Microtubule-associated protein 1S Recombinant Protein | MAP1S recombinant protein

Recombinant Human Microtubule-associated protein 1S

Cat. Num. AAA1265455

• Gene Names: MAP1S; MAP8; BPY2IP1; C19orf5; VCY2IP1; VCY2IP-1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Microtubule-associated protein 1S; Recombinant Human Microtubule-associated protein 1S; BPY2-interacting protein 1; Microtubule-associated protein 8; Variable charge Y chromosome 2-interacting protein 1; VCY2-interacting protein 1; VCY2IP-1; MAP1S 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: 794-1053. Partial
• Sequence: LSDSDPVPLAPGAADSDEDTEGFGVPRHDPLPDPLKVPPPLPDPSSICMVDPEMLPPKTARQTENVSRTRKPLARPNSRAAAPKATPVAAAKTKGLAGGDRASRPLSARSEPSEKGGRAPLSRKSSTPKTATRGPSGSASSRPGVSATPPKSPVYLDLAYLPSGSSAHLVDEEFFQRVRALCYVISGQDQRKEEGMRAVLDALLASKQHWDRDLQVTLIPTFDSVAMHTWYAETHARHQALGITVLGSNSMVSMQDDAFP

• 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 MAP1S recombinant protein

Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles.

Product Categories/Family for MAP1S recombinant protein

Apoptosis

References

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Genet. 36:40-45(2004) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) The DNA sequence and biology of human chromosome 19.Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.Nature 428:529-535(2004) Identification of immuno-peptidmics that recognized by tumor-reactive CTL generated from TIL of colon cancer patients.Shichijo S., Itoh K.Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity.Liu L., McKeehan W.L.Genomics 79:124-136(2002) Novel complex integrating mitochondria and the microtubular cytoskeleton with chromosome remodeling and tumor suppressor RASSF1 deduced by in silico homology analysis, interaction cloning in yeast, and colocalization in cultured cells.Liu L., Amy V., Liu G., McKeehan W.L.2.0.CO;2>In Vitro Cell. Dev. Biol. Anim. 38:582-594(2002) RASSF1A interacts with microtubule-associated proteins and modulates microtubule dynamics.Dallol A., Agathanggelou A., Fenton S.L., Ahmed-Choudhury J., Hesson L., Vos M.D., Clark G.J., Downward J., Maher E.R., Latif F.Cancer Res. 64:4112-4116(2004) Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein.Liu L., Vo A., Liu G., McKeehan W.L.Biochem. Biophys. Res. Commun. 332:670-676(2005) Specificity of the methylation-suppressed A isoform of candidate tumor suppressor RASSF1 for microtubule hyperstabilization is determined by cell death inducer C19ORF5.Liu L., Vo A., McKeehan W.L.Cancer Res. 65:1830-1838(2005) Distinct structural domains within C19ORF5 support association with stabilized microtubules and mitochondrial aggregation and genome destruction.Liu L., Vo A., Liu G., McKeehan W.L.Cancer Res. 65:4191-4201(2005) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain.Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L., Benedikz E., Sundstroem E.Biochem. Biophys. Res. Commun. 361:127-132(2007) Depletion of the Ras association domain family 1, isoform A-associated novel microtubule-associated protein, C19ORF5/MAP1S, causes mitotic abnormalities.Dallol A., Cooper W.N., Al-Mulla F., Agathanggelou A., Maher E.R., Latif F.Cancer Res. 67:492-500(2007) MAP1 structural organization in Drosophila in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site.Zou B., Yan H., Kawasaki F., Ordway R.W.Biochem. J. 414:63-71(2008) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. IIIJ. Proteome Res. 7:1346-1351(2008) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.Mol. Cell. Proteomics 8:1751-1764(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) 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) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) Nemitin, a novel Map8/Map1s interacting protein with Wd40 repeats.Wang W., Lundin V.F., Millan I., Zeng A., Chen X., Yang J., Allen E., Chen N., Bach G., Hsu A., Maloney M.T., Kapur M., Yang Y.PLoS ONE 7:E33094-E33094(2012) 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) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 816197590
• NCBI GeneID: 55201
• NCBI Accession #: NP_001295292.1
• NCBI GenBank Nucleotide #: NM_001308363.1
• UniProt Accession #: Q66K74; Q27QB1; Q6NXF1; Q8N3L8; Q8N3W5; Q8NI88; Q96H94; Q96IT4; Q96SP8; Q9BRC6; Q9H928; B4DH53
• Molecular Weight: 31.7 kDa
• NCBI Official Full Name: microtubule-associated protein 1S isoform 2
• NCBI Official Synonym Full Names: microtubule associated protein 1S
• NCBI Official Symbol: MAP1S
• NCBI Official Synonym Symbols: MAP8; BPY2IP1; C19orf5; VCY2IP1; VCY2IP-1
• NCBI Protein Information: microtubule-associated protein 1S
• UniProt Protein Name: Microtubule-associated protein 1S
• Protein Family: Microtubule-associated protein
• UniProt Gene Name: MAP1S
• UniProt Synonym Gene Names: BPY2IP1; C19orf5; MAP8; VCY2IP1; MAP-1S; VCY2-interacting protein 1; VCY2IP-1
• UniProt Entry Name: MAP1S_HUMAN

Uniprot Description

BPY2-IP1: Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule-organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles. Belongs to the MAP1 family.

Protein type: Microtubule-binding; Apoptosis

Chromosomal Location of Human Ortholog: 19p13.11

Cellular Component: cell junction; cell projection; cell soma; cytoplasm; cytosol; dendrite; microtubule; nucleolus; nucleus; perinuclear region of cytoplasm; spindle; synapse

Molecular Function: actin filament binding; beta-tubulin binding; deoxyribonuclease activity; DNA binding; identical protein binding; microtubule binding; protein binding; tubulin binding

Biological Process: apoptosis; autophagy; brain development; microtubule bundle formation; mitochondrion transport along microtubule; nervous system development; neurite morphogenesis