Spermatogenesis-defective protein 39 homolog Recombinant Protein | VIPAS39 recombinant protein

Recombinant Human Spermatogenesis-defective protein 39 homolog

Cat. Num. AAA1418195

• Gene Names: VIPAS39; SPE39; VIPAR; SPE-39; VPS16B; hSPE-39; C14orf133
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Spermatogenesis-defective protein 39 homolog; Recombinant Human Spermatogenesis-defective protein 39 homolog; VPS33B-interacting protein in apical-basolateral polarity regulator; VPS33B-interacting protein in polarity and apical restriction; VIPAS39 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: 1-493aa; Full Length
• Sequence: MNRTKGDEEEYWNSSKFKAFTFDDEDDELSQLKESKRAVNSLRDFVDDDDDDDLERVSWSGEPVGSISWSIRETAGNSGSTHEGREQLKSRNSFSSYAQLPKPTSTYSLSSFFRGRTRPGSFQSLSDALSDTPAKSYAPELGRPKGEYRDYSNDWSPSDTVRRLRKGKVCSLERFRSLQDKLQLLEEAVSMHDGNVITAVLIFLKRTLSKEILFRELEVRQVALRHLIHFLKEIGDQKLLLDLFRFLDRTEELALSHYREHLNIQDPDKRKEFLKTCVGLPFSAEDSAHIQDHYTLLERQIIIEANDRHLESAGQTEIFRKHPRKASILNMPLVTTLFYSCFYHYTEAEGTFSSPVNLKKTFKIPDKQYVLTALAARAKLRAWNDVDALFTTKNWLGYTKKRAPIGFHRVVEILHKNNAPVQILQEYVNLVEDVDTKLNLATKFKCHDVVIDTYRDLKDRQQLLAYRSKVDKGSAEEEKIDALLSSSQIRWKN
• Sequence Length: 493

• 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 VIPAS39 recombinant protein

May play a role in vesicular trafficking during spermatogenesis. Plays a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes. May play a role in epithelial polarization through stabilization of apical membrane protein content, possibly via the RAB11A-dependent apical recycling pathway. Also involved in direct or indirect transcriptional regulation of E-cadherin.

References

Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and analysis of human chromosome 14.Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.Nature 421:601-607(2003) 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) SPE-39 family proteins interact with the HOPS complex and function in lysosomal delivery.Zhu G.D., Salazar G., Zlatic S.A., Fiza B., Doucette M.M., Heilman C.J., Levey A.I., Faundez V., L'hernault S.W.Mol. Biol. Cell 20:1223-1240(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) Mutations in VIPAR cause an arthrogryposis, renal dysfunction and cholestasis syndrome phenotype with defects in epithelial polarization.Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y., Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B., Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P., Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H., Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P.Nat. Genet. 42:303-312(2010) On the endosomal function and gene nomenclature of human SPE-39.L'Hernault S.W., Faundez V.Nat. Genet. 43:176-176(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)

NCBI and Uniprot Product Information

• NCBI GI #: 300934874
• NCBI GeneID: 63894
• NCBI Accession #: NP_001180243.1
• NCBI GenBank Nucleotide #: NM_001193314.1
• UniProt Accession #: Q9H9C1; O95434; Q9H7E1; Q9H9I9; B4DPI6
• Molecular Weight: 73 kDa
• NCBI Official Full Name: spermatogenesis-defective protein 39 homolog isoform 1
• NCBI Official Synonym Full Names: VPS33B interacting protein, apical-basolateral polarity regulator, spe-39 homolog
• NCBI Official Symbol: VIPAS39
• NCBI Official Synonym Symbols: SPE39; VIPAR; SPE-39; VPS16B; hSPE-39; C14orf133
• NCBI Protein Information: spermatogenesis-defective protein 39 homolog
• UniProt Protein Name: Spermatogenesis-defective protein 39 homolog
• Protein Family: Spermatogenesis-defective protein
• UniProt Gene Name: VIPAS39
• UniProt Synonym Gene Names: C14orf133; SPE39; VIPAR; hSPE-39
• UniProt Entry Name: SPE39_HUMAN

NCBI Description

This gene encodes a protein involved in the sorting of lysosomal proteins. Mutations in this gene are associated with ARCS2 (arthrogryposis, renal dysfunction, and cholestasis-2). Alternative splicing results in multiple transcript variants.[provided by RefSeq, Jul 2010]

Uniprot Description

VIPAS39: a protein of unknown function. Two splice-variant isoforms have been described.

Protein type: Vesicle

Chromosomal Location of Human Ortholog: 14q24.3

Cellular Component: cytoplasm; cytoplasmic membrane-bound vesicle; early endosome; late endosome; recycling endosome

Molecular Function: protein binding

Biological Process: cell differentiation; endosome to lysosome transport; intracellular protein transport; regulation of transcription, DNA-dependent; spermatogenesis; transcription, DNA-dependent

Disease: Arthrogryposis, Renal Dysfunction, And Cholestasis 2