SPG7 Antibody (YA8277)
(Synonyms: CAR; CMAR; PGN; SPG5C)SPG7 Antibody (YA8277) is a Mouse-derived and non-conjugated IgG2a monoclonal antibody, targeting to SPG7.
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Host:
Mouse
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Isotype:
IgG
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Application:
ICC/IF, FC
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Reactivity :
Human, Mouse, Rat
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Formulation:
Spplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Conjugation:
Non-conjugated
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Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
FC
FC: Flow Cytometry
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|---|---|---|
| Dilution Ratio | 1:50-100 | 1:100 |
Product Details
SPG7 Antibody (YA8277) is a Mouse-derived and non-conjugated IgG2a monoclonal antibody, targeting to SPG7.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Calculated Molecular Weight Predicted band size: 88.1 kDa
Human recombinant protein fragment corresponding to amino acids 300-573 of human SPG7 prodduced in E.coli.
Endogenous
Affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Spplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% 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
SPG7 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. SPG7 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 exerts a dual role in the mitochondrial inner membrane: it mediates the processing of specific regulatory proteins and ensures protein quality control by degrading misfolded polypeptides. 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. 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. Also regulates mitochondrial calcium by catalyzing degradation of MCU. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function[1][2][3][4][5].
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Subcellular Localization
Mitochondrion inner membrane
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Expression
Tissue_Specificity: Ubiquitous -
Isoforms & Post-Translational Modification
Q9UQ90 has two isomers: Q9UQ90-1: 88235 Da (predicted); Q9UQ90-2: 53940 Da (predicted).
Upon import into the mitochondrion, the N-terminal transit peptide is cleaved by the mitochondrial-processing peptidase (MPP) to generate an intermediate form which undergoes a second proteolytic cleavage mediated by proteases AFG3L2 removing an additional N-terminal fragment to generate the proteolytically active mature form -
Subunit
Forms heterooligomers with AFG3L2; the m-AAA protease is composed of heterohexamers of AFG3L2 and SPG7 (PubMed:14623864, PubMed:28396416)
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SwissProt ID
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Synonyms
CAR; CMAR; PGN; SPG5C
Documentation
References
[1]. Kremmidiotis G, et al. Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein. Genomics. 2001 Aug;76(1-3):58-65. [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]. Hurst S, et al. SPG7 targets the m-AAA protease complex to process MCU for uniporter assembly, Ca(2+) influx, and regulation of mitochondrial permeability transition pore opening. J Biol Chem. 2019 Jul 12;294(28):10807-10818. [Content Brief]
[4]. Casari G, et al. Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell. 1998 Jun 12;93(6):973-83. [Content Brief]
[5]. Shanmughapriya S, et al. SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability Transition Pore. Mol Cell. 2015 Oct 1;60(1):47-62. [Content Brief]
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