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Mouse Anti-ACE Recombinant Antibody (V2-179255) (CBMAB-A0527-YC)


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Summary

Host Animal
Mouse
Specificity
Mouse
Clone
V2-179255
Antibody Isotype
IgG2a
Application
ELISA, WB

Basic Information

Immunogen
KLH conjugated synthetic peptide selected from human ACE
Specificity
Mouse
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:10,000
ELISA1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Ascites
Preservative
0.09% sodium azide
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Angiotensin I Converting Enzyme
Introduction
ACE is an enzyme involved in catalyzing the conversion of angiotensin I into a physiologically active peptide angiotensin II. Angiotensin II is a potent vasopressor and aldosterone-stimulating peptide that controls blood pressure and fluid-electrolyte bal
Entrez Gene ID
11421
UniProt ID
P09470
Alternative Names
Angiotensin I Converting Enzyme; Angiotensin I Converting Enzyme (Peptidyl-Dipeptidase A) 1; Dipeptidyl Carboxypeptidase I; CD143 Antigen; Kininase II; DCP1; DCP; Angiotensin Converting Enzyme, Somatic Isoform; Angiotensin-Converting Enzyme;
Function
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.
Biological Process
Amyloid-beta metabolic process
Angiotensin maturation
Antigen processing and presentation of peptide antigen via MHC class I
Arachidonic acid secretion
Blood vessel diameter maintenance
Blood vessel remodeling
Cell proliferation in bone marrow
Heart contraction
Hematopoietic stem cell differentiation
Hormone catabolic process
Kidney development
Mononuclear cell proliferation
Negative regulation of gap junction assembly
Negative regulation of gene expression
Negative regulation of protein binding
Neutrophil mediated immunity
Peptide catabolic process
Positive regulation of peptidyl-cysteine S-nitrosylation
Positive regulation of peptidyl-tyrosine autophosphorylation
Positive regulation of protein binding
Positive regulation of protein tyrosine kinase activity
Positive regulation of systemic arterial blood pressure
Posttranscriptional regulation of gene expression
Proteolysis
Regulation of angiotensin metabolic process
Regulation of blood pressure
Regulation of hematopoietic stem cell proliferation
Regulation of renal output by angiotensin
Regulation of smooth muscle cell migration
Regulation of systemic arterial blood pressure by renin-angiotensin
Regulation of vasoconstriction
Spermatogenesis
Cellular Location
Secreted; Cell membrane; Cytoplasm. Detected in both cell membrane and cytoplasm in neurons.
Involvement in disease
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.
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).
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.
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.
Topology
Extracellular: 30-1256 aa
Helical: 1257-1277 aa
Cytoplasmic: 1278-1306 aa
PTM
Phosphorylated by CK2 on Ser-1299; which allows membrane retention.
More Infomation

Santos, M. C., Toson, N. S., Pimentel, M. C., Bordignon, S. A., Mendez, A. S., & Henriques, A. T. (2020). Polyphenols composition from leaves of Cuphea spp. and inhibitor potential, in vitro, of angiotensin I-converting enzyme (ACE). Journal of ethnopharmacology, 255, 112781.

Oh, J. Y., Kim, E. A., Lee, H., Kim, H. S., Lee, J. S., & Jeon, Y. J. (2019). Antihypertensive effect of surimi prepared from olive flounder (Paralichthys olivaceus) by angiotensin-I converting enzyme (ACE) inhibitory activity and characterization of ACE inhibitory peptides. Process Biochemistry, 80, 164-170.

Abachi, S., Bazinet, L., & Beaulieu, L. (2019). Antihypertensive and angiotensin-I-converting enzyme (ACE)-inhibitory peptides from fish as potential cardioprotective compounds. Marine drugs, 17(11), 613.

Bhaskar, B., Ananthanarayan, L., & Jamdar, S. (2019). Purification, identification, and characterization of novel angiotensin I-converting enzyme (ACE) inhibitory peptides from alcalase digested horse gram flour. LWT, 103, 155-161.

Deng, Z., Liu, Y., Wang, J., Wu, S., Geng, L., Sui, Z., & Zhang, Q. (2018). Antihypertensive effects of two novel angiotensin I-converting enzyme (ACE) inhibitory peptides from Gracilariopsis lemaneiformis (Rhodophyta) in spontaneously hypertensive rats (SHRs). Marine drugs, 16(9), 299.

Auwal, S. M., Zarei, M., Tan, C. P., Basri, M., & Saari, N. (2018). Enhanced physicochemical stability and efficacy of angiotensin I-converting enzyme (ACE)-inhibitory biopeptides by chitosan nanoparticles optimized using Box-Behnken design. Scientific reports, 8(1), 1-11.

Hanafi, M. A., Hashim, S. N., Chay, S. Y., Ebrahimpour, A., Zarei, M., Muhammad, K., ... & Saari, N. (2018). High angiotensin-I converting enzyme (ACE) inhibitory activity of Alcalase-digested green soybean (Glycine max) hydrolysates. Food Research International, 106, 589-597.

Liu, C., Fang, L., Min, W., Liu, J., & Li, H. (2018). Exploration of the molecular interactions between angiotensin-I-converting enzyme (ACE) and the inhibitory peptides derived from hazelnut (Corylus heterophylla Fisch.). Food chemistry, 245, 471-480.

Daskaya-Dikmen, C., Yucetepe, A., Karbancioglu-Guler, F., Daskaya, H., & Ozcelik, B. (2017). Angiotensin-I-converting enzyme (ACE)-inhibitory peptides from plants. Nutrients, 9(4), 316.

Paiva, L., Lima, E., Neto, A. I., & Baptista, J. (2017). Angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant properties, phenolic content and amino acid profiles of Fucus spiralis L. protein hydrolysate fractions. Marine drugs, 15(10), 311.

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For research use only. Not intended for any clinical use.

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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