Recombinant Human Protein Xrp2 (RP2) Protein (GST)

Name: Recombinant Human Protein Xrp2 (RP2) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09136P
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 Protein Xrp2 (RP2) 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	O75695
Target Symbol	RP2
Synonyms	RP2; Protein XRP2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	GCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI
Expression Range	1-350aa
Protein Length	Full Length
Mol. Weight	66.5kDa
Research Area	Neuroscience
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	Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins.
Subcellular Location	Cell membrane; Lipid-anchor; Cytoplasmic side. Cell projection, cilium.
Protein Families	TBCC family
Database References	HGNC: 10274 OMIM: 300757 KEGG: hsa:6102 STRING: 9606.ENSP00000218340 UniGene: PMID: 28294154 RP2 mutation would have a moderate pathogenic effect in photoreceptors carrying the mutation, causing abnormal outer segments, with the accumulation of lipofuscin similar to RDS/PRPH2 pattern dystrophy. PMID: 26885761 this study identifies ARL3 as a key player in prenylated protein trafficking in rod photoreceptor cells and establishes the potential role for ARL3 dysregulation in the pathogenesis of RP2-related forms of XLRP PMID: 26936825 Studies indicate taht the majority of patients with X-linked RP have mutations in the retinitis pigmentosa GTPase regulator (RPGR) or retinitis pigmentosa 2 protein (RP2) genes. PMID: 27911705 study also reveals a role of the C-terminal domain of RP2 in maintaining the overall protein stability. PMID: 28209709 Three XLRP families (RP-001, RP-002, and RP-003), composed of 13 individuals, were reported in this study, and 2 different mutations were detcted We found 3 genetic variants: a novel mutation c.1591G>T in exon 14 and a novel polymorphism c.1105C>T in exon 10, resulting in p.Glu531* and p.Arg369Cys of RPGR gene, respectively, and one already known mutation c.413A>G in exon 2, resulting in a p.Glu138Gly of RP2 gene PMID: 27768226 We identified a novel causative mutation in RP2 from a single proband's exome sequence data analysis. This study highlights the effectiveness of the whole-exome sequencing in the genetic diagnosis of X-linked retinitis pigmentosa, over the conventional sequencing methods. PMID: 27769321 Three mutations were identified in the ORF15 exon of RPGR. No RP2 mutations were found among the examined families. Mutation screening of RP patients is essential to understand the mechanism behind this disease and develop treatments PMID: 27323122 The ability of the restored RP2 protein level to reverse the observed cellular phenotypes in cells lacking RP2 indicates that translational read-through could be clinically beneficial for patients. PMID: 25292197 ellipsometric measurements of naRP2 demonstrated that its particular affinity for saturated phospholipids can be explained by its larger extent of insertion in this phospholipid monolayer compared to that in polyunsaturated phospholipid monolayers. PMID: 25844643 The methylation state of CpG sites close to the RP2 core promoter (GAAA)n repeat serves as a proxy measurement of X-chromosome inactivation in human and non-human primates. PMID: 25078280 A novel frameshift mutation in RP2 was detected. This mutation was located in exon 2 of the RP2 gene: a nucleotide C was inserted at 111 (c.111insC, Fig. 1A), which caused a protein translation frameshift PMID: 24479636 Direct sequencing of RPGR and RP2 allowed for identification of a disease-causing mutation in 21 families. Of these "adRP" families 19 had RPGR mutations, and two had RP2 mutations. PMID: 23372056 Based on our findings, we suggest that RPGR should be considered as a first tier gene for screening isolated males with retinal degeneration. PMID: 23150612 data support a role for RP2 in facilitating the membrane association and traffic of Gbeta1, potentially prior to the formation of the obligate Gbeta:Ggamma heterodimer; combined with other recent evidence, this suggests that RP2 may co-operate with Arl3 and its effectors in the cilia-associated traffic of G proteins PMID: 22072390 The localization of RP2 to basal bodies and cilia in photoreceptors and kidney cells has linked RP2 dysfunction with ciliopathies. PMID: 22183373 Data demonstrate that Importin beta2 is necessary for localization of retinitis pigmentosa 2 (RP2) to the primary cilium, and identify two distinct binding sites of RP2, which interact independently with Importin beta2. PMID: 21285245 An identifiable phenotype for RP2-X-linked retinitis pigmentosa aids in clinical diagnosis and targeted genetic screening. PMID: 20625056 We propose that RP2 regulation of Arl3 is important for maintaining Golgi cohesion, facilitating the transport and docking of vesicles and thereby carrying proteins to the base of the photoreceptor connecting cilium for transport to the outer segment. PMID: 20106869 Our results expand the frequency and spectrum of mutations at RPGR and RP2 as well as their associated clinical phenotypes in Chinese patients. PMID: 20021257 The mutation 358C-->T is useful in analyzing the function of RP2 protein and gene diagnosis of X-linked retinitis pigmentosa (XLRP). PMID: 11798852 functional overlap with tubulin-specific chaperone cofactor C PMID: 11847227 A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa. PMID: 11992260 Patients with RP2 mutations had, on average, lower visual acuity but similar visual field area, final dark-adapted threshold, and 30-Hz ERG amplitude compared with those with RPGR mutations PMID: 14564670 Mutations in the RP2 gene is associated with X-linked retinitis pigmentosa PMID: 14566651 The data suggest that RP2 may have previously unrecognized roles as a DNA damage response factor and 3' to 5' exonuclease. PMID: 16457815 The N-terminal 34 residues and beta helix domain of RP2 are required for interaction with Arl3. PMID: 16472755 In this cohort of XLRP families, as has happened in previous studies, RP3 also seems to be the most prevalent form of XLRP, and, based on the results, the authors propose a four-step protocol for molecular diagnosis of XLRP families. PMID: 16936086 Three ORF15 mutations and one RP2 mutation in five Japanese retinitis pigmentosa families. PMID: 17093403 The proportion of RP2-mediated XLRP in the Danish population is higher and the proportion of RPGR-ORF15 is lower than reported in other studies. PMID: 17724181 RP2 is an efficient GAP for Arl3, with structural features similar to other GAPs PMID: 18376416 A transversion (T>A) at position -9 in intron 3 of RP2 causes X-linked retinitis pigmentosa (XLRP) by altering the splicing pattern and highlights the pathogenicity of intronic variants. PMID: 19516003

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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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