Sesquipedalian-2 Recombinant Protein | FAM109B recombinant protein

Recombinant Human Sesquipedalian-2

Cat. Num. AAA1391034

• Gene Names: FAM109B; Ses2; IPIP27B
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Sesquipedalian-2; Recombinant Human Sesquipedalian-2; 27 kDa inositol polyphosphate phosphatase interacting protein B; IPIP27B; FAM109B recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-259aa; Full Length
• Sequence: MKLNERSVAHYALSDSPADHMGFLRTWGGPGTPPTPSGTGRRCWFVLKGNLLFSFESREGRAPLSLVVLEGCTVELAEAPVPEEFAFAICFDAPGVRPHLLAAEGPAAQEAWVKVLSRASFGYMRLVVRELESQLQDARQSLALQRRSSWKSVASRCKPQAPNHRAAGLENGHCLSKDSSPVGLVEEAGSRSAGWGLAEWELQGPASLLLGKGQSPVSPETSCFSTLHDWYGQEIVELRQCWQKRAQGSHSKCEEQDRP
• Sequence Length: 259

• 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 FAM109B recombinant protein

Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane.

Product Categories/Family for FAM109B recombinant protein

Cancer

References

A genome annotation-driven approach to cloning the human ORFeome.Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.Genome Biol. 5:R84.1-R84.11(2004) The DNA sequence of human chromosome 22.Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.Nature 402:489-495(1999) Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1.Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010) The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway.Noakes C.J., Lee G., Lowe M.Mol. Biol. Cell 22:606-623(2011)

NCBI and Uniprot Product Information

• NCBI GI #: 115583657
• NCBI GeneID: 150368
• NCBI Accession #: NP_001002034.2
• NCBI GenBank Nucleotide #: NM_001002034.2
• UniProt Accession #: Q6ICB4; Q3SXQ3; Q8N6L9
• Molecular Weight: 44.3 kDa
• NCBI Official Full Name: sesquipedalian-2
• NCBI Official Synonym Full Names: family with sequence similarity 109 member B
• NCBI Official Symbol: FAM109B
• NCBI Official Synonym Symbols: Ses2; IPIP27B
• NCBI Protein Information: sesquipedalian-2
• UniProt Protein Name: Sesquipedalian-2
• Protein Family: Sesquipedalian
• UniProt Gene Name: FAM109B
• UniProt Synonym Gene Names: Ses2; IPIP27B
• UniProt Entry Name: SESQ2_HUMAN

Uniprot Description

FAM109B: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Belongs to the sesquipedalian family.

Chromosomal Location of Human Ortholog: 22q13.2

Cellular Component: clathrin-coated vesicle; early endosome; recycling endosome; trans-Golgi network

Molecular Function: protein binding; protein homodimerization activity

Biological Process: endosome organization and biogenesis; receptor recycling; retrograde transport, endosome to Golgi