HuR/ELAVL1 Antibody [G18B5] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

Lane 1: 293T, Lane 2: HCT116, Lane 3: 3T3, Lane 4: RAW264.7

Usage Information

Dilution
WB1:1000 IP1:50 IF1:50 FCM1:50

Application
WB, IP, IF, FCM

Reactivity
Human, Mouse, Rat, Monkey

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
30 kDa

Datasheet & SDS

Biological Description

Specificity
HuR/ELAVL1 Antibody [G18B5] detects endogenous levels of total HuR/ELAVL1 protein.

Clone
G18B5

Synonym(s)
ELAV-like protein 1; Hu-antigen R (HuR); ELAVL1; HUR

Background
HuR (ELAVL1), the ubiquitously expressed founding member of the ELAV RNA-binding protein family alongside neuron-restricted HuB/C/D, orchestrates post-transcriptional control of mRNA stability and translation through high-affinity binding to AU- and U-rich elements (AREs) predominantly in 3' untranslated regions of proliferation, survival, and inflammatory transcripts. Its three tandem RNA recognition motifs (RRMs) form a compact clamp that engages adenine-rich stems with subnanomolar affinity, while nuclear localization/importin signals enable continuous nucleocytoplasmic shuttling that accelerates upon transcriptional stress when HuR relocates to cytoplasmic stress granules. Upon binding, HuR recruits poly(A)-binding protein to circularize mRNAs and excludes decay factors like TTP/BRF1 while promoting cap-dependent translation via eIF4A/eIF4G interactions; concurrently, HuR antagonizes miR-16 and let-7 repression by sterically occluding RISC loading sites on VEGF, c-Myc, and COX-2 transcripts. Phosphorylation by p38 MAPK, PKC, or Chk2 at S202/S220/S318 shifts HuR from nuclear retention to cytoplasmic export, coupling genotoxic stress or inflammatory cues to rapid proteome reprogramming. Physiologically, HuR sustains intestinal epithelial barrier integrity through sustained Mcl-1 expression, coordinates T cell activation via CD154 stabilization, and buffers oncogenic stress in fibroblasts, positioning it as the master regulator of immediate-early gene expression that researchers target with RRM-competitive quinazolines or antisense morpholinos to dissect translational buffering in tumorspheres. Cytoplasmic sequestration via 14-3-3 binding provides feedback inhibition, while HuR auto-regulates its own decay through intronic ARE binding. Overexpression drives chemoresistance through MDR1 stabilization while deficiency impairs wound healing through VEGF deficits.

Background

HuR (ELAVL1), the ubiquitously expressed founding member of the ELAV RNA-binding protein family alongside neuron-restricted HuB/C/D, orchestrates post-transcriptional control of mRNA stability and translation through high-affinity binding to AU- and U-rich elements (AREs) predominantly in 3' untranslated regions of proliferation, survival, and inflammatory transcripts. Its three tandem RNA recognition motifs (RRMs) form a compact clamp that engages adenine-rich stems with subnanomolar affinity, while nuclear localization/importin signals enable continuous nucleocytoplasmic shuttling that accelerates upon transcriptional stress when HuR relocates to cytoplasmic stress granules. Upon binding, HuR recruits poly(A)-binding protein to circularize mRNAs and excludes decay factors like TTP/BRF1 while promoting cap-dependent translation via eIF4A/eIF4G interactions; concurrently, HuR antagonizes miR-16 and let-7 repression by sterically occluding RISC loading sites on VEGF, c-Myc, and COX-2 transcripts. Phosphorylation by p38 MAPK, PKC, or Chk2 at S202/S220/S318 shifts HuR from nuclear retention to cytoplasmic export, coupling genotoxic stress or inflammatory cues to rapid proteome reprogramming. Physiologically, HuR sustains intestinal epithelial barrier integrity through sustained Mcl-1 expression, coordinates T cell activation via CD154 stabilization, and buffers oncogenic stress in fibroblasts, positioning it as the master regulator of immediate-early gene expression that researchers target with RRM-competitive quinazolines or antisense morpholinos to dissect translational buffering in tumorspheres. Cytoplasmic sequestration via 14-3-3 binding provides feedback inhibition, while HuR auto-regulates its own decay through intronic ARE binding. Overexpression drives chemoresistance through MDR1 stabilization while deficiency impairs wound healing through VEGF deficits.

References
https://pubmed.ncbi.nlm.nih.gov/9628881/ https://pubmed.ncbi.nlm.nih.gov/21948791/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%