Recombinant Human Retinoschisin(RS1)

Code CSB-EP020534HUe0
Size US$1726
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names RS1
Uniprot No. O15537
Research Area Cell Adhesion
Alternative Names Retinoschisin; RS1; X-linked juvenile retinoschisis protein; XLRS1_HUMAN
Species Homo sapiens (Human)
Source E.coli
Expression Region 24-224aa
Target Protein Sequence STEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 50.0kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal GST-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (By similarity). May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells
Gene References into Functions
  1. molecular detail such as the precise localization of mutant protein in the cell as well as its ability to assemble into a functionally active oligomer might largely influence disease severity among XLRS patients PMID: 29851975
  2. These results establish that extracellular delivery of RS1 rescues the structural and functional deficits in the Rs1h knockout mouse model and that this ex vivo gene therapy approach can inhibit progression of disease. PMID: 27390514
  3. Taken together, RS1 mutation was found to segregate with retinoschisis phenotype while none of the other identified variations were co-segregating with the systemic defects. Hereby, we infer that the multisystemic defects harbored by the patient are a rare coexistence of XLRS, developmental delay, sensorineural hearing loss, and reduced axial tone reported for the first time in the literature. PMID: 28574807
  4. Results suggest a regulatory effect of retinoschisin on Na/K-ATPase signaling and localization, whereas Na/K-ATPase-dysregulation caused by retinoschisin deficiency could represent an initial step in XLRS pathogenesis. PMID: 28615319
  5. these findings support distinct mechanisms of pathology for two classes of X-linked retinoschisis -associated mutations in the retinoschisin assembly. PMID: 27798099
  6. A novel RS1 (97delT) mutation was identified in a Taiwanese family with X-linked retinoschisis (XLRS). This finding expands the RS1 mutation spectrum and may help to further understand the molecular pathogenesis of XLRS. PMID: 24529551
  7. Clinical and genetic characterization of affected homozygous females in XLRS affords the rare opportunity to explore the molecular mechanisms of XLRS and the manifestation of these mutations as disease in humans. PMID: 25894957
  8. A novel RS1 (304C > T) mutation in a Taiwanese family with X-linked retinoschisis. PMID: 26043410
  9. We identified a novel causative mutation of RS1 in a Chinese family with X-linked juvenile retinoschisis. PMID: 25168411
  10. the disease and p.Arg197Cys mutation of RS1 gene was identified PMID: 25799783
  11. X-linked retinoschisis despite striking differences in phenotypic presentation in affected subjects, homozygosity of one affected female, and seemingly dominant inheritance in three subsequent generations because of multiple consanguinity. PMID: 25054456
  12. Sequencing of the RS1 gene identified 16 mutations, nine of which were novel. PMID: 24505212
  13. Severe RS1 missense changes were associated with a lower ERG b/a ratio than were mild changes in X-linked retinoschisis suggesting the effect of the mutations on protein structure influenced the retinal dysfunction. PMID: 23847049
  14. Two novel exonic deletions within the RS1 gene locus, are reported. PMID: 24227916
  15. There is profound phenotypic variability in patients with XLRS. Nonsense, splice-site, or frame-shifting mutations in RS1 consistently caused electronegative bright-flash ERG, delayed flicker response, and abnormal PERG PMID: 23453514
  16. Four novel RS1 gene mutations have been described in male Polish patients with X-linked juvenile retinoschisis. PMID: 23288992
  17. aggregation propensity in the RS1 C110Y mutant is dependent upon the formation of suitable aggregating substrates for propagation of aggregation and not directly related to or determined by overall structural instability PMID: 22292953
  18. Clinical follow-up of an X-linked juvenile retinoschisis (XLRS) patient with a typical juvenile retinoschisis phenotype revealed no significant decline in visual acuity during this time period. PMID: 22171610
  19. Ten hemizygous mutations in RS1 were detected in patients from 14 of the 20 families with retinoschisis. PMID: 22245991
  20. Loss of RS1 due to mutations in the X-linked retinoschsis gene leads to splitting within the retinal layers. PMID: 22183371
  21. adaptive optics scanning laser ophthalmoscopy images of two patients with molecularly characterized XLRS revealed increased cone spacing and abnormal packing in the macula of each patient, but cone coverage and function were near normal. PMID: 22110067
  22. RS1 mutation putative severity and age both had significant effects on retinal function in X-linked retinoschisis only in the severe mutation group, as judged by electroretinography analysis of the b-wave amplitude and the b/a-ratio PMID: 22039241
  23. Data suggest that retinoschisin secretion is regulated by the F-actin cytoskeleton, that cGMP or inhibition of ROCK alters F-actin structure enhancing the secretion, and that the microtubule cytoskeleton is also involved in this process. PMID: 21738583
  24. Two novel mutations (W112X and S134P) and three previously identified missense mutations (R102Q, R200H, and R213W) were found. PMID: 21701876
  25. Retinoschisin, the protein involved in the pathogenesis of X-linked juvenile retinoschisis, membrane association is severely impaired in the absence of ATP1A3 and ATP1B2. PMID: 21196491
  26. analyzed the biochemical consequences of several RS1 signal-sequence mutants (c.1A>T, c.35T>A, c.38T>C, and c.52G>A) in X-linked retinoschisis disease PMID: 20809529
  27. The R213W mutation in RS1 causes various severities of retinoschisis in a large Chinese family. PMID: 20806044
  28. Clinical follow-up of ten young XLRS (X-linked retinoschisis) patients with a typical congenital retinoschisis phenotype revealed no significant decline in retinal function during this time period. PMID: 20569020
  29. A novel p.D126G mutation appeared to be associated with a severe phenotype with vitreous hemorrhage developing in infancy. PMID: 20151283
  30. Results show that missense mutations of retinoschisin which cause intracellular retention also lead to an unfolded protein response. PMID: 19849666
  31. Novel and known missense mutations of XLRS1 gene in the diagnosis retinoschisis. PMID: 12055472
  32. Two novel point mutations of the XLRS1 gene in two Japanese patients with X-linked juvenile retinoschisis. One novel splice donor site mutation (IVS2 + 1g to a) and one missense mutation of exon 6 (Ala211Thr) were found. PMID: 12383832
  33. Basis of RS1 is intracellular retention of mutant proteins, which may explain why disease severity is not mutation-specific. PMID: 12417531
  34. Electroretinographic findings in three family members with X-linked juvenile retinoschisis associated with a novel Pro192Thr missense mutation of the XLRS1 gene. PMID: 12457918
  35. X-linked retinoschisis is caused by defective discoidin domain structure, subunit assembly, and endoplasmic reticulum processing of retinoschisin PMID: 12746437
  36. analysis of folding of mutant RS1 protein PMID: 12782284
  37. Each family had a different mutation, Trp96stop, 522+1g-->a, and Lys167Asn in the XLRS1 gene. PMID: 12920343
  38. four base pair deletion (375- 378 del AGAT) in exon 5 of the XLRS1 gene was found in all affected males. PMID: 12967815
  39. Molecular testing revealed a novel 473-bp deletion including exon 4 in the XLRS1 gene in both siblings. This resulted in a frameshift mutation and a premature termination at codon 78. PMID: 14986011
  40. One patient with more severe clinical presentation had a RS1 exon 1 deletion and a P193S mutation was found in the other patient with mild macular involvement PMID: 15281981
  41. In three patients, we identified three different missense mutations (p.S73P, p.Y89C, p.R209C) in the functionally important discoidin domain of the RS1 gene. PMID: 15531314
  42. assembly of RS1 into a disulfide-linked homo-octamer appears to be critical for its function as a retinal cell adhesion protein PMID: 15644328
  43. A novel Leu103Phe mutation is an additional missense mutation which is responsible for the pathogenesis of X-linked retinoschisis. PMID: 16768192
  44. We identified a novel point mutation (1A>T transversion) in the initiation codon of the XLRS1 gene in affected males PMID: 17031297
  45. Retinoschisin protein(RS) is expressed in the pinealocytes but not in interstitial glial cells. The lack of structural abnormalities in the RS1(-/Y) mice suggests that RS serves a different function in the pineal gland than in the retina. PMID: 17093404
  46. Review. Many mutations have been found in RS1, which encodes a 224-AA secreting retinal protein, retinoschisin. Retinoschisin octamerisation is implicated in cell-cell interactions & cell adhesion perhaps by interacting with beta2 laminin. PMID: 17172462
  47. We describe a novel nonsense mutation in the conserved region of Rs1 in a Japanese XLRS family. PMID: 17295148
  48. Multiple fine white dots at the macula may be the initial fundus feature in RS1 mutation. PMID: 17296904
  49. Mutations in RS1 to be associated with XLRS in the Indian population. PMID: 17515881
  50. Severe X linked juvenile retinoschisis phenotypes are associated with the frameshift mutation 26 del T, splice donor site mutation (IVS1+2T to C), and Arg102Gln, Asp145His, Arg209His, and Arg213Gln mutations. PMID: 17615541
  51. We identified unusual presentations of X-linked retinoschisis with the help of electroretinography, optical coherence tomography, family screening, and genetic analysis PMID: 17631851
  52. confirmed the co-localization of retinoschisin with Na/K ATPase and SARM1 in photoreceptors and bipolar cells of retina tissue PMID: 17804407
  53. We found there are five different mutations with four containing missense point mutations and one having a frame-shift deletion PMID: 17852193
  54. In clinically suspected X-linked congenital retinoschisis (RS), a combination of ERG, FAF, OCT, and molecular-genetic testing is advised to verify the diagnosis. PMID: 17987333
  55. RS1 gene mutations caused X-linked juvenile retinoschisis in these Chinese families. PMID: 18369700
  56. The ocular findings of a Hungarian family with X-linked juvenile retinoschisis (XLRS) reveals a novel putative splice mutation leading to serious truncation of retinoschisin (RS1) protein. PMID: 18728755
  57. This study showed that the response of macular cysts to dorzolamide in patients with XLRS may be observed independent of the mechanism responsible for retinoschisin protein dysfunction. PMID: 18834580
  58. This report describes a novel mutation in a family in which consanguinity has led to XLRS in 4 females. PMID: 18982040
  59. The prevalent p.Gln154Arg mutation is first reported in this work and presents a common origin in Spanish patients with X-linked juvenile retinoschisis. PMID: 19324861
  60. characterization of the mutational spectrum of the RS1 gene in Korean patients with X-linked retinoschisis (XLRS); a missense mutation was the predominant type & common or founder mutations were not observed in the Korean patients in this study with XLRS PMID: 19390641
  61. hemizygous 371 A/G missense mutation and hemizygous 214 G/A missense mutation in exon 5 in juvenile retinoschisis PMID: 19393523
  62. The c354del1-ins18 mutation caused an RS1-null biochemical phenotype and a progressive clinical phenotype in a 5-year-old boy, whereas the older XLRS relatives had macular atrophy. PMID: 19474399

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Involvement in disease Retinoschisis juvenile X-linked 1 (XLRS1)
Subcellular Location Secreted, Cell membrane, Peripheral membrane protein, Extracellular side
Tissue Specificity Restricted to the retina (at protein level) (PubMed:10915776). Detected in the inner segment of the photoreceptors, the inner nuclear layer, the inner plexiform layer and the ganglion cell layer (at protein level). At the macula, expressed in both the out
Database Links

HGNC: 10457

OMIM: 300839

KEGG: hsa:6247

STRING: 9606.ENSP00000369320

UniGene: Hs.715725

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