- 39-0600 - Invitrogen Antibodies ELAVL1 antibody

Submitted references RNA structural dynamics regulate early embryogenesis through controlling transcriptome fate and function.

Shi B, Zhang J, Heng J, Gong J, Zhang T, Li P, Sun BF, Yang Y, Zhang N, Zhao YL, Wang HL, Liu F, Zhang QC, Yang YG
Genome biology 2020 May 18;21(1):120

Abemaciclib Is Effective Against Pancreatic Cancer Cells and Synergizes with HuR and YAP1 Inhibition.

Dhir T, Schultz CW, Jain A, Brown SZ, Haber A, Goetz A, Xi C, Su GH, Xu L, Posey J 3rd, Jiang W, Yeo CJ, Golan T, Pishvaian MJ, Brody JR
Molecular cancer research : MCR 2019 Oct;17(10):2029-2041

A Translation-Activating Function of MIWI/piRNA during Mouse Spermiogenesis.

Dai P, Wang X, Gou LT, Li ZT, Wen Z, Chen ZG, Hua MM, Zhong A, Wang L, Su H, Wan H, Qian K, Liao L, Li J, Tian B, Li D, Fu XD, Shi HJ, Zhou Y, Liu MF
Cell 2019 Dec 12;179(7):1566-1581.e16

DAZL Regulates Germ Cell Survival through a Network of PolyA-Proximal mRNA Interactions.

Zagore LL, Sweet TJ, Hannigan MM, Weyn-Vanhentenryck SM, Jobava R, Hatzoglou M, Zhang C, Licatalosi DD
Cell reports 2018 Oct 30;25(5):1225-1240.e6

ALS-associated mutant FUS inhibits macroautophagy which is restored by overexpression of Rab1.

Soo KY, Sultana J, King AE, Atkinson R, Warraich ST, Sundaramoorthy V, Blair I, Farg MA, Atkin JD
Cell death discovery 2015;1:15030

A cytoplasmic RNA virus generates functional viral small RNAs and regulates viral IRES activity in mammalian cells.

Weng KF, Hung CT, Hsieh PT, Li ML, Chen GW, Kung YA, Huang PN, Kuo RL, Chen LL, Lin JY, Wang RY, Chen SJ, Tang P, Horng JT, Huang HI, Wang JR, Ojcius DM, Brewer G, Shih SR
Nucleic acids research 2014 Nov 10;42(20):12789-805

ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation.

Walker AK, Soo KY, Sundaramoorthy V, Parakh S, Ma Y, Farg MA, Wallace RH, Crouch PJ, Turner BJ, Horne MK, Atkin JD
PloS one 2013;8(11):e81170

Welander distal myopathy is caused by a mutation in the RNA-binding protein TIA1.

Hackman P, Sarparanta J, Lehtinen S, Vihola A, Evilä A, Jonson PH, Luque H, Kere J, Screen M, Chinnery PF, Åhlberg G, Edström L, Udd B
Annals of neurology 2013 Apr;73(4):500-9

Resveratrol, by modulating RNA processing factor levels, can influence the alternative splicing of pre-mRNAs.

Markus MA, Marques FZ, Morris BJ
PloS one 2011;6(12):e28926

Expression of HuR, COX-2, and survivin in lung cancers; cytoplasmic HuR stabilizes cyclooxygenase-2 in squamous cell carcinomas.

Kim GY, Lim SJ, Kim YW
Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc 2011 Oct;24(10):1336-47

BRCA1-IRIS overexpression abrogates UV-induced p38MAPK/p53 and promotes proliferation of damaged cells.

Chock K, Allison JM, Elshamy WM
Oncogene 2010 Sep 23;29(38):5274-85

Activity-dependent expression of ELAV/Hu RBPs and neuronal mRNAs in seizure and cocaine brain.

Tiruchinapalli DM, Caron MG, Keene JD
Journal of neurochemistry 2008 Dec;107(6):1529-43

Overexpression of the embryonic-lethal abnormal vision-like protein HuR in ovarian carcinoma is a prognostic factor and is associated with increased cyclooxygenase 2 expression.

Denkert C, Weichert W, Pest S, Koch I, Licht D, Köbel M, Reles A, Sehouli J, Dietel M, Hauptmann S
Cancer research 2004 Jan 1;64(1):189-95

HuR binding to cytoplasmic mRNA is perturbed by heat shock.

Gallouzi IE, Brennan CM, Stenberg MG, Swanson MS, Eversole A, Maizels N, Steitz JA
Proceedings of the National Academy of Sciences of the United States of America 2000 Mar 28;97(7):3073-8

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Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis of HeLa cells using Ms anti-HuR (Product # 39-0600).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Western blot analysis was performed on whole cell extracts (30 µg lysate) of HeLa (Lane 1), HCT 116 (Lane 2), Jurkat (Lane 3), MCF-7 (Lane 4), Hep G2 (Lane 5), A549 (Lane 6), and LNCaP (Lane 7). The blots were probed with Mouse Anti-HuR Monoclonal Antibody (Product # 39-0600, 2 µg/mL) and detected by chemiluminescence using Goat anti-Mouse IgG (H+L) Superclonal™ Secondary Antibody, HRP conjugate (Product # A28177, 0.25 µg/mL, 1:4000 dilution). A 38 kDa band corresponding to HuR was observed across the cell lines tested. Known quantity of protein samples were electrophoresed using Novex® NuPAGE® 4-12 % Bis-Tris gel (Product # NP0321BOX), XCell SureLock™ Electrophoresis System (Product # EI0002) and Novex® Sharp Pre-Stained Protein Standard (Product # LC5800). Resolved proteins were then transferred onto a nitrocellulose membrane with iBlot® 2 Dry Blotting System (Product # IB21001). The membrane was probed with the relevant primary and secondary Antibody following blocking with 5 % skimmed milk. Chemiluminescent detection was performed using Pierce™ ECL Western Blotting Substrate (Product # 32106).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Indirect immunofluorescent analysis of heat shock-induced cytoplasmic relocalization of HuR in HeLa cells using Zymed Ms anti-HuR (Product # 39-0600).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Immunofluorescence analysis of HuR was performed using 70% confluent log phase HeLa cells. The cells were fixed with 4% paraformaldehyde for 10 minutes, permeabilized with 0.1% Triton™ X-100 for 10 minutes, and blocked with 1% BSA for 1 hour at room temperature. The cells were labeled with HuR (3A2) Mouse Monoclonal Antibody (Product # 39-0600) at 1:250 dilution in 0.1% BSA and incubated for 3 hours at room temperature and then labeled with Goat anti-Mouse IgG (H+L) Superclonal™ Secondary Antibody, Alexa Fluor® 488 conjugate (Product # A28175) at a dilution of 1:2000 for 45 minutes at room temperature (Panel a: green). Nuclei (Panel b: blue) were stained with SlowFade® Gold Antifade Mountant with DAPI (Product # S36938). F-actin (Panel c: red) was stained with Rhodamine Phalloidin (Product # R415, 1:300). Panel d represents the merged image showing nuclear localization. Panel e shows the no primary antibody control. The images were captured at 60X magnification.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Detection of binding of endogenous HuR protein to specific RNA using Anti-HuR Antibody: RNA Immunoprecipitation (RIP) was performed using Anti-HuR Mouse Monoclonal Antibody (Product # 39-0600, 10 ul) on clarified whole cell lysate from 2 million HCT 116 cells. Normal Rabbit IgG was used as a negative IP control. RNA purified by RiboPure™ RNA Purification Kit (Product # AM1924) was analyzed by RT-PCR using the Power SYBR® Green RNA-to-CT™ 1-Step Kit (Product # 4389986) with RIP primer pairs over ACTB mRNA (positive) and GAPDH mRNA, U1 snRNA and 18s rRNA (negative). Data is presented as fold enrichment of the antibody signal versus the negative control IgG using the comparative CT method.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 4 Resveratrol does not influence the intracellular localization of splicing factors. Immunofluorescence results for HEK293 cells treated with 20 uM resveratrol for 18 h. Shown is immunofluorescent signal obtained for the specific splicing factor antibodies indicated. Left panel: untreated control cells. Right panel: resveratrol-treated cells. The nucleus was stained with DAPI. Shown are merged images of DAPI staining (blue) and splicing factor staining (red or green, depending on the secondary antibody used). Scale bar: 20 um.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 2 Formation of ER stress-induced TDP-43-positive stress granules is enhanced by salubrinal pre-treatment. HeLa cells were pre-treated for 2 h with either vehicle control, 50 uM salubrinal or 50 ug/mL cycloheximide and then stressed for an additional 1 h by treatment with vehicle control ( A ), 0.5 mM arsenite ( B ), or 10 uM thapsigargin ( C ) in the presence of the respective pre-treatment conditions. Cells were processed for immunocytochemistry using antibodies against TDP-43 (left panels) and HuR (middle panels). Merged images are shown on the right. Boxed regions in the main panels are shown magnified in the bottom left of each panel. ( D ) Quantification of the effect of aresenite or thapsigargin in the presence of salubrinal or cycloheximide on the formation of HuR-positive or HuR/TDP-43-positive cytoplasmic SGs. Results are expressed as mean +- SEM, n = 3, *p

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 7 Rab1 overexpression inhibits the recruitment of mFUS to SGs and reduces the size of SGs formed. ( a ) Neuro2a cells were transfected with HA-FUS (WT or mutant) for 18 h. Cells were fixed and immunostained with anti-TIAR antibodies, and counterstained with DAPI to identify the nucleus. Merge images between HA, TIAR and DAPI are shown. White arrows indicate SGs. Scale bar=10 mu m. ( b ) Quantification of the % of cells displaying co-localisation between FUS and TIAR, indicating recruitment of FUS to SGs, n =3. ( c ) Neuro2a cells were co-transfected with HA-FUS (WT or mutant) and CFP-Rab1 vectors (or CFP empty vector) for 18 h. Cells were fixed and immunostained with anti-HuR antibodies and counterstained with DAPI to identify the nucleus. Merge images between HA, HuR and DAPI are shown. White arrows indicate SGs. Scale bar=10 mu m. ( d ) Quantification of cells displaying co-localisation between FUS and HuR, indicating recruitment of FUS to SGs, n =3. ( e ) Quantification of the size of each SG formed ( mu m 2 ). The size of SG was scored from at least 40 SGs in each sample, n =3. Mean+-S.E.M. Two-paired Student t -test. * P

39-0600

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