AFG3-like protein 2 Recombinant Protein | AFG3L2 recombinant protein

Recombinant Human AFG3-like protein 2

Cat. Num. AAA1265281

• Gene Names: AFG3L2; SCA28; SPAX5
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: AFG3-like protein 2; Recombinant Human AFG3-like protein 2; Paraplegin-like protein; AFG3L2 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 550-759aa; Partial
• Sequence: ERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARLIDDEVRILINDAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGPRPFAEKSTYEEF
• Sequence Length: 797

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for AFG3L2 recombinant protein

ATP-dependent protease which is essential for axonal development.

Product Categories/Family for AFG3L2 recombinant protein

Metabolism

References

Identification and characterization of AFG3L2, a novel paraplegin-related gene.Banfi S., Bassi M.T., Andolfi G., Marchitiello A., Zanotta S., Ballabio A., Casari G., Franco B.Genomics 59:51-58(1999) Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia.Atorino L., Silvestri L., Koppen M., Cassina L., Ballabio A., Marconi R., Langer T., Casari G.J. Cell Biol. 163:777-787(2003) Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia.Koppen M., Metodiev M.D., Casari G., Rugarli E.I., Langer T.Mol. Cell. Biol. 27:758-767(2007) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Northeast structural genomics consortium target HR6741A.Northeast structural genomics consortium (NESG) Submitted (MAR-2012) to the PDB data bankEarly onset and slow progression of SCA28, a rare dominant ataxia in a large four-generation family with a novel AFG3L2 mutation.Edener U., Wollner J., Hehr U., Kohl Z., Schilling S., Kreuz F., Bauer P., Bernard V., Gillessen-Kaesbach G., Zuhlke C.Eur. J. Hum. Genet. 18:965-968(2010) Missense mutations in the AFG3L2 proteolytic domain account for approximately 1.5% of European autosomal dominant cerebellar ataxias.Cagnoli C., Stevanin G., Brussino A., Barberis M., Mancini C., Margolis R.L., Holmes S.E., Nobili M., Forlani S., Padovan S., Pappi P., Zaros C., Leber I., Ribai P., Pugliese L., Assalto C., Brice A., Migone N., Durr A., Brusco A.Hum. Mutat. 31:1117-1124(2010) Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28.Di Bella D., Lazzaro F., Brusco A., Plumari M., Battaglia G., Pastore A., Finardi A., Cagnoli C., Tempia F., Frontali M., Veneziano L., Sacco T., Boda E., Brussino A., Bonn F., Castellotti B., Baratta S., Mariotti C., Gellera C., Fracasso V., Magri S., Langer T., Plevani P., Di Donato S., Muzi-Falconi M., Taroni F.Nat. Genet. 42:313-321(2010) Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases.Pierson T.M., Adams D., Bonn F., Martinelli P., Cherukuri P.F., Teer J.K., Hansen N.F., Cruz P., Mullikin J.C., Blakesley R.W., Golas G., Kwan J., Sandler A., Fuentes Fajardo K., Markello T., Tifft C., Blackstone C., Rugarli E.I., Langer T., Gahl W.A., Toro C.PLoS Genet. 7:E1002325-E1002325(2011)

NCBI and Uniprot Product Information

• NCBI GI #: 300192933
• NCBI GeneID: 10939
• NCBI Accession #: NP_006787.2
• NCBI GenBank Nucleotide #: NM_006796.2
• UniProt Accession #: Q9Y4W6; Q6P1L0
• Molecular Weight: 50.8 kDa
• NCBI Official Full Name: AFG3-like protein 2
• NCBI Official Synonym Full Names: AFG3-like AAA ATPase 2
• NCBI Official Symbol: AFG3L2
• NCBI Official Synonym Symbols: SCA28; SPAX5
• NCBI Protein Information: AFG3-like protein 2
• UniProt Protein Name: AFG3-like protein 2
• Protein Family: AFG3-like protein
• UniProt Gene Name: AFG3L2
• UniProt Entry Name: AFG32_HUMAN

NCBI Description

This gene encodes a protein localized in mitochondria and closely related to paraplegin. The paraplegin gene is responsible for an autosomal recessive form of hereditary spastic paraplegia. This gene is a candidate gene for other hereditary spastic paraplegias or neurodegenerative disorders. [provided by RefSeq, Jul 2008]

Uniprot Description

AFG3L2: ATP-dependent protease which is essential for axonal development. Defects in AFG3L2 are the cause of spinocerebellar ataxia type 28 (SCA28). It is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA28 is an autosomal dominant cerebellar ataxia (ADCA) with a slow progressive course and no evidence of sensory involvement or cognitive impairment. Defects in AFG3L2 are the cause of spastic ataxia autosomal recessive type 5 (SPAX5). A neurodegenerative disorder characterized by early onset spasticity, peripheral neuropathy, ptosis, oculomotor apraxia, dystonia, cerebellar atrophy, and progressive myoclonic epilepsy.

Protein type: Mitochondrial; Membrane protein, multi-pass; EC 3.4.24.-; Chaperone; Cell development/differentiation; Protease; Membrane protein, integral

Chromosomal Location of Human Ortholog: 18p11

Cellular Component: integral to membrane; mitochondrial inner membrane; mitochondrion

Molecular Function: ATP binding; ATP-dependent peptidase activity; metalloendopeptidase activity; metallopeptidase activity; protein binding; unfolded protein binding; zinc ion binding

Biological Process: axonogenesis; cristae formation; mitochondrial fusion; muscle fiber development; myelination; nerve development; neuromuscular junction development; protein complex assembly; protein import into mitochondrial intermembrane space; regulation of multicellular organism growth; righting reflex

Disease: Spastic Ataxia 5, Autosomal Recessive; Spinocerebellar Ataxia 28