AFG3L2 Antibody
(Synonyms: Mitochondrial inner membrane m-AAA protease component AFG3L2, AFG3-like protein 2, Paraplegin-like protein, AFG3L2)AFG3L2 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to AFG3L2.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, IP
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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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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IP
IP: Immunoprecipitation
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|---|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 | 1:10-50 |
Product Details
AFG3L2 Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to AFG3L2.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 89 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: 88 kDa
Purified recombinant protein of human AFG3L2.
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 30% glycerol, and 0.01% sodium azide.
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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
AFG3L2 is a Catalytic component of the m-AAA protease, a protease that plays a key role in proteostasis of inner mitochondrial membrane proteins, and which is essential for axonal and neuron development. AFG3L2 possesses both ATPase and protease activities: the ATPase activity is required to unfold substrates, threading them into the internal proteolytic cavity for hydrolysis into small peptide fragments. The m-AAA protease carries out quality control in the inner membrane of the mitochondria by mediating degradation of mistranslated or misfolded polypeptides. The m-AAA protease complex also promotes the processing and maturation of mitochondrial proteins, such as MRPL32/bL32m, PINK1 and SP7. Mediates protein maturation of the mitochondrial ribosomal subunit MRPL32/bL32m by catalyzing the cleavage of the presequence of MRPL32/bL32m prior to assembly into the mitochondrial ribosome. Required for SPG7 maturation into its active mature form after SPG7 cleavage by mitochondrial-processing peptidase (MPP). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Acts as a regulator of calcium in neurons by mediating degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU. Promotes the proteolytic degradation of GHITM upon hyperpolarization of mitochondria: progressive GHITM degradation leads to respiratory complex I degradation and broad reshaping of the mitochondrial proteome by AFG3L2. Also acts as a regulator of mitochondrial glutathione homeostasis by mediating cleavage and degradation of SLC25A39. SLC25A39 cleavage is prevented when SLC25A39 binds iron-sulfur. Also acts as a regulator of carnitine biosynthesis by mediating cleavage and degradation of SLC25A45. Involved in the regulation of OMA1-dependent processing of OPA1. May act by mediating processing of OMA1 precursor, participating in OMA1 maturation[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17].
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Subcellular Localization
Mitochondrion inner membrane
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Expression
Tissue_Specificity: Ubiquitous. Highly expressed in the cerebellar Purkinje cells. -
Isoforms & Post-Translational Modification
AFG3L2 has an amino acid length of 797, molecular weight is 88584 Da.
Upon import into the mitochondrion, the N-terminal transit peptide is cleaved to generate an intermediate form which undergoes autocatalytic proteolytic processing to generate the proteolytically active mature form. -
Subunit
Homohexamer.
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SwissProt ID
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Synonyms
Mitochondrial inner membrane m-AAA protease component AFG3L2, AFG3-like protein 2, Paraplegin-like protein, AFG3L2
Documentation
[1]. Augustin S, et al. An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell. 2009 Sep 11;35(5):574-85. [Content Brief]
[2]. Tsai CW, et al. Proteolytic control of the mitochondrial calcium uniporter complex. Proc Natl Acad Sci U S A. 2017 Apr 25;114(17):4388-4393. [Content Brief]
[3]. Ding B, et al. Dissecting Substrate Specificities of the Mitochondrial AFG3L2 Protease. Biochemistry. 2018 Jul 17;57(28):4225-4235. [Content Brief]
[4]. Richter U, et al. Mitochondrial stress response triggered by defects in protein synthesis quality control. Life Sci Alliance. 2019 Feb;2(1):. [Content Brief]
[5]. Puchades C, et al. Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease. Mol Cell. 2019 Sep 5;75(5):1073-1085.e6. [Content Brief]
[6]. Liu Y, et al. Autoregulatory control of mitochondrial glutathione homeostasis. Science. 2023 Nov 17;382(6672):820-828. [Content Brief]
[7]. Shi X, et al. Dual regulation of SLC25A39 by AFG3L2 and iron controls mitochondrial glutathione homeostasis. Mol Cell. 2024 Feb 15;84(4):802-810.e6. [Content Brief]
[8]. Dias MM, et al. SLC25A45 is required for mitochondrial uptake of methylated amino acids and de novo carnitine biosynthesis. Mol Cell. 2025 Nov 6;85(21):4093-4104.e8. [Content Brief]
[9]. Richter U, et al. Quality control of mitochondrial protein synthesis is required for membrane integrity and cell fitness. J Cell Biol. 2015 Oct 26;211(2):373-89. [Content Brief]
[10]. Ng KY, et al. Translation of MT-ATP6 pathogenic variants reveals distinct regulatory consequences from the co-translational quality control of mitochondrial protein synthesis. Hum Mol Genet. 2022 Apr 22;31(8):1230-1241. [Content Brief]
[11]. Greene AW, et al. Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment. EMBO Rep. 2012 Apr;13(4):378-85. [Content Brief]
[12]. Magri S, et al. Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation. Hum Mutat. 2018 Dec;39(12):2060-2071. [Content Brief]
[13]. König T, et al. The m-AAA Protease Associated with Neurodegeneration Limits MCU Activity in Mitochondria. Mol Cell. 2016 Oct 6;64(1):148-162. [Content Brief]
[14]. Patron M, et al. Regulation of mitochondrial proteostasis by the proton gradient. EMBO J. 2022 Aug 16;41(16):e110476. [Content Brief]
[15]. Duvezin-Caubet S, et al. OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria. Mol Biol Cell. 2007 Sep;18(9):3582-90. [Content Brief]
[16]. Consolato F, et al. m-AAA and i-AAA complexes coordinate to regulate OMA1, the stress-activated supervisor of mitochondrial dynamics. J Cell Sci. 2018 Apr 9;131(7):. [Content Brief]
[17]. Baderna V, et al. A novel AFG3L2 mutation close to AAA domain leads to aberrant OMA1 and OPA1 processing in a family with optic atrophy. Acta Neuropathol Commun. 2020 Jun 29;8(1):93. [Content Brief]
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