HuD Antibody [M19B4] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:30 IHC1:500 IF1:500 FCM1:500

Application
WB, IP, IHC, IF, FCM

Reactivity
Human

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 Observed MW
42 kDa 40 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
HuD Antibody [M19B4] detects endogenous levels of total HuD protein.

Clone
M19B4

Synonym(s)
HUD, PNEM, ELAVL4, ELAV-like protein 4, Hu-antigen D, Paraneoplastic encephalomyelitis antigen HuD, HuD

Background
HuD (ELAVL4) is a neuron-enriched member of the ELAV family of RNA-binding proteins, featuring three RNA recognition motifs that enable preferential cytoplasmic localization and selective binding to AU-rich elements within the 3′ untranslated regions of numerous neuronal mRNAs. The protein’s N-terminal tandem RRMs and a third C-terminal RRM confer specificity for U-rich and AU-rich sequences, and this modular organization allows HuD to simultaneously engage multiple cis-elements in target 3′UTRs and to assemble higher-order ribonucleoprotein complexes with other RNA-binding proteins and translation factors. Through binding to AU-rich elements, HuD stabilizes neuronal transcripts by antagonizing mRNA decay mechanisms, which extends transcript half-life and increases steady-state protein expression of key factors involved in neurite extension, dendritic growth, synaptic plasticity, and injury-induced regeneration, establishing HuD as a central post-transcriptional regulator in neuronal development and adult neural plasticity. In neuroblastoma, HuD is specifically expressed in neuroblastic N- and I-type cells, where it interacts with multiple AU-rich destabilizing elements within the MYCN 3′UTR; overexpression of HuD in these cells blocks mRNA decay mediated by these elements and increases MYCN mRNA stability in vivo, raising steady-state MYCN levels, which connects HuD activity directly to the maintenance of an oncogenic transcription factor that supports cell proliferation and tumor aggressiveness. HuD is also a principal neuronal autoantigen in paraneoplastic encephalomyelitis and sensory neuropathy associated with small cell lung cancer, as ectopic expression of HuD in tumor cells provokes anti-Hu immune responses that cross-react with neuronal Hu proteins, linking HuD’s neuronal specificity to paraneoplastic neuroimmunological disease.

Background

HuD (ELAVL4) is a neuron-enriched member of the ELAV family of RNA-binding proteins, featuring three RNA recognition motifs that enable preferential cytoplasmic localization and selective binding to AU-rich elements within the 3′ untranslated regions of numerous neuronal mRNAs. The protein’s N-terminal tandem RRMs and a third C-terminal RRM confer specificity for U-rich and AU-rich sequences, and this modular organization allows HuD to simultaneously engage multiple cis-elements in target 3′UTRs and to assemble higher-order ribonucleoprotein complexes with other RNA-binding proteins and translation factors. Through binding to AU-rich elements, HuD stabilizes neuronal transcripts by antagonizing mRNA decay mechanisms, which extends transcript half-life and increases steady-state protein expression of key factors involved in neurite extension, dendritic growth, synaptic plasticity, and injury-induced regeneration, establishing HuD as a central post-transcriptional regulator in neuronal development and adult neural plasticity. In neuroblastoma, HuD is specifically expressed in neuroblastic N- and I-type cells, where it interacts with multiple AU-rich destabilizing elements within the MYCN 3′UTR; overexpression of HuD in these cells blocks mRNA decay mediated by these elements and increases MYCN mRNA stability in vivo, raising steady-state MYCN levels, which connects HuD activity directly to the maintenance of an oncogenic transcription factor that supports cell proliferation and tumor aggressiveness. HuD is also a principal neuronal autoantigen in paraneoplastic encephalomyelitis and sensory neuropathy associated with small cell lung cancer, as ectopic expression of HuD in tumor cells provokes anti-Hu immune responses that cross-react with neuronal Hu proteins, linking HuD’s neuronal specificity to paraneoplastic neuroimmunological disease.

References
https://pubmed.ncbi.nlm.nih.gov/11711535/ https://pubmed.ncbi.nlm.nih.gov/33922479/

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%