X-linked juvenile retinoschisis protein

For Research Use Only. Not for use in diagnostic procedures.

E Coli or Yeast or Baculovirus or Mammalian Cell

Greater than 90% as determined by SDS-PAGE. (lot specific)

Liquid containing glycerol

This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.

Sterile filter available upon request.

Low endotoxin available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of RS1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

May be active in cell adhesion processes during retinal development.

Cell Adhesion

(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)

27.1kD

retinoschisin 1

retinoschisin

Retinoschisin

XLRS1??[Similar Products]

XLRS1_HUMAN

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]

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

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)

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