Angiotensin I Converting Enzyme (ACE) Recombinant Protein | ACE recombinant protein

Recombinant Angiotensin I Converting Enzyme (ACE)

Cat. Num. AAA2011111

• Gene Names: Ace; CD143; AW208573
• Applications: SDS-Page, Western Blot, ELISA, Immunoprecipitation
• Purity: > 95%
• Synonyms: Angiotensin I Converting Enzyme (ACE); Recombinant Angiotensin I Converting Enzyme (ACE); ACE recombinant protein

• Host: E Coli
• Purity/Purification: > 95%
• Form/Format: Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
• Sequence: The target protein is fused with two N-terminal Tags, His-tag and MBP-tag, its sequence is listed below.; MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIA VEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDE ALKDAQTGST SGSGHHHHHH SAGLVPRGST AIGMKETAAA KFERQHMDSP DLGTLEVLFQ GPLGSEF-YQGICPP VARNETHFDA GAKFHIPNVT PYIRYFVSFV LQFQFHQALC KEAGHQGPLH QCDIYQSAQA GAKLKQVLQA GCSRPWQEVL KDLVGSD
• Sequence Length: 732

• Applicable Applications for ACE recombinant protein: SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
• Organism: Mus musculus (Mouse)
• Expression System: Prokaryotic expression
• Residues: Tyr504~Asp597 (Accession # P09470) with two N-terminal Tags, His-tag and MBP-tag
• Subcellular Location: Angiotensin-converting enzyme, soluble form: Secreted. Cell membrane; Single-pass type I membrane protein
• Endotoxin Level: <1.0EU per 1ug (determined by the LAL method)
• Predicted Isoelectric Point: 5.9
• Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.
• Preparation and Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.; Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

SDS-Page

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: 55.2kDa
• 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; kininase II; dipeptidyl peptidase; dipeptidyl carboxypeptidase I
• UniProt Protein Name: Angiotensin-converting enzyme
• Protein Family: Acetylcholinesterase
• 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; vesicle; endosome; external side of plasma membrane

Molecular Function: zinc ion binding; metallopeptidase activity; 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; lytic transglycosylase activity; galactosidase activity; hexosaminidase activity; bradykinin receptor binding; exopeptidase activity; mannosidase activity

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