Anti-DHX36 Antibody

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure. DHX36 (DEAH box protein 36), also known as MLE-like protein 1 and RNA helicase associated with AU-rich element ARE (RHAU), belongs to RNA helicase of the DEAH family and may function in sex development and spermatogenesis. It is expressed in testis and is evolutionary conserved with true orthologs in almost all animal species. DHX36 plays a role in degradation and deadenylation of mRNAs containing in their 3'-UTR the consensus ARE sequence element. DHX36 is required for early embryogenesis.

Rabbit polyclonal DHX36 antibody was raised against a 19 amino acid peptide near the carboxy terminus of human DHX36. The immunogen is located within the last 50 amino acids of DHX36.

Proposed to have a global role in regulating mRNA expression including transcriptional regulation and mRNA stability. Binds with high affinity to and resolves tetramolecular RNA and DNA quadruplex structures. Unwinds intramolecular quadruplexes derived from the ZIC1 and the MYC promoters. Binds to quadruplex structures in the promoters of YY1 and ALPL genes and regulates their expression. Binds to telomerase RNA template component (TERC) 5'-end (nucleotides 1-43) and unwinds an internal quadruplex formation in TERC 5'-end to promote P1 helix formation; the P1 helix acts as a template boundary ensuring accurate reverse transcription and is disrupted by quadruplex formation. May be involved in regulation of telomere length. Plays a role in degradation and deadenylation of mRNAs containing in their 3'-UTR the consensus ARE sequence element. May function in sex development and spermatogenesis. May play a role in ossification.

Nucleus. Cytoplasm. Chromosome, telomere . Isoform 1 preferentially localized to the nucleus and isoform 2 localized to the cytoplasm. However, partitioning of cellular localization between the nucleus and cytoplasm is not exclusive, as isoform 1 was also detected in the cytoplasm. Both isoforms were excluded from nucleoli. Localizes to cytoplasmic stress granules.