RPL36 Antibody Kit

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Leader in Biomolecular Solutions for Life Science [One Step]RPL36 Antibody Kit Catalog No.: RK05700 Basic Information Background Catalog No. Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit RK05700 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 Applications that is a component of the 60S subunit. The protein belongs to the L36E family of WB ribosomal proteins. It is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding Cross-Reactivity ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed Human, Mouse, Rat through the genome. Observed MW 15kDa Calculated MW 12kDa Category Antibody kit Product Information Component & Recommended Dilutions Source Catalog No. Product Name Dilutions Rabbit RK05700-1 RPL36 Rabbit pAb 1:1000 dilution Purification RK05700-2 HRP Goat Anti-Rabbit IgG (H+L) 1:10000 dilution Affinity purification Storage Store at -20℃. Avoid freeze / thaw Immunogen Information cycles. Buffer: PBS with 0.02% sodium azide, Gene ID Swiss Prot 50% glycerol, pH7.3. 25873 Q9Y3U8 Avoid repeated freeze-thaw cycles. Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 1-105 Contact of human RPL36 (NP_056229.2). www.abclonal.com Synonyms RPL36;L36 Validation Data Western blot analysis of extracts of various cells, using RPL36 antibody (A7793) at 1:1000 dilution ratio through one-step method. Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

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Micrornas Mediated Regulation of the Ribosomal Proteins and Its Consequences on the Global Translation of Proteins
cells Review microRNAs Mediated Regulation of the Ribosomal Proteins and Its Consequences on the Global Translation of Proteins Abu Musa Md Talimur Reza 1,2 and Yu-Guo Yuan 1,3,* 1 Jiangsu Co-Innovation Center of Prevention and Control of Important Animal Infectious Diseases and Zoonoses, College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China; [email protected] 2 Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawi´nskiego5a, 02-106 Warsaw, Poland 3 Jiangsu Key Laboratory of Zoonosis/Joint International Research Laboratory of Agriculture and Agri-Product Safety, The Ministry of Education of China, Yangzhou University, Yangzhou 225009, China * Correspondence: [email protected]; Tel.: +86-514-8797-9228 Abstract: Ribosomal proteins (RPs) are mostly derived from the energy-consuming enzyme families such as ATP-dependent RNA helicases, AAA-ATPases, GTPases and kinases, and are important structural components of the ribosome, which is a supramolecular ribonucleoprotein complex, composed of Ribosomal RNA (rRNA) and RPs, coordinates the translation and synthesis of proteins with the help of transfer RNA (tRNA) and other factors. Not all RPs are indispensable; in other words, the ribosome could be functional and could continue the translation of proteins instead of lacking in some of the RPs. However, the lack of many RPs could result in severe defects in the biogenesis of ribosomes, which could directly inﬂuence the overall translation processes and global expression of the proteins leading to the emergence of different diseases including cancer. While microRNAs (miRNAs) are small non-coding RNAs and one of the potent regulators of the post-transcriptional 0 gene expression, miRNAs regulate gene expression by targeting the 3 untranslated region and/or coding region of the messenger RNAs (mRNAs), and by interacting with the 50 untranslated region, Citation: Reza, A.M.M.T.; Yuan, Y.-G.
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Patterns of Ribosomal Protein Expression Specify Normal and Malignant Human Cells Joao C
Guimaraes and Zavolan Genome Biology (2016) 17:236 DOI 10.1186/s13059-016-1104-z RESEARCH Open Access Patterns of ribosomal protein expression specify normal and malignant human cells Joao C. Guimaraes* and Mihaela Zavolan* Abstract Background: Ribosomes are highly conserved molecular machines whose core composition has traditionally been regarded as invariant. However, recent studies have reported intriguing differences in the expression of some ribosomal proteins (RPs) across tissues and highly specific effects on the translation of individual mRNAs. Results: To determine whether RPs are more generally linked to cell identity, we analyze the heterogeneity of RP expression in a large set of human tissues, primary cells, and tumors. We find that about a quarter of human RPs exhibit tissue-specific expression and that primary hematopoietic cells display the most complex patterns of RP expression, likely shaped by context-restricted transcriptional regulators. Strikingly, we uncover patterns of dysregulated expression of individual RPs across cancer types that arise through copy number variations and are predictive for disease progression. Conclusions: Our study reveals an unanticipated plasticity of RP expression across normal and malignant human cell types and provides a foundation for future characterization of cellular behaviors that are orchestrated by specific RPs. Keywords: Ribosomal proteins, Ribosome heterogeneity, Translation, Hematopoiesis, Cancer Background Indeed, many feedback mechanisms have been discov- Protein synthesis is at the core of cellular life. It is car- ered that link the production of different ribosomal ried out by the ribosome, a highly conserved molecular components to maintain an appropriate stoichiometry machine with the same basic architecture in all free- [7]; a number of RPs act in negative feedback loops to living organisms [1–3].
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Suppl.Table 1 (Sample Description).Psd
Y+MCx upregulated over Y+SSCx (Change call ≥ 66%; average change p-value of all I/MI calls ≤0.001, P calls min. ≥2/3 in Y+MCx) 103 Probe Avg. Avg. Avg. Set ID Gene Title Gene Symbol SLR ± SD (n=9) SLR ± SD (n=4) SLR ± SD (n=9) Y+Cx ± SD Cx V ± SD Cx I-VI ± SD 1455913_x_at transthyretin Ttr 4.07 ± 0.54 1.92 ± 1.84 1.17 ± 1.83 1425466_at RIKEN cDNA 4930538C18 gene 4930538C18Rik 2.55 ± 1.36 -0.51 ± 0.76 0.00 ± 0.35 1434544_at RIKEN cDNA 1110025L05 gene 1110025L05Rik 1.18 ± 0.74 -0.01 ± 0.13 0.13 ± 0.33 1433570_s_at RIKEN cDNA C030004C14 gene C030004C14Rik 0.88 ± 0.88 -0.18 ± 0.44 0.12 ± 0.32 1424443_at transmembrane 6 superfamily member 1 Tm6sf1 0.72 ± 0.52 -0.11 ± 0.09 0.27 ± 0.28 1427183_at epidermal growth factor-containing fibulin-like extracellular matrix protein 1 Efemp1 0.72 ± 0.21 0.02 ± 0.23 0.40 ± 0.24 1454064_a_at ring finger protein 138 Rnf138 0.72 ± 0.53 0.19 ± 0.28 -0.04 ± 0.20 1417002_at RIKEN cDNA 0610012G03 gene 0610012G03Rik 0.71 ± 0.44 -0.13 ± 0.18 0.08 ± 0.22 1418188_a_at RIKEN cDNA 2210401K01 gene 2210401K01Rik 0.68 ± 0.37 0.31 ± 0.33 -0.90 ± 1.11 1451317_at RIKEN cDNA 9430020E02 gene 9430020E02Rik 0.68 ± 0.32 -0.14 ± 0.44 0.34 ± 0.40 1417972_s_at RIKEN cDNA 1500019J17 gene 1500019J17Rik 0.65 ± 0.34 0.09 ± 0.25 -0.04 ± 0.11 1436064_x_at ribosomal protein S24 Rps24 0.65 ± 0.39 -0.13 ± 0.09 -0.23 ± 0.22 1438403_s_at RIKEN cDNA 2210401K01 gene 2210401K01Rik 0.64 ± 0.36 0.90 ± 0.48 -1.42 ± 1.15 1424018_at histidine triad nucleotide binding protein Hint 0.63 ± 0.43 -0.06 ± 0.02 0.01 ± 0.25 1416427_at cyclin I Ccni 0.62 ±
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Alt-RPL36 Downregulates the PI3K-AKT-Mtor Signaling Pathway by Interacting with TMEM24
bioRxiv preprint doi: https://doi.org/10.1101/2020.03.04.977314; this version posted November 9, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Alt-RPL36 downregulates the PI3K-AKT-mTOR signaling pathway by interacting with TMEM24 Xiongwen Cao1,2,5, Alexandra Khitun1,2,5, Yang Luo1,2, Zhenkun Na1,2, Thitima Phoodokmai3, Khomkrit Sappakhaw3, Elizabeth Olatunji2, Chayasith Uttamapinant3, Sarah A. Slavoff1,2,4* 1Department of Chemistry, Yale University, New Haven, Connecticut 06520, United States 2Chemical Biology Institute, Yale University, West Haven, Connecticut 06516, United States 3School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand 4Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06529, United States 5These authors contributed equally *Correspondence: [email protected] Abstract Thousands of previously unannotated small and alternative open reading frames (alt-ORFs) have recently been revealed in the human genome, and hundreds are now known to be required for cell proliferation. Many alt-ORFs are co-encoded with proteins of known function in multicistronic human genes, but the functions of only a handful are currently known in molecular detail. Using a proteomic strategy for discovery of unannotated short open reading frames in human cells, we report the detection of alt-RPL36, a 148-amino acid protein co-encoded with and overlapping human RPL36 (ribosomal protein L36). Alt-RPL36 partially localizes to the endoplasmic reticulum, where it interacts with TMEM24, which transports the phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] precursor phosphatidylinositol from the endoplasmic reticulum to the plasma membrane.
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Autocrine IFN Signaling Inducing Profibrotic Fibroblast Responses By
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Vaccine-Increased Seq ID Unigene ID Uniprot ID Gene Names
BMJ Publishing Group Limited (BMJ) disclaims all liability and responsibility arising from any reliance Supplemental material placed on this supplemental material which has been supplied by the author(s) J Immunother Cancer Vaccine-Increased Seq ID Unigene ID Uniprot ID Gene Names 1_HSPA1A_3303 Hs.274402 P0DMV8 HSPA1A HSP72 HSPA1 HSX70 100_AKAP17A_8227 Hs.522572 Q02040 AKAP17A CXYorf3 DXYS155E SFRS17A XE7 1000_H2AFY_9555 Hs.420272 O75367 H2AFY MACROH2A1 1001_ITPK1_3705 Hs.308122 Q13572 ITPK1 1002_PTPN11_5781 Hs.506852 Q06124 PTPN11 PTP2C SHPTP2 1003_EIF3J_8669 Hs.404056 O75822 EIF3J EIF3S1 PRO0391 1004_TRIP12_9320 Hs.591633 Q14669 TRIP12 KIAA0045 ULF 1006_YEATS2_55689 Hs.632575 Q9ULM3 YEATS2 KIAA1197 1007_SEL1L3_23231 Hs.479384 Q68CR1 SEL1L3 KIAA0746 1008_IDH1_3417 Hs.593422 O75874 IDH1 PICD 101_HSPH1_10808 Hs.36927 Q92598 HSPH1 HSP105 HSP110 KIAA0201 1010_LDLR_3949 Hs.213289 P01130 LDLR 1011_FAM129B_64855 Hs.522401 Q96TA1 NIBAN2 C9orf88 FAM129B 1012_MAP3K5_4217 Hs.186486 Q99683 MAP3K5 ASK1 MAPKKK5 MEKK5 1013_NEFH_4744 Hs.198760 P12036 NEFH KIAA0845 NFH 1014_RAP1B_5908 Hs.369920 P61224 RAP1B OK/SW-cl.11 1015_MCCC1_56922 Hs.47649 Q96RQ3 MCCC1 MCCA 1017_MT1E_4493 Hs.534330 P04732 MT1E 1022_TXNDC5_81567 Hs.150837 Q8NBS9 TXNDC5 TLP46 UNQ364/PRO700 1023_STRA13_201254 Hs.37616 O14503 BHLHE40 BHLHB2 DEC1 SHARP2 STRA13 1024_NPEPPS_9520 Hs.443837 P55786 NPEPPS PSA 1025_YIPF6_286451 Hs.82719 Q96EC8 YIPF6 1026_CLIP1_6249 Hs.524809 P30622 CLIP1 CYLN1 RSN 1027_SRSF7_6432 Hs.309090 Q16629 SRSF7 SFRS7 103_RPS25_6230 Hs.512676 P62851 RPS25 1031_SOCS7_30837
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