Anti-hnRNP D/AUF1/HNRNPD Antibody Picoband® (monoclonal, 4F3), PE Conjugate

Heterogeneous nuclear ribonucleoprotein D0 (HNRNPD) also known as AU-rich element RNA-binding protein 1 (AUF1) is a protein that in humans is encoded by the HNRNPD gene. It is mapped to 4q21.22. This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are nucleic acid binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. It localizes to both the nucleus and the cytoplasm. This protein is implicated in the regulation of mRNA stability. Alternative splicing of this gene results in four transcript variants.

ATP synthase D chain mitochondrial antibody|ATP synthase H+ transporting mitochondrial F1F0 subunit antibody|ATP synthase H+ transporting mitochondrial F1F0 subunit d antibody|ATP synthase subunit d antibody|ATP synthase subunit d, mitochondrial antibody|ATP synthase, H+ transporting, mitochondrial F0 complex, subunit d antibody|ATP5H antibody|ATP5H_HUMAN antibody|ATP5JD antibody|ATPase subunit d antibody|ATPQ antibody|mitochondrial antibody|My032 protein antibody

Mitochondrial membrane ATP synthase (F (1)F (0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F (1) - containing the extramembraneous catalytic core, and F (0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F (1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F (0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha (3)beta (3) subcomplex and subunit a/ATP6 static relative to the rotary elements.

1. Arao Y, Kuriyama R, Kayama F, Kato S (August 2000). "A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D". Arch. Biochem. Biophys. 380 (2): 228–36. 2. Sinsimer KS, Gratacós FM, Knapinska AM, Lu J, Krause CD, Wierzbowski AV, Maher LR, Scrudato S, Rivera YM, Gupta S, Turrin DK, De La Cruz MP, Pestka S, Brewer G (September 2008). "Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU-rich element-mediated mRNA decay". Mol. Cell. Biol. 28 (17): 5223–37. 3. Panda AC, Abdelmohsen K, Yoon JH, Martindale JL, Yang X, Curtis J, Mercken EM, Chenette DM, Zhang Y, Schneider RJ, Becker KG, de Cabo R, Gorospe M (Aug 2014). "RNA-binding protein AUF1 promotes myogenesis by regulating MEF2C expression levels". Mol Cell Biol. 34 (16): 3106–19.

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.

Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat<br>Immunohistochemistry (Paraffin-embedded Section), 0.5-1μg/ml, Human, Rat<br>Immunocytochemistry/Immunofluorescence, 4μg/ml, Human<br>Immunofluorescence, 4μg/ml, Human<br>Flow Cytometry (Fixed), 1-3μg/1x10⁶ cells, Human