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RPS23 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P62266 |
| Other Accession | P62268, P62267, Q3T199, NP_001016.1, G1SZ47 |
| Reactivity | Human |
| Predicted | Bovine, Mouse, Rabbit, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 15808 Da |
| Antigen Region | 1-30 aa |
| Gene ID | 6228 |
|---|---|
| Other Names | 40S ribosomal protein S23, RPS23 |
| Target/Specificity | This RPS23 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human RPS23. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | RPS23 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | RPS23 |
|---|---|
| Function | 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). |
| Cellular Location | Cytoplasm, cytosol. Cytoplasm Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6SA96}. Nucleus, nucleolus. Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity) {ECO:0000250|UniProtKB:Q6SA96, ECO:0000269|PubMed:25957688} |
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Provided below are standard protocols that you may find useful for product applications.
Background
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S12P family of ribosomal proteins. It is located in the cytoplasm. The protein shares significant amino acid similarity with S. cerevisiae ribosomal protein S28. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq].
References
Yu, Y., et al. Protein Sci. 14(6):1438-1446(2005)
Andersen, J.S., et al. Nature 433(7021):77-83(2005)
Kapp, L.D., et al. Annu. Rev. Biochem. 73, 657-704 (2004) :
Sampath, P., et al. Mol. Cell. Biol. 23(5):1509-1519(2003)
Kenmochi, N., et al. Genome Res. 8(5):509-523(1998)
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