ATP7A sirna

ATP7A siRNA (Rat)

Cat. Num. AAA8239839

• Gene Names: Atp7a; Mnk
• Reactivity: Rat
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: ATP7A; ATP7A siRNA (Rat); MNK; Copper-transporting ATPase 1; Copper pump 1; Menkes disease-associated protein homolog; ATP7A sirna

• Host: Synthetic
• Reactivity: Rat
• Specificity: ATP7A siRNA (Rat) is a target-specific 19-23 nt siRNA oligo duplexes designed to knock down gene expression.
• Purity/Purification: > 97%
• Form/Format: Lyophilized powder
• Sequence Length: 1492

• Applicable Applications for ATP7A sirna: RNA Interference (RNAi)
• Quality Control: Oligonucleotide synthesis is monitored base by base through trityl analysis to ensure appropriate coupling efficiency. The oligo is subsequently purified by affinity-solid phase extraction. The annealed RNA duplex is further analyzed by mass spectrometry to verify the exact composition of the duplex. Each lot is compared to the previous lot by mass spectrometry to ensure maximum lot-to-lot consistency.
• Directions for Use: We recommends transfection with 100 nM siRNA 48 to 72 hours prior to cell lysis. Before resuspending, briefly centrifuge the tube to ensure the lyophilized siRNA is at the bottom of the tube. Resuspend the siRNA oligos to an appropriate concentration with DEPC water. For each vial, suitable for 250 transfections in 24 well plate (20 pmol for each well).
• Components: We offer pre-designed sets of 3 different target-specific siRNA oligo duplexes of rat ATP7A gene. Each vial contains 5 nmol of lyophilized siRNA. The duplexes can be transfected individually or pooled together to achieve knockdown of the target gene, which is most commonly assessed by qPCR or western blot. Our siRNA oligos are also chemically modified (2'-OMe) at no extra charge for increased stability and enhanced knockdown in vitro and in vivo.
• Preparation and Storage: Shipped at 4 degree C. Store at -20 degree C for one year.

Related Product Information for ATP7A sirna

siRNA to inhibit ATP7A expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 16258817
• NCBI GeneID: 24941
• NCBI Accession #: NP_434690.1
• NCBI GenBank Nucleotide #: NM_052803.2
• UniProt Accession #: P70705
• Molecular Weight: 162,093 Da
• NCBI Official Full Name: copper-transporting ATPase 1
• NCBI Official Synonym Full Names: ATPase, Cu++ transporting, alpha polypeptide
• NCBI Official Symbol: Atp7a
• NCBI Official Synonym Symbols: Mnk
• NCBI Protein Information: copper-transporting ATPase 1
• UniProt Protein Name: Copper-transporting ATPase 1
• UniProt Gene Name: Atp7a
• UniProt Synonym Gene Names: Mnk
• UniProt Entry Name: ATP7A_RAT

NCBI Description

This gene encodes a transmembrane protein that functions in copper transport across membranes. The protein localizes to the trans-Golgi network, where it is predicted to supply copper to copper-dependent enzymes in the secretory pathway. The protein relocalizes to the plasma membrane under conditions of elevated extracellular copper and functions in the efflux of copper from cells. In human, mutations in this gene result in Menkes disease, X-linked cutis laxa, and occipital horn syndrome. [provided by RefSeq, Nov 2009]

Uniprot Description

ATP7A: a multi-pass membrane protein and cation transporting ATPase. A copper-transporter that may supply copper to copper-requiring proteins within the secretory pathway when localized in the trans-Golgi network. Cycles between the trans-Golgi network (TGN) and the plasma membrane. Predominantly found in the TGN and relocalizes to the plasma membrane in response to elevated extracellular copper levels where it functions in the efflux of copper from cells. Defects in ATP7A are the cause of Menkes syndrome (MD) and occipital horn syndrome (OHS). Six alternatively spliced isoforms have been described. The longest isoform has 6 transmembrane regions. Isoform 3, lacking all 6 transmembrane regions and 5 heavy-metal-associated (HMA) domains, is probably cytosolic. Isoform 6 lacks all transmembrane regions and 5 heavy-metal-associated (HMA) domains, but has a putative nuclear localization signal attached at the N-terminus.

Protein type: Vesicle; Chaperone; Transporter; Transporter, ion channel; Apoptosis; Membrane protein, multi-pass; Hydrolase; Membrane protein, integral; Cell development/differentiation; EC 3.6.3.54

Cellular Component: Golgi apparatus; neuron projection; endoplasmic reticulum; brush border membrane; basolateral plasma membrane; cell; integral to membrane; trans-Golgi network; secretory granule; trans-Golgi network transport vesicle; membrane; cell soma; perinuclear region of cytoplasm; late endosome; plasma membrane; cytoplasmic vesicle

Molecular Function: copper ion transmembrane transporter activity; copper ion binding; metal ion binding; copper-exporting ATPase activity; superoxide dismutase copper chaperone activity; ATP binding; copper-dependent protein binding

Biological Process: skin development; positive regulation of catalytic activity; hindlimb morphogenesis; extracellular matrix organization and biogenesis; collagen fibril organization; catecholamine metabolic process; dopamine metabolic process; norepinephrine biosynthetic process; metal ion transport; plasma membrane copper ion transport; tryptophan metabolic process; negative regulation of neuron apoptosis; central nervous system neuron development; positive regulation of oxidoreductase activity; mitochondrion organization and biogenesis; release of cytochrome c from mitochondria; response to iron(III) ion; dendrite morphogenesis; detoxification of copper ion; ATP metabolic process; elastic fiber assembly; regulation of gene expression; response to zinc ion; regulation of oxidative phosphorylation; cerebellar Purkinje cell differentiation; copper ion import; alveolus development; lactation; removal of superoxide radicals; pyramidal neuron development; locomotory behavior; norepinephrine metabolic process; peptidyl-lysine modification; epinephrine metabolic process; serotonin metabolic process; blood vessel development; negative regulation of metalloenzyme activity; hair follicle morphogenesis; cellular copper ion homeostasis; T-helper cell differentiation; in utero embryonic development; tyrosine metabolic process; positive regulation of metalloenzyme activity; copper ion transport; elastin biosynthetic process; pigmentation; response to copper ion; cartilage development; blood vessel remodeling; copper ion export; neurite morphogenesis