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AB316476

Recombinant Human ACE Protein Standard (His tag)

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Recombinant Human ACE Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for sELISA, SDS-PAGE.

View Alternative Names

CD143, DCP, DCP1, ACE, Angiotensin-converting enzyme, Dipeptidyl carboxypeptidase I, Kininase II

2 Images
Sandwich ELISA - Recombinant Human ACE Protein Standard (His tag) (AB316476)
  • sELISA

Supplier Data

Sandwich ELISA - Recombinant Human ACE Protein Standard (His tag) (AB316476)

Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL

SDS-PAGE - Recombinant Human ACE Protein Standard (His tag) (AB316476)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human ACE Protein Standard (His tag) (AB316476)

SDS-PAGE analysis of ab316476.

Key facts

Purity

>80% SDS-PAGE

Expression system

HEK 293 cells

Tags

His tag C-Terminus

Applications

SDS-PAGE, sELISA

applications

Biologically active

No

Accession

P12821

Animal free

Yes

Carrier free

No

Species

Human

Storage buffer

pH: 7.3 - 7.5 Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "sELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.

Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.

The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.

Sequence info

[{"sequence":null,"proteinLength":"Fragment","predictedMolecularWeight":"70.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P12821","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Angiotensin Converting Enzyme 1 also known as ACE1 or ACE is an important enzyme in the renin-angiotensin system. This enzyme exhibits a significant role in blood pressure regulation. ACE1 is a zinc-metallopeptidase with a molecular weight of approximately 130 kDa. It converts angiotensin I into the potent vasoconstrictor angiotensin II a critical function in cardiovascular physiology. ACE1 is widely expressed in endothelial cells particularly in the lungs kidneys and the small intestine.
Biological function summary

The enzyme generates angiotensin II by cleaving angiotensin I. Angiotensin II an important effector peptide impacts cardiovascular and renal systems influencing vasoconstriction and fluid balance. While not directly forming a complex ACE1's activity increases the potency of angiotensin II which binds to angiotensin II receptors to exert its effects therefore indirectly forming a functional signaling complex.

Pathways

ACE1 plays a central role in the renin-angiotensin system and the kallikrein-kinin system. The enzyme's activity boosts angiotensin II production which connects it to the regulation of blood pressure via the renin-angiotensin pathway. ACE1 also indirectly interacts with proteins like bradykinin by degrading them modulating kinin-related functions and influencing inflammation and tension in vascular smooth muscle.

Understanding ACE1 is important for addressing hypertension and congestive heart failure. ACE1's conversion of angiotensin I to angiotensin II means overactivity can cause elevated blood pressure leading to hypertension. This makes ACE inhibitors such as lisinopril and ramipril therapeutic for these conditions. Furthermore its connection with aldosterone production places ACE1 in relevance to heart failure as excessive aldosterone can cause detrimental remodeling of cardiac tissue.

Specifications

Form

Liquid

General info

Function

Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed : 15615692, PubMed : 20826823, PubMed : 2558109, PubMed : 4322742, PubMed : 7523412, PubMed : 7683654). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed : 10913258, PubMed : 1320019, PubMed : 1851160, PubMed : 19773553, PubMed : 7683654, PubMed : 7876104). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed : 11432860, PubMed : 1851160, PubMed : 19773553, PubMed : 23056909, PubMed : 4322742). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed : 15615692, PubMed : 2558109, PubMed : 4322742, PubMed : 6055465, PubMed : 6270633, PubMed : 7683654). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (PubMed : 15615692, PubMed : 6208535, PubMed : 6270633, PubMed : 656131). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (PubMed : 2982830, PubMed : 6270633, PubMed : 656131). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (PubMed : 26403559, PubMed : 7876104, PubMed : 8257427, PubMed : 8609242). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (PubMed : 18077343). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (PubMed : 11604391, PubMed : 16154999, PubMed : 19773553). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed : 10336644, PubMed : 2983326, PubMed : 7683654, PubMed : 9371719). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (PubMed : 10336644, PubMed : 19773553, PubMed : 7876104).. Angiotensin-converting enzyme, soluble form. Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.. Isoform Testis-specific. Isoform produced by alternative promoter usage that is specifically expressed in spermatocytes and adult testis, and which is required for male fertility (PubMed : 1651327, PubMed : 1668266). In contrast to somatic isoforms, only contains one catalytic domain (PubMed : 1651327, PubMed : 1668266). Acts as a dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of substrates (PubMed : 1668266, PubMed : 24297181). The identity of substrates that are needed for male fertility is unknown (By similarity). May also have a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. The GPIase activity was reported to be essential for the egg-binding ability of the sperm (By similarity). This activity is however unclear and has been challenged by other groups, suggesting that it may be indirect (By similarity).

Sequence similarities

Belongs to the peptidase M2 family.

Post-translational modifications

Angiotensin-converting enzyme, soluble form. Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769). Cleavage can take place at different sites of the juxtamembrane stalk region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769).. Phosphorylated by CK2 on Ser-1299; which allows membrane retention (PubMed:12386153). Phosphorylated on tyrosine residues on its extracellular part, promoting cleavage by secretase enzymes and formation of the soluble form (Angiotensin-converting enzyme, soluble form) (By similarity).

Product protocols

Target data

Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed : 15615692, PubMed : 20826823, PubMed : 2558109, PubMed : 4322742, PubMed : 7523412, PubMed : 7683654). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed : 10913258, PubMed : 1320019, PubMed : 1851160, PubMed : 19773553, PubMed : 7683654, PubMed : 7876104). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed : 11432860, PubMed : 1851160, PubMed : 19773553, PubMed : 23056909, PubMed : 4322742). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed : 15615692, PubMed : 2558109, PubMed : 4322742, PubMed : 6055465, PubMed : 6270633, PubMed : 7683654). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (PubMed : 15615692, PubMed : 6208535, PubMed : 6270633, PubMed : 656131). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (PubMed : 2982830, PubMed : 6270633, PubMed : 656131). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (PubMed : 26403559, PubMed : 7876104, PubMed : 8257427, PubMed : 8609242). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (PubMed : 18077343). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (PubMed : 11604391, PubMed : 16154999, PubMed : 19773553). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed : 10336644, PubMed : 2983326, PubMed : 7683654, PubMed : 9371719). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (PubMed : 10336644, PubMed : 19773553, PubMed : 7876104).. Angiotensin-converting enzyme, soluble form. Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.. Isoform Testis-specific. Isoform produced by alternative promoter usage that is specifically expressed in spermatocytes and adult testis, and which is required for male fertility (PubMed : 1651327, PubMed : 1668266). In contrast to somatic isoforms, only contains one catalytic domain (PubMed : 1651327, PubMed : 1668266). Acts as a dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of substrates (PubMed : 1668266, PubMed : 24297181). The identity of substrates that are needed for male fertility is unknown (By similarity). May also have a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. The GPIase activity was reported to be essential for the egg-binding ability of the sperm (By similarity). This activity is however unclear and has been challenged by other groups, suggesting that it may be indirect (By similarity).
See full target information ACE

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