Retinoschisin (RS1) Recombinant Protein | RS1 recombinant protein

Recombinant Human Retinoschisin (RS1)

Cat. Num. AAA1178415

• Gene Names: RS1; RS; XLRS1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Retinoschisin (RS1); Recombinant Human Retinoschisin (RS1); X-linked juvenile retinoschisis protein; RS1 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: 24-224aa; Full Length of Mature Protein
• Sequence: STEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• 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 RS1 recombinant protein

May be active in cell adhesion processes during retinal development.

Product Categories/Family for RS1 recombinant protein

Cell adhesion

References

Positional cloning of the gene associated with X-linked juvenile retinoschisis.Sauer C.G., Gehrig A., Warneke-Wittstock R., Marquardt A., Ewing C.C., Gibson A., Lorenz B., Jurklies B., Weber B.H.Nat. Genet. 17:164-170(1997) The DNA sequence of the human X chromosome.Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.Nature 434:325-337(2005) Mapping of transcription start sites of human retina expressed genes.Roni V., Carpio R., Wissinger B.BMC Genomics 8:42-42(2007) Retinoschisin, the X-linked retinoschisis protein, is a secreted photoreceptor protein, and is expressed and released by Weri-Rb1 cells.Grayson C., Reid S.N., Ellis J.A., Rutherford A., Sowden J.C., Yates J.R., Farber D.B., Trump D.Hum. Mol. Genet. 9:1873-1879(2000) RS1, a discoidin domain-containing retinal cell adhesion protein associated with X-linked retinoschisis, exists as a novel disulfide-linked octamer.Wu W.W., Wong J.P., Kast J., Molday R.S.J. Biol. Chem. 280:10721-10730(2005) Japanese juvenile retinoschisis is caused by mutations of the XLRS1 gene.Hotta Y., Fujiki K., Hayakawa M., Ohta T., Fujimaki T., Tamaki K., Yokoyama T., Kanai A., Hirakata A., Hida T., Nishina S., Azuma N.Hum. Genet. 103:142-144(1998) Recurrent missense (R197C) and nonsense (Y89X) mutations in the XLRS1 gene in families with X-linked retinoschisis.Shastry B.S., Hejtmancik F.J., Trese M.T.Biochem. Biophys. Res. Commun. 256:317-319(1999) Assessment of RS1 in X-linked juvenile retinoschisis and sporadic senile retinoschisis.Gehrig A., White K., Lorenz B., Andrassi M., Clemens S., Weber B.H.Clin. Genet. 55:461-465(1999) Three widespread founder mutations contribute to high incidence of X-linked juvenile retinoschisis in Finland.Huopaniemi L., Rantala A., Forsius H., Somer M., de la Chapelle A., Alitalo T.Eur. J. Hum. Genet. 7:368-376(1999) X-linked retinoschisis with a novel substitutive amino acid (P193S) in XLRS1.Duval P.-A., Marlhens F., Griffoin J.-M., Millet P., Arnaud B., Hamel C.P.Hum. Mutat. 13:259-259(1999) Identification of four novel mutations of the XLRS1 gene in Japanese patients with X-linked juvenile retinoschisis.Mashima Y., Shinoda K., Ishida S., Ozawa Y., Kudoh J., Iwata T., Oguchi Y., Shimizu N.3.0.CO;2-0>Hum. Mutat. 13:338-338(1999) Novel mutations in XLRS1 causing retinoschisis, including first evidence of putative leader sequence change.Hiriyanna K.T., Bingham E.L., Yashar B.M., Ayyagari R., Fishman G., Small K.W., Weinberg D.V., Weleber R.G., Lewis R.A., Andreasson S., Richards J.E., Sieving P.A.3.0.CO;2-D>Hum. Mutat. 14:423-427(1999) X-linked retinoschisis in a female with a heterozygous RS1 missense mutation.Saldana M., Thompson J., Monk E., Trump D., Long V., Sheridan E.Am. J. Med. Genet. A 143:608-609(2007) Clinical features of X linked juvenile retinoschisis in Chinese families associated with novel mutations in the RS1 gene.Li X., Ma X., Tao Y.Mol. Vis. 13:804-812(2007) Clinical and genetic findings in Hungarian patients with X-linked juvenile retinoschisis.Lesch B., Szabo V., Kanya M., Somfai G.M., Vamos R., Varsanyi B., Pamer Z., Knezy K., Salacz G., Janaky M., Ferencz M., Hargitai J., Papp A., Farkas A.Mol. Vis. 14:2321-2332(2008)

NCBI and Uniprot Product Information

• NCBI GI #: 10835083
• NCBI GeneID: 6247
• NCBI Accession #: NP_000321.1
• NCBI GenBank Nucleotide #: NM_000330.3
• UniProt Accession #: O15537; Q0QD39
• Molecular Weight: 27 kDa
• NCBI Official Full Name: retinoschisin
• NCBI Official Synonym Full Names: retinoschisin 1
• NCBI Official Symbol: RS1
• NCBI Official Synonym Symbols: RS; XLRS1
• NCBI Protein Information: retinoschisin
• UniProt Protein Name: Retinoschisin
• Protein Family: Homeobox protein
• UniProt Gene Name: RS1
• UniProt Synonym Gene Names: XLRS1
• UniProt Entry Name: XLRS1_HUMAN

NCBI Description

This gene encodes an extracellular protein that plays a crucial role in the cellular organization of the retina. The encoded protein is assembled and secreted from photoreceptors and bipolar cells as a homo-oligomeric protein complex. Mutations in this gene are responsible for X-linked retinoschisis, a common, early-onset macular degeneration in males that results in a splitting of the inner layers of the retina and severe loss in vision. [provided by RefSeq, Oct 2008]

Uniprot Description

RS1: a highly conserved extracellular protein essential for proper retinal structure. Must interact with L-type voltage-gated calcium channels (L-VGCCs) correctly so that the photoreceptor cells in the eye can function properly. Genetic mutations in RS1 cause X-linked retinoschisis (XLRS) and early onset of macular degeneration. Interacts with the L-VGCCa1D subunit, regulating its activity. The expression and secretion of retinoschisin are modulated by circadian rhythms, peaking at night and diminishing during the day.

Protein type: Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: Xp22.13

Cellular Component: extracellular space; extrinsic to plasma membrane

Molecular Function: phosphatidylinositol 3-phosphate binding; phosphatidylinositol-3,4,5-triphosphate binding; phosphatidylinositol-3,4-bisphosphate binding; phosphatidylinositol-4,5-bisphosphate binding; phosphatidylinositol-5-phosphate binding; phosphatidylserine binding

Biological Process: adaptation of rhodopsin mediated signaling; cell adhesion; multicellular organismal development; visual perception

Disease: Retinoschisis 1, X-linked, Juvenile