Recombinant Human RPS3 Protein

Name: Recombinant Human RPS3 Protein
Brand: Beta LifeScience
SKU: BLA-7927P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P23396
Synonym	40S ribosomal protein S3 fb13d09 FLJ26283 FLJ27450 IMR 90 ribosomal protein S3 MGC56088 MGC87870 OTTHUMP00000229804 OTTHUMP00000229805 OTTHUMP00000229874 OTTHUMP00000229877 OTTHUMP00000229878 OTTHUMP00000229879 OTTHUMP00000229880 OTTHUMP00000229882 OTTHUMP00000229883 OTTHUMP00000229886 Ribosomal protein S3 rps3 RS3_HUMAN S3 wu:fb13d09 zgc:56088
Description	Recombinant Human RPS3 Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHHSSGLVPRGSHMAVQISKKRKFVADGIFKAELNEFLTRELA EDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFP EGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESG AKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQG VLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGK PEPPAMPQPVPTA
Molecular Weight	29 kDa
Purity	Greater than 90% SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Involved in translation as a component of the 40S small ribosomal subunit. Has endonuclease activity and plays a role in repair of damaged DNA. Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA. Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS). Has also been shown to bind with similar affinity to intact and damaged DNA. Stimulates the N-glycosylase activity of the base excision protein OGG1. Enhances the uracil excision activity of UNG1. Also stimulates the cleavage of the phosphodiester backbone by APEX1. When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage. Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide. 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. Represses its own translation by binding to its cognate mRNA. Binds to and protects TP53/p53 from MDM2-mediated ubiquitination. Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization. Involved in induction of apoptosis through its role in activation of CASP8. 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. Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation.
Subcellular Location	Cytoplasm. Nucleus. Nucleus, nucleolus. Mitochondrion inner membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, spindle.
Protein Families	Universal ribosomal protein uS3 family
Database References	HGNC: 10420 OMIM: 600454 KEGG: hsa:6188 STRING: 9606.ENSP00000433821 UniGene: Hs.546286

Gene Functions References

Results found that BfrB subverts the host innate immune system by binding the NF-kappaB subunit RPS3 and promotes the survival of mycobacteria in macrophages by inhibiting cytokine production in host cells. PMID: 29018126
These results reveal that RPS3 upregulates XIAP independently of the NF-kappaB pathway in human breast cancer cells PMID: 29048653
Asn 165 residue of rpS3 is a critical site for N-linked glycosylation and passage through the ER-Golgi secretion pathway. PMID: 27384988
findings suggest that uS3 residing in the 40S ribosome might perform extra-ribosomal functions related to control of DNA quality PMID: 28334742
Short 5'UTR mRNAs are enriched with TISU (translation initiator of short 5'UTR), a 12-nucleotide element directing efficient scanning-independent translation. This study demonstrate that TISU is particularly dependent on eukaryotic initiation factor 1A (eIF1A) which interacts with both RPS3 and RPS10e. PMID: 28584194
Data show that ribosomal protein S3 (RPS3) knockdown decreased mitochondrial calcium uptake 1 protein (MICU1) expression. PMID: 26336993
Increased RPS3 expression is associated with osteosarcoma invasion. PMID: 25449781
RPS3, a component of basic translation machinery operates at initiation and most probably elongation of protein synthesis, is also implicated in various events of the cell life as an extraribosomal player. [Review] PMID: 24239944
These findings suggest that the secreted rpS3 protein is an indicator of malignant tumors. PMID: 24211576
rpS3 accumulates in the mitochondria to repair damaged DNA due to the decreased interaction between rpS3 and HSP90 in the cytosol. PMID: 23911537
rpS3 acts as a microtubule associated protein and regulates spindle dynamics during mitosis. PMID: 23131551
A novel radioresistance mechanism through functional orchestration of rpS3, TRAF2, and NF-kappaB in non-small cell lung cancer cells, is reported. PMID: 23188828
rpS3 is recruited to the DISC and plays a critical role in both genotoxic stress and cytokine induced apoptosis. PMID: 22510408
The phosphorylation of rpS3 by Cdk1 occurs at Thr221 during G2/M phase. PMID: 21871177
rpS3 is covalently modified by SUMO-1 and this post-translational modification regulates rpS3 function by increasing rpS3 protein stability. PMID: 21968017
Data show that the IKKbeta-dependent modification of a specific amino acid in RPS3 promoted specific NF-kappaB functions that underlie the molecular pathogenetic mechanisms of E. coli O157:H7. PMID: 21399639
PEP-1-rpS3 inhibits inflammatory response cytokines and enzymes by blocking NF-kappaB and MAP kinase, prompting the suggestion that PEP-1-rpS3 can be used as a therapeutic agent against skin inflammation. PMID: 20709134
when Flag-tagged rpS3 was transiently transfected into 293T cells, the level of endogenous rpS3 gradually decreased regardless of transcription PMID: 20217897
DNA pull-down assays using a 7,8-dihydro-8-oxoguanine duplex oligonucleotide as a substrate found that RPS3 acted as a scaffold for the additional binding of MDM2 and p53. PMID: 19656744
Electron paramagnetic resonance study reveals a putative iron-sulfur cluster in human rpS3 protein. PMID: 11911468
RPS3 is involved in apoptosis. PMID: 14988002
Using surface plasmon resonance technology, the authors show that ribosomal protein S3 positively interacts with the human base excision repair enzymes N-glycosylase/apurinic-apyrimidinic lyase OGG1 and APE/Ref-1. PMID: 15518571
The S3-K132A mutant retained the ability to cleave abasic DNA, but its capacity to bind 8-oxoG was abrogated completely. PMID: 16737853
PEP-1-rpS3 fusion protein can be used in protein therapy for various disorders related to UV, including skin aging and cancer PMID: 17140567
S3 is a key protein at the mRNA binding site neighboring mRNA downstream of the codon at the decoding site in the human ribosome. PMID: 17179743
hRpS3 may be involved in the uracil-excision pathway, probably by participating in the DNA repair mechanism to remove uracil generated by the deamination of cytosine in DNA, and by preventing C/G-->T/A transition mutations. PMID: 18973764
Protein S3 fragments neighboring mRNA during elongation and translation termination on the human ribosome PMID: 19088750
these results clearly show that arginine methylation of rpS3 plays a critical role in its import into the nucleolus, as well as in small subunit assembly of the ribosome. PMID: 19460357

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.