MCU Antibody (YA10009)
(Synonyms: C10orf42, CCDC109A, MCU, HsMCU, Coiled-coil domain-containing protein 109A)MCU Antibody (YA10009) is a Rabbit-derived and non-conjugated IgG Monoclonal, Recombinant antibody, targeting to MCY.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 50% glycerol, 0.05% BSA, and 0.05% Proclin300.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 | 1:50-200 |
Product Details
MCU Antibody (YA10009) is a Rabbit-derived and non-conjugated IgG Monoclonal, Recombinant antibody, targeting to MCY.
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Host Rabbit
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Clonality Monoclonal,Recombinant
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 32 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 40 kDa
Synthetic peptide corresponding to human CCDC109A protein.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 50% glycerol, 0.05% BSA, and 0.05% Proclin300.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
MCU is a Channel-forming and calcium-conducting subunit of the mitochondrial inner membrane calcium uniporter complex (uniplex), which mediates calcium uptake into the mitochondrial matrix. MCU channel activity is regulated by the calcium-sensor subunits of the uniplex MICU1 and MICU2 (or MICU3). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates ATP production, cytoplasmic calcium signals and activation of cell death pathways. Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes. While dispensable for baseline homeostatic cardiac function, acts as a key regulator of short-term mitochondrial calcium loading underlying a 'fight-or-flight' response during acute stress: acts by mediating a rapid increase of mitochondrial calcium in pacemaker cells. Participates in mitochondrial permeability transition during ischemia-reperfusion injury (By similarity). Mitochondrial calcium uptake in skeletal muscle cells is involved in muscle size in adults (By similarity). Regulates synaptic vesicle endocytosis kinetics in central nerve terminal (By similarity). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Involved in antigen processing and presentation (By similarity)[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23].
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Subcellular Localization
Mitochondrion inner membrane
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Expression
Induction: MCU transcripts are down-regulated by microRNA miR-25. Down-regulation by miR-25 may protect cardiomyocytes against oxidative damage in cardiomyocytes. -
Isoforms & Post-Translational Modification
MCU has 3 isoforms, Q8NE86-1: amino acid length is 351, molecular weight is 39867 Da (predicted); Q8NE86-2: amino acid length is 330, molecular weight is 36996 Da (predicted); Q8NE86-3: amino acid length is 302, molecular weight is 35159 Da (predicted).
Phosphorylation by CaMK2 in heart leads to increased MCU current. The regulation of MCU by CaMK2 is however subject to discussion: another group was unable to reproduce these results. Phosphorylated on tyrosines by PTK2B/PYK2, promoting oligomerization. -
Subunit
Homotetramer.
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SwissProt ID
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Synonyms
C10orf42, CCDC109A, MCU, HsMCU, Coiled-coil domain-containing protein 109A
Documentation
References
[1]. Baughman JM, et al. Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature. 2011 Jun 19;476(7360):341-5. [Content Brief]
[2]. De Stefani D, et al. A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature. 2011 Jun 19;476(7360):336-40. [Content Brief]
[3]. Drago I, et al. Mitochondrial Ca2+ uptake contributes to buffering cytoplasmic Ca2+ peaks in cardiomyocytes. Proc Natl Acad Sci U S A. 2012 Aug 7;109(32):12986-91. [Content Brief]
[4]. Tarasov AI, et al. The mitochondrial Ca2+ uniporter MCU is essential for glucose-induced ATP increases in pancreatic β-cells. PLoS One. 2012;7(7):e39722. [Content Brief]
[5]. Alam MR, et al. Mitochondrial Ca2+ uptake 1 (MICU1) and mitochondrial ca2+ uniporter (MCU) contribute to metabolism-secretion coupling in clonal pancreatic β-cells. J Biol Chem. 2012 Oct 5;287(41):34445-54. [Content Brief]
[6]. Mallilankaraman K, et al. MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca(2+) uptake that regulates cell survival. Cell. 2012 Oct 26;151(3):630-44. [Content Brief]
[7]. Mallilankaraman K, et al. MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism. Nat Cell Biol. 2012 Dec;14(12):1336-43. [Content Brief]
[8]. Chaudhuri D, et al. MCU encodes the pore conducting mitochondrial calcium currents. Elife. 2013 Jun 4;2:e00704. [Content Brief]
[9]. Hoffman NE, et al. MICU1 motifs define mitochondrial calcium uniporter binding and activity. Cell Rep. 2013 Dec 26;5(6):1576-1588. [Content Brief]
[10]. Patron M, et al. MICU1 and MICU2 finely tune the mitochondrial Ca2+ uniporter by exerting opposite effects on MCU activity. Mol Cell. 2014 Mar 6;53(5):726-37. [Content Brief]
[11]. Lee Y, et al. Structure and function of the N-terminal domain of the human mitochondrial calcium uniporter. EMBO Rep. 2015 Oct;16(10):1318-33. [Content Brief]
[12]. Yoo J, et al. Cryo-EM structure of a mitochondrial calcium uniporter. Science. 2018 Aug 3;361(6401):506-511. [Content Brief]
[13]. Baradaran R, et al. Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters. Nature. 2018 Jul;559(7715):580-584. [Content Brief]
[14]. Paillard M, et al. MICU1 Interacts with the D-Ring of the MCU Pore to Control Its Ca(2+) Flux and Sensitivity to Ru360. Mol Cell. 2018 Nov 15;72(4):778-785.e3. [Content Brief]
[15]. Phillips CB, et al. The conserved aspartate ring of MCU mediates MICU1 binding and regulation in the mitochondrial calcium uniporter complex. Elife. 2019 Jan 15;8:. [Content Brief]
[16]. Wang Y, et al. Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter. Cell. 2019 May 16;177(5):1252-1261.e13. [Content Brief]
[17]. Fan M, et al. Structure and mechanism of the mitochondrial Ca(2+) uniporter holocomplex. Nature. 2020 Jun;582(7810):129-133. [Content Brief]
[18]. Wang Y, et al. Structural insights into the Ca(2+)-dependent gating of the human mitochondrial calcium uniporter. Elife. 2020 Aug 7;9:. [Content Brief]
[19]. Van Keuren AM, et al. Mechanisms of EMRE-Dependent MCU Opening in the Mitochondrial Calcium Uniporter Complex. Cell Rep. 2020 Dec 8;33(10):108486. [Content Brief]
[20]. Tsai CW, et al. Evidence supporting the MICU1 occlusion mechanism and against the potentiation model in the mitochondrial calcium uniporter complex. Proc Natl Acad Sci U S A. 2023 Apr 18;120(16):e2217665120. [Content Brief]
[21]. Rodríguez-Prados M, et al. MICU1 occludes the mitochondrial calcium uniporter in divalent-free conditions. Proc Natl Acad Sci U S A. 2023 May 9;120(19):e2218999120. [Content Brief]
[22]. Matesanz-Isabel J, et al. Functional roles of MICU1 and MICU2 in mitochondrial Ca(2+) uptake. Biochim Biophys Acta. 2016 Jun;1858(6):1110-7. [Content Brief]
[23]. Wu Y, et al. The mitochondrial uniporter controls fight or flight heart rate increases. Nat Commun. 2015 Jan 20;6:6081. [Content Brief]
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