Recombinant Human Retinoschisin (RS1) Protein (GST)

Name: Recombinant Human Retinoschisin (RS1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08127P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Retinoschisin (RS1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O15537
Target Symbol	RS1
Synonyms	Retinoschisin; RS1; X-linked juvenile retinoschisis protein; XLRS1_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	STEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA
Expression Range	24-224aa
Protein Length	Full Length of Mature Protein
Mol. Weight	50.0kDa
Research Area	Cell Adhesion
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides. 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. Required for normal structure and function of the retina.
Subcellular Location	Secreted. Cell membrane; Peripheral membrane protein; Extracellular side.
Database References	HGNC: 10457 OMIM: 300839 KEGG: hsa:6247 STRING: 9606.ENSP00000369320 UniGene: PMID: 29851975 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 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 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 these findings support distinct mechanisms of pathology for two classes of X-linked retinoschisis -associated mutations in the retinoschisin assembly. PMID: 27798099 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 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 A novel RS1 (304C > T) mutation in a Taiwanese family with X-linked retinoschisis. PMID: 26043410 We identified a novel causative mutation of RS1 in a Chinese family with X-linked juvenile retinoschisis. PMID: 25168411 the disease and p.Arg197Cys mutation of RS1 gene was identified PMID: 25799783 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 Sequencing of the RS1 gene identified 16 mutations, nine of which were novel. PMID: 24505212 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 Two novel exonic deletions within the RS1 gene locus, are reported. PMID: 24227916 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 Four novel RS1 gene mutations have been described in male Polish patients with X-linked juvenile retinoschisis. PMID: 23288992 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 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 Ten hemizygous mutations in RS1 were detected in patients from 14 of the 20 families with retinoschisis. PMID: 22245991 Loss of RS1 due to mutations in the X-linked retinoschsis gene leads to splitting within the retinal layers. PMID: 22183371 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 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 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 Two novel mutations (W112X and S134P) and three previously identified missense mutations (R102Q, R200H, and R213W) were found. PMID: 21701876 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 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 The R213W mutation in RS1 causes various severities of retinoschisis in a large Chinese family. PMID: 20806044 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 A novel p.D126G mutation appeared to be associated with a severe phenotype with vitreous hemorrhage developing in infancy. PMID: 20151283 Results show that missense mutations of retinoschisin which cause intracellular retention also lead to an unfolded protein response. PMID: 19849666 Novel and known missense mutations of XLRS1 gene in the diagnosis retinoschisis. PMID: 12055472 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 Basis of RS1 is intracellular retention of mutant proteins, which may explain why disease severity is not mutation-specific. PMID: 12417531 Electroretinographic findings in three family members with X-linked juvenile retinoschisis associated with a novel Pro192Thr missense mutation of the XLRS1 gene. PMID: 12457918 X-linked retinoschisis is caused by defective discoidin domain structure, subunit assembly, and endoplasmic reticulum processing of retinoschisin PMID: 12746437 analysis of folding of mutant RS1 protein PMID: 12782284 Each family had a different mutation, Trp96stop, 522+1g-->a, and Lys167Asn in the XLRS1 gene. PMID: 12920343 four base pair deletion (375- 378 del AGAT) in exon 5 of the XLRS1 gene was found in all affected males. PMID: 12967815 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 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 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 assembly of RS1 into a disulfide-linked homo-octamer appears to be critical for its function as a retinal cell adhesion protein PMID: 15644328 A novel Leu103Phe mutation is an additional missense mutation which is responsible for the pathogenesis of X-linked retinoschisis. PMID: 16768192 We identified a novel point mutation (1A>T transversion) in the initiation codon of the XLRS1 gene in affected males PMID: 17031297 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 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 We describe a novel nonsense mutation in the conserved region of Rs1 in a Japanese XLRS family. PMID: 17295148 Multiple fine white dots at the macula may be the initial fundus feature in RS1 mutation. PMID: 17296904 Mutations in RS1 to be associated with XLRS in the Indian population. PMID: 17515881 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

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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