Mouse Anti-RPS3 Recombinant Antibody (CF374) (CBMAB-FT135LY)

Mouse

Human, Mouse, Rat

CF374

IgG1

ELISA, WB, IHC, IF, IP

ribosomal protein S3

Human, Mouse, Rat

IgG1

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Liquid

50% glycerol

0.02% sodium azide

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Ribosomal Protein S3

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, where it forms part of the domain where translation is initiated. The protein belongs to the S3P family of ribosomal proteins. Studies of the mouse and rat proteins have demonstrated that the protein has an extraribosomal role as an endonuclease involved in the repair of UV-induced DNA damage. The protein appears to be located in both the cytoplasm and nucleus but not in the nucleolus. Higher levels of expression of this gene in colon adenocarcinomas and adenomatous polyps compared to adjacent normal colonic mucosa have been observed. This gene is co-transcribed with the small nucleolar RNA genes U15A and U15B, which are located in its first and fifth introns, respectively. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012]

40S ribosomal protein S3, ribosomal protein S3, RPS3

Involved in translation as a component of the 40S small ribosomal subunit (PubMed:8706699).
Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413).
Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971).
Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345).
Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840).
Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571).
Enhances the uracil excision activity of UNG1 (PubMed:18973764).
Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764).
When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537).
Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931).
Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535).
Represses its own translation by binding to its cognate mRNA (PubMed:20217897).
Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744).
Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551).
Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002).
Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787).
Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408).

Biological Process apoptotic processIEA:UniProtKB-KW
Biological Process cell divisionIEA:UniProtKB-KW
Biological Process cellular response to DNA damage stimulusManual Assertion Based On ExperimentIEP:UniProtKB
Biological Process cellular response to hydrogen peroxideManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process cellular response to reactive oxygen speciesManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process cellular response to tumor necrosis factorManual Assertion Based On ExperimentIMP:CAFA
Biological Process chromosome segregationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process cytoplasmic translation1 PublicationIC:FlyBase
Biological Process DNA repairManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of DNA repairManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of protein ubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process negative regulation of translationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of activated T cell proliferationManual Assertion Based On ExperimentIMP:CAFA
Biological Process positive regulation of apoptotic signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of base-excision repairManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosisManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of DNA N-glycosylase activityManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of DNA repairManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of endodeoxyribonuclease activityManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of gene expressionManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of interleukin-2 productionManual Assertion Based On ExperimentIMP:CAFA
Biological Process positive regulation of intrinsic apoptotic signaling pathway in response to DNA damageManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of JUN kinase activityManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of microtubule polymerizationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of NF-kappaB transcription factor activityManual Assertion Based On ExperimentIMP:CAFA
Biological Process positive regulation of NIK/NF-kappaB signalingManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of protein-containing complex assemblyManual Assertion Based On ExperimentIMP:CAFA
Biological Process positive regulation of T cell receptor signaling pathwayManual Assertion Based On ExperimentIMP:CAFA
Biological Process regulation of apoptotic processManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process response to TNF agonistManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process spindle assemblyManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process translation1 PublicationNAS:UniProtKB
Biological Process translational initiation1 PublicationNAS:UniProtKB

Cytoplasm
Nucleus
Nucleus, nucleolus
Mitochondrion inner membrane
Cytoplasm, cytoskeleton, spindle
In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucleus in cells undergoing apoptosis (By similarity).
Nuclear translocation is induced by DNA damaging agents such as hydrogen peroxide (PubMed:17560175).
Accumulates in the mitochondrion in response to increased ROS levels (PubMed:23911537).
Localizes to the spindle during mitosis (PubMed:23131551).
Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661).

Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly.
Sumoylation by SUMO1 enhances protein stability through increased resistance to proteolysis. Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.
Phosphorylation at Thr-221 by CDK1 ^oCcurs mainly in G2/M phase (PubMed:21871177).
Phosphorylation by PRKCD occurs on a non-ribosomal-associated form which results in translocation of RPS3 to the nucleus and enhances its endonuclease activity (PubMed:19059439).
Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3 (PubMed:21399639).
Phosphorylation by MAPK is required for translocation to the nucleus following exposure of cells to DNA damaging agents such as hydrogen peroxide (PubMed:17560175).
Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation, enhances RPS3 endonuclease activity and suppresses RPS3-induced neuronal apoptosis (PubMed:20605787).
Ubiquitinated (PubMed:16314389).
This is prevented by interaction with HSP90 which stabilizes the protein (PubMed:16314389).
Monoubiquitinated at Lys-214 by ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide (PubMed:28065601, PubMed:28132843).
Ufmylated by UFL1.