ACE sirna

ACE siRNA (Mouse)

Cat. Num. AAA8210081

• Gene Names: Ace; CD143; AW208573
• Reactivity: Mouse
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: ACE; ACE siRNA (Mouse); DCP1; Angiotensin-converting enzyme; Dipeptidyl carboxypeptidase I; Kininase II; CD antigen CD143; ACE sirna

• Host: Synthetic
• Reactivity: Mouse
• Specificity: ACE siRNA (Mouse) 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: 732

• Applicable Applications for ACE 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 mouse ACE 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 ACE sirna

siRNA to inhibit ACE expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 33468873
• NCBI GeneID: 11421
• NCBI Accession #: NP_033728.1
• NCBI GenBank Nucleotide #: NM_009598.2
• UniProt Accession #: P09470; P22967; Q6GTS2
• Molecular Weight: 84,047 Da
• NCBI Official Full Name: angiotensin-converting enzyme isoform 2
• NCBI Official Synonym Full Names: angiotensin I converting enzyme (peptidyl-dipeptidase A) 1
• NCBI Official Symbol: Ace
• NCBI Official Synonym Symbols: CD143; AW208573
• NCBI Protein Information: angiotensin-converting enzyme
• UniProt Protein Name: Angiotensin-converting enzyme
• Protein Family: Acetamidase
• UniProt Gene Name: Ace
• UniProt Synonym Gene Names: Dcp1; ACE
• UniProt Entry Name: ACE_MOUSE

Uniprot Description

ACE: Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR); also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Defects in ACE are a cause of renal tubular dysgenesis (RTD). RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new- onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH). A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. Belongs to the peptidase M2 family. 4 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, integral; Protease; EC 3.4.15.1

Cellular Component: extracellular space; membrane; brush border membrane; lysosome; cytoplasm; extracellular region; plasma membrane; integral to membrane; basal plasma membrane; endosome; vesicle; external side of plasma membrane

Molecular Function: metallopeptidase activity; zinc ion binding; carboxypeptidase activity; mitogen-activated protein kinase kinase binding; mannosyl-oligosaccharide mannosidase activity; metal ion binding; drug binding; actin binding; glucosidase activity; endopeptidase activity; mitogen-activated protein kinase binding; amylase activity; chloride ion binding; peptidyl-dipeptidase activity; tripeptidyl-peptidase activity; hydrolase activity; trehalase activity; peptidase activity; protein binding; fucosidase activity; galactosidase activity; lytic transglycosylase activity; hexosaminidase activity; bradykinin receptor binding; exopeptidase activity; mannosidase activity

Biological Process: vasoconstriction; organ regeneration; positive regulation of neurogenesis; positive regulation of protein binding; eating behavior; positive regulation of apoptosis; neutrophil mediated immunity; response to lipopolysaccharide; regulation of angiotensin metabolic process; positive regulation of systemic arterial blood pressure; sensory perception of pain; arachidonic acid secretion; proteolysis; regulation of systemic arterial blood pressure by renin-angiotensin; regulation of smooth muscle cell migration; peptide metabolic process; heart contraction; peptide catabolic process; beta-amyloid metabolic process; regulation of blood pressure; spermatogenesis; hormone catabolic process; kidney development; negative regulation of protein binding; alveolus development; positive regulation of inflammatory response