Recombinant Human 40S Ribosomal Protein S3 (RPS3) Protein (His-SUMO)

Name: Recombinant Human 40S Ribosomal Protein S3 (RPS3) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04012P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human 40S Ribosomal Protein S3 (RPS3) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P23396
Target Symbol	RPS3
Synonyms	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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	AVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA
Expression Range	2-243aa
Protein Length	Full Length of Mature Protein
Mol. Weight	42.6kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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

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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.