Recombinant Human X-Linked Retinitis Pigmentosa Gtpase Regulator (RPGR) Protein (hFc)

Name: Recombinant Human X-Linked Retinitis Pigmentosa Gtpase Regulator (RPGR) Protein (hFc)
Brand: Beta LifeScience
SKU: BLC-01288P
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 X-Linked Retinitis Pigmentosa Gtpase Regulator (RPGR) Protein (hFc) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q92834
Target Symbol	RPGR
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-hFC
Target Protein Sequence	NKLYMFGSNNWGQLGLGSKSAISKPTCVKALKPEKVKLAACGRNHTLVSTEGGNVYATGGNNEGQLGLGDTEERNTFHVISFFTSEHKIKQLSAGSNTSAALTEDGRLFMWGDNSEGQIGLKNVSNVCVPQQVTIGKPVSWISCGYYHSAFVTTDGELYVFGEPENGKLGLPNQLLGNHRTPQLVSEIPEKVIQVACGGEHTVVLTENAVYTFGLGQFGQLGLGTFLFETSEPKVIENIRDQTISYISCGENHTALITDIGLMYTFGDGRHGKLGLGLENFTNHFIPTLCSNFLRFIVKLVACGGCHMVVFAAP
Expression Range	54-367aa
Protein Length	partial of Isoform 1
Mol. Weight	62.8 kDa
Research Area	Guanine-Nucleotide Releasing Factor
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	Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes. May be involved in microtubule organization and regulation of transport in primary cilia.
Subcellular Location	Cytoplasm, cytoskeleton, flagellum axoneme. Golgi apparatus. Cell projection, cilium.; [Isoform 6]: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme.
Database References	HGNC: 10295 OMIM: 300029 KEGG: hsa:6103 STRING: 9606.ENSP00000367766 UniGene: PMID: 30313097 this is the first report of a molecular genetic diagnosis of XLRP in a patient with Turner syndrome. The X-linked RP in this woman may not be related to Turner syndrome, but may be a manifestation of the lack of a normal paternal X chromosome with in tact but mutate d RPGR PMID: 29135076 A novel frame-shift mutation in exon ORF15 of RPGR gene attributes of this heterozygosity suggest that gain-of-function mechanism could give rise to pathologic myopia via a degenerative cell-cell remodeling of the retinal structures. PMID: 27995965 RPGR interacts with PDE6delta and INPP5E. PDE6delta binds selectively to the C-terminus of RPGR and that this interaction is critical for RPGR's localization to cilia. INPP5E associates with the N-terminus of RPGR and trafficking of INPP5E to cilia is dependent upon the ciliary localization of RPGR. PMID: 28172980 In induced pluripotent stem cells and mouse knockouts that RPGR mediates actin dynamics in photoreceptors via the actin-severing protein, gelsolin. PMID: 28814713 Together with a physical interaction between RPGR and the C-terminal domain of CEP290, our data suggest that RPGR and CEP290 genetically interact and highlight the involvement of hypomorphic alleles of genes as potential modifiers of heterogeneous retinal ciliopathies. PMID: 26936822 We also correlated the features observed in patients with those of three Rpgr-mutant (Rpgr-ko, Rd9, and Rpgr-cko) mice. In patients, there was pronounced macular disease PMID: 27798110 Profound visual loss occurred by the second decade of life with progression to near no light perception by age 60 in this kindred of X-linked RP associated with the RPGR genotype. PMID: 24555744 Although carriers of XLRP are usually asymptomatic or have a mild disease of late onset, the proband presented here exhibited an early-onset, aggressive form of the disease. PMID: 24428633 The regulator of chromosome condensation 1-like domain of RPGR was conserved in vertebrates and invertebrates, but RPGR(ORF15) was unique to vertebrates. PMID: 26431479 Coverage-based analysis indicated that the RPGR open reading frame (ORF)15 was located in an uncovered or low-depth region. Through additional screening of ORF15, we identified pathogenic mutations in 14% (7/50) of patients. PMID: 25569437 X-linked retinitis pigmentosa caused by mutations in the RPGR gene is a severe and early onset form of retinal degeneration. [review] PMID: 25301933 Severe retinal degeneration is found in a Czech family women with a c.2543del mutation in ORF15 of the RPGR gene. PMID: 25352739 The edge of the ellipsoid zone in each patient with X-linked retinitis pigmentosa indicates a transition zone between relatively healthy and relatively degenerate retina. PMID: 25556114 RPGR mutations associated with X-linked retinitis pigmentosa. PMID: 24454928 We will summarize the functional characterization of RPGR and highlight recent studies in animal models, which will not only shed light on the disease mechanisms in X linked retinitis pigmentosa but will also provide therapeutic strategies for treatment. PMID: 24664734 A novel RPGR gene was found in a retinal dystrophy patient in a family with Stargardt disease. PMID: 24489377 While visual acuity and electroretinography phenotypes are concordant in only some patients carrying identical mutations, assessment of phenotypes revealed stronger phenotypic conservation. PMID: 23681342 RPGR is acting as a scaffold protein recruiting cargo-loaded PDE6D and Arl3 to release lipidated cargo into cilia. PMID: 23559067 Mutations in RPGR were found in two patients and relatives with primary ciliary dyskinesia and retinitis pigmentosa. Reduced ciliary orientation and coordination of ciliary bundles suggest RPGR may play a role in respiratory cilia orientation. PMID: 22888088 Mutations in RPGR are one of the most common causes of all forms of retinitis pigmentosa. PMID: 23372056 the human RPGR proximal promoter region in which a 3-kb fragment contained sufficient regulatory elements to control RPGR expression in mouse retina and other tissues. PMID: 22577079 Genetic variation of RPGRIP1L and IQCB1 may affect severity in RPGR mutation X-linked retinitis pigmentosa. PMID: 22183348 This novel mutation in RPGR ORF15 causes serious retinitis pigmentosa phenotype in males and no RP phenotype in female carriers. PMID: 21914266 The function of RPGR was analysed by RNA interference-mediated translational suppression. PMID: 21933838 Data show that the minor allele (N) of I393N in IQCB1 and the common allele (R) of R744Q in RPGRIP1L were associated with severe disease in XlRP with RPGR mutations. PMID: 21857984 Expression of RPGR mutations in this particular region appears to be relatively homogeneous and predisposed to cones. PMID: 21866333 a micro-deletion through prenatal genetic diagnosis and another novel nonsense mutation in RPGR-ORF15. PMID: 21683121 Recent advances on understanding the role of RPGR in photoreceptor protein trafficking, are summarized. PMID: 20238008 a novel deletion mutation in the retinitis pigmentosa GTPase regulator gene, gORF15+556delA, in a Han Chinese family with retinitis pigmentosa PMID: 21227725 Mutations in the RPGR gene lead to X-linked Retinitis pigmentosa (XLRP), one of the most severe and early onset forms of RP. Gene therapy is considered a potential therapeutic option and is currently under investigation. PMID: 21174525 The pedigree we have investigated here represents the first Czech family with an identified molecular genetic cause of retinitis pigmentosa PMID: 20064120 RPGR modulates intracellular localization and function of RAB8A. PMID: 20631154 Differentially expressed genes were identified in mutant retinas. At 7 and 16 weeks, a combination of nonclassic anti- and proapoptosis genes and mitochondria-related genes appear to be involved in photoreceptor degeneration. PMID: 20574030 The novel mutation in RPGR ORF15 causes a serious retinitis pigmentosa phenotype in males and noretinitis pigmentosa phenotype in female carriers. PMID: 20806050 Studies highlight the recent developments in understanding the mechanism of cilia-dependent photoreceptor degeneration due to mutations in RPGR and PGR-interacting proteins in severe genetic diseases. PMID: 20090203 These findings show that splicing of RPGR is precisely regulated in a tissue-dependent fashion and suggest that mutations in RPGR frequently interfere with the expression of alternative transcript isoforms. PMID: 19834030 RPGR is involved in cilia-dependent cascades during development in zebrafish. PMID: 19815619 This novel mutation in RPGRcauses X-Linked RP with complete penetrance in males and females and affected females are highly myopic but retain better visual function than affected males. PMID: 19218993 Insertional/deletional mutations observed in the three families with X-linked retinitis pigmentosa are all different and new, and are predicted to lead to a frameshift, resulting in a truncated protein. PMID: 11754050 X-linked cone-rod dystrophy (locus COD1): identification of mutations in RPGR exon ORF15 PMID: 11857109 A mutation in this gene causes X-linked cone dystrophy. This type of hereditary retinal degeneration is distinct from retinitis pigmentosa. PMID: 11875055 RPGR and RPGRIP isoforms are distributed and co-localized at restricted foci throughout the outer segments of human and bovine, but not mice rod photoreceptors. PMID: 12140192 Identification of an RPGR mutation in atrophic macular degeneration expands the phenotypic range from retinitis pigmentosa. PMID: 12160730 RPGR mutations in most families with definite X linkage and clustering of mutations in a short sequence stretch of exon ORF15. PMID: 12657579 Different RPGR mutations lead to distinct RP (retinitis pigmentosa) phenotypes, with a highly variable inter- and intrafamilial phenotypic spectrum of disease PMID: 14516808 Among patients with RPGR mutations, those with ORF15 mutations had, on average, a significantly larger visual field area and a borderline larger ERG amplitude than did patients with RPGR mutations in exons 1-14 PMID: 14564670 Mutations in the RPGR gene is associated with X-linked retinitis pigmentosa PMID: 14566651 Sequencing revealed skipping of exon 2 in the mutated transcript, leading to in-frame deletion of 42 amino acids affecting the critical RCC1-like domain. PMID: 15364249 RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin. PMID: 15772089

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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.

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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.

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Recombinant Human X-Linked Retinitis Pigmentosa Gtpase Regulator (RPGR) Protein (hFc)

Recombinant Human X-Linked Retinitis Pigmentosa Gtpase Regulator (RPGR) Protein (hFc)

Product Overview

Target Details

FAQs