved basic and aromatic residues that binds rRNA and contributes to formation of the decoding center, and these core architectural features are retained in eukaryotic S7e family members. RPS7 therefore contributes to the structural integrity of the small subunit and to the correct positioning of rRNA and tRNA within the decoding center, supporting accurate codon recognition and peptide chain elongation during translation, and is annotated as a structural constituent of the ribosome with additional RNA‑binding activity. Human RPS7 also has extra‑ribosomal functions in stress signaling: it interacts with the E3 ligase MDM2, and this interaction inhibits MDM2 ubiquitin ligase activity and stabilizes both MDM2 and p53, linking perturbed ribosome biogenesis and “ribosomal stress” to activation of the p53 pathway and cell‑cycle arrest or apoptosis. RPS7 behaves as both a regulator and substrate of MDM2, as MDM2 ubiquitinates RPS7 and modulates its levels, creating a feedback loop that couples ribosomal protein homeostasis to p53‑dependent transcriptional programs. Genetic annotations associate RPS7 with Diamond–Blackfan anemia subtypes and other ribosomopathies, consistent with its essential role in rRNA maturation and small-subunit production.

References
https://pubmed.ncbi.nlm.nih.gov/9331423/ https://pubmed.ncbi.nlm.nih.gov/19683495/

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%