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AB185372

Anti-RPS23 antibody

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(1 Publication)

Rabbit Polyclonal RPS23 antibody. Suitable for IHC-P, WB, ICC/IF and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human 40S ribosomal protein S23 aa 1-100.

View Alternative Names

Small ribosomal subunit protein uS12, 40S ribosomal protein S23, RPS23

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-RPS23 antibody (AB185372)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-RPS23 antibody (AB185372)

Immunohistochemical analysis of paraffin-embedded Human stomach tissue, labeling RPS23 using ab185372 at 1/20 dilution.

Immunocytochemistry/ Immunofluorescence - Anti-RPS23 antibody (AB185372)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-RPS23 antibody (AB185372)

MCF7 cells stained for RPS23 (green) using ab185372 at 2 μg/ml dilution in ICC/IF.

Western blot - Anti-RPS23 antibody (AB185372)
  • WB

Supplier Data

Western blot - Anti-RPS23 antibody (AB185372)

Lane 1:

Western blot - Anti-RPS23 antibody (ab185372)

Lane 2:

Western blot - Anti-RPS23 antibody (ab185372) at 0.4 µg/mL

Lane 1:

Molecular weight ladder

Lane 2:

HEK-293 cell lysate

Predicted band size: 16 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, ICC/IF, IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human 40S ribosomal protein S23 aa 1-100. The exact immunogen used to generate this antibody is proprietary information.

P62266

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Ribosomal protein S23 (RPS23) is an important component of the 40S ribosomal subunit which plays a central role in protein synthesis. Also known simply as S23 this protein has a mass of approximately 15 kDa. RPS23 is ubiquitously expressed in different tissues reflecting its essential role in cellular function. It is highly conserved across species highlighting its importance in fundamental biological processes.
Biological function summary

RPS23 is critical in the assembly and structural stability of ribosomes. Within the ribosomal complex it contributes to the accurate decoding of messenger RNA (mRNA) during translation. RPS23 forms part of the small ribosomal subunit which recognizes and binds mRNA and transfer RNA (tRNA). Its position and structure facilitate correct alignment of the mRNA ensuring precise protein synthesis.

Pathways

RPS23 has essential roles in the protein synthesis pathway and is involved in the translation initiation complex. It interacts closely with other ribosomal proteins like RPS19 to enable the production of polypeptide chains from mRNA templates. Through this process RPS23 connects to cellular growth and differentiation pathways such as the mTOR signaling pathway which influences protein biosynthesis and cell survival.

Abnormalities in RPS23 can lead to disorders such as ribosomopathies and cancer. Mutations in RPS23 affect ribosome function and efficiency linking it to diseases that involve rapid cell proliferation. In cancer alterations in ribosomal biogenesis often correlate with aggressive tumor growth where RPS23 may interact with proteins such as p53 that regulate cell cycle and apoptosis. This highlights the significance of maintaining normal RPS23 functions for cellular homeostasis and disease prevention.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed : 23636399, PubMed : 25901680, PubMed : 25957688, PubMed : 28257692). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed : 23636399, PubMed : 25901680, PubMed : 25957688). 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 (PubMed : 23636399, PubMed : 25901680, PubMed : 25957688). 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 (PubMed : 23636399, PubMed : 25901680, PubMed : 25957688). Plays an important role in translational accuracy (PubMed : 28257692). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed : 34516797).
See full target information 40S ribosomal protein S23

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Analytical cellular pathology (Amsterdam) 2019:4265040 PubMed30838170

2019

Downregulation of PTPRK Promotes Cell Proliferation and Metastasis of NSCLC by Enhancing STAT3 Activation.

Applications

Unspecified application

Species

Unspecified reactive species

Xuting Xu,Dong Li,Jin Liu,Zhihong Ma,Huilian Huang,Lishan Min,Licheng Dai,Shunli Dong
View all publications

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