Recombinant Human Radixin (RDX)
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中文名称:人RDX重组蛋白
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货号:CSB-YP019532HU
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规格:
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来源:Yeast
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其他:
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中文名称:人RDX重组蛋白
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货号:CSB-EP019532HU
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规格:
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来源:E.coli
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其他:
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中文名称:人RDX重组蛋白
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货号:CSB-EP019532HU-B
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规格:
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来源:E.coli
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共轭:Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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其他:
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中文名称:人RDX重组蛋白
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货号:CSB-BP019532HU
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规格:
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来源:Baculovirus
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其他:
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中文名称:人RDX重组蛋白
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货号:CSB-MP019532HU
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规格:
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来源:Mammalian cell
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其他:
产品详情
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纯度:>85% (SDS-PAGE)
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基因名:
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Uniprot No.:
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别名:CB567; CG12537; DFNB24; ESP10; Hh-induced MATH and BTB domain-containing protein; HIB; Moesin-B; Protein roadkill; RADI_HUMAN; Radixin; RDX
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种属:Homo sapiens (Human)
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蛋白长度:Full length protein
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表达区域:1-583
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氨基酸序列MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE TAVLLASYAV QAKYGDYNKE IHKPGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR GMLREDSMME YLKIAQDLEM YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER LKQIEEQTIK AQKELEEQTR KALELDQERK RAKEEAERLE KERRAAEEAK SAIAKQAADQ MKNQEQLAAE LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPVIP PTENEHDEHD ENNAEASAEL SNEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD ETKKTQNDVL HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
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蛋白标签:Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially. -
产品提供形式: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. -
复溶: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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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储存条件:Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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保质期: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. -
货期:Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
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注意事项:Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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Datasheet :Please contact us to get it.
相关产品
靶点详情
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功能:Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
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基因功能参考文献:
- CPI-17 drives Ras activity and tumorigenesis in melanomas in a two-fold way; inactivation of the tumor suppressor merlin and activation of the growth promoting ERM family. PMID: 27793041
- The results reveal a supportive role of ERMs in cortical activities during cytokinesis, and also provide insight into the selective mechanism that preferentially associates cytokinesis-relevant proteins with the division site. PMID: 28889652
- Radixin knockdown suppresses the metastasis of SGC-7901 cells in vitro by up-regulation of E-cadherin. The NF-kappaB/snail pathway contributes to the regulation of E-cadherin in response to depletion of radixin. PMID: 27855404
- Phospho-Ezrin/Radixin/Moesin (ERM) inhibit cell adhesion, and therefore, dephosphorylation of ERM proteins is essential for cell adhesion.Phospho-ERM induce formation and/or maintenance of spherical cell shape. PMID: 26555866
- These studies identify Akt2 as a critical kinase that regulates radixin phosphorylation and leads to Mrp-2 translocation and function. PMID: 26500117
- Intracellular sphingosine kinase 2-derived sphingosine-1-phosphate mediates epidermal growth factor-induced ezrin-radixin-moesin phosphorylation and cancer cell invasion. PMID: 26209696
- High Radixin expression is associated with glioblastoma. PMID: 25520109
- Ezrin, radixin and moesin are unlikely targets for autoantibodies in demyelinating neuropathies. PMID: 25286001
- These data suggest an association between RDX polymorphisms and the clinical features of RA patients, particularly the ESR PMID: 24854655
- Radixin was identified as a target gene of miR-196a/-196b. Elevated miR-196a/-196b expression in GC cells led to reduced radixin protein levels and vice versa. PMID: 24933454
- This study finding have implications concerning the importance of concomitant radixin upregulation in tumor progression and poor prognosis of patients with gliomas. PMID: 24380686
- important role of ezrin-moesin-radixin proteins during HCV infection at the postentry level and highlight possible novel targets for HCV treatment. PMID: 23703860
- ERM proteins play important differential roles in the thrombin-induced modulation of EC permeability, with moesin promoting barrier dysfunction and radixin opposing it. PMID: 23729486
- Data suggest that P-glycoprotein associate with the F-actin cytoskeleton through ezrin/radixin/moesin (ERM) in CCR9/CCL25 induced multidrug resistance of acute T-lymphocytic leukemia (T-ALL) cells. PMID: 23326330
- Control of adipogenesis by ezrin, radixin and moesin-dependent biomechanics remodeling. PMID: 23116763
- Data show that silencing of radixin (RDX) phenocopied the effects of miR-409 overexpression, whereas restoration of RDX in miR-409-overexpressed gastric cancer (GC) cells reversed the suppressive effects of miR-409. PMID: 22179828
- Ezrin/radixin/moesin are required for the purinergic P2X7 receptor (P2X7R)-dependent processing of the amyloid precursor protein. PMID: 22891241
- results suggest that radixin might play a critical role in pancreatic cancer progression, possibly through involvement of down-regulation of TSP-1 and E-cadherin expression. PMID: 22631643
- role of CCM3 and ezrin/radixin/moesin family of proteins in cell's response to oxidative stress PMID: 22291017
- Ano1, ezrin, and moesin/radixin colocalize apically in salivary gland epithelial cells, and overexpression of moesin and Ano1 in HEK cells alters the subcellular localization of both proteins PMID: 22685202
- Radixin selectively modulates the expression and function of MRP2 in human gastric adenocarcinoma. PMID: 22469515
- MiR-31 targeted radixin predominantly via inhibition of protein translation instead of degradation of mRNA. PMID: 22089331
- results indicate that ezrin influences the expression of P-gp at the translational level, whereas radixin is involved in membrane localization of P-gp in HepG2 cells PMID: 21837648
- The ERM (ezrin, radixin, moesin) proteins are novel scaffolds at the level of SOS activity control, which is relevant for both normal Ras function and dysfunction known to occur in several human cancers. PMID: 22132106
- Ezrin, radixin, and moesin are phosphorylated in response to 2-methoxyestradiol and modulate endothelial hyperpermeability. PMID: 21659656
- the ezrin, radixin and moesin proteins differentially modulate sphingosine 1 phosphate-induced alterations in lung endoethlial cell cytoskeleton and permeability PMID: 21864676
- This study provides the novel evidence that increased phosphorylation of Ezrin/radixin/moesin proteins may contribute to proliferation of rheumatoid fibroblast-like synoviocytes. PMID: 21278069
- Dysregulation of the ezrin/radixin/moesin-RAGE complex might be an important step in rearrangement of the actin cytoskeleton during proinflammatory cytokine-induced epithelial-mesenchymal transition of human alveolar epithelial cells. PMID: 21278261
- ezrin, radixin and moesin play similar roles in the tumor cell metastatic potential and their roles of upregulating the expression of E-cadherin may be important in tumor progression PMID: 21352885
- Polar distribution of radixin suggest a role in promoting formation and plasticity of membrane surface projections and also suggest that radixin is an organizer and regulator of Mrp-2 and cell polarity in hepatocytes. PMID: 21160029
- the identification of radixin as a scaffolding unit for both cAMP effectors, Epac and PKA PMID: 21047789
- Results demonstrate a new regulatory mechanism of ezrin-radixin-moesin phosphorylation by sphingolipids with opposing actions of ceramide and sphingosine 1-phosphate. PMID: 20679347
- Data suggest that ezrin-radixin-moesin proteins are involved in the spatial regulation of Epac1 and cooperate with cAMP- and Rap-mediated signaling to regulate adhesion to the extracellular matrix. PMID: 20855527
- amino-terminal domains of the ezrin, radixin, and moesin (ERM) proteins bind advanced glycation end products and have a role in diabetes PMID: 12734202
- Disrupted localization of radixin and MRP2 supports the concept that radixin contributes to the canalicular localization of MRP2. PMID: 14568249
- ezrin/radixin/moesin proteins are recruited by NHE1 Na+/H+ exchanger and have roles in regulating Akt-dependent cell survival PMID: 15096511
- All three ERM family members can localise to the nucleus; a specific nuclear localisation sequence, which is conserved and functional in all ERM family members, is identified, implying specific regulated nuclear import. PMID: 15149851
- results suggest that ezrin-radixin-moesin proteins are required for microvillar positioning of L-selectin and that this is important both for leukocyte tethering and L-selectin shedding PMID: 15178693
- Ezrin, radixin and moesin are ADP-ribosylated by Pseudomonas aeruginosa ExoS PMID: 15252013
- Conformational regulation of radixin protein function occurs by association of the FERM and C-terminal domains, whereby the membrane- and actin-binding activities are mutually suppressed [review] PMID: 15313460
- Expression of ExoS in HeLa cells led to a loss of phosphorylation of Ezrin/radixin/moesin proteins that was dependent upon the expression of ADP-ribosyltransferase activity. PMID: 16889625
- 2 mutant alleles of RDX in 2 consanguineous families associated with neurosensory hearing loss; sequence analysis of RDX from original DFNB24 family revealed a c.463C>T transition substitution predicted to truncate radixin in the FERM domain PMID: 17226784
- increased CD44, ezrin, radixin, and moesin phosphorylation represents a key molecular abnormality that guides T cell adhesion and migration in SLE patients. PMID: 17237445
- RDX was differentially expressed in sclerotic hippocampi compared to non-sclerotic ones. PMID: 17515952
- Report disturbed colocalization of multidrug resistance protein 2 and radixin in human cholestatic liver diseases. PMID: 17725603
- Radixin and ezrin play similar roles in the apical membrane localization of ABCC2 (MRP2) and their expression level and subcellular distribution are important factors in the regulation of ABCC2 (MRP2) at the post-transcriptional level. PMID: 17825285
- the ezrin, radixin, and moesin proteins function as positive regulators of infection by X4-tropic HIV-1 PMID: 18295815
- Unlike ezrin and moesin, radixin (a member of the ezrin-radixin-moesin protein family)is not expressed in Jurkat cells, nor is it involved in apoptotic signaling following Fas receptor triggering in these cells. PMID: 18941185
- No aspects of T cell receptor signaling uniquely require transgenic ezrin or moesin; instead, T cell activation appears to depend on net ezrin, radixin, and moesin (ERM)protein expression, while ezrin and moesin function together. PMID: 19124745
- In Vitro and in Vivo Characterization of Molecular Interactions between Calmodulin, Ezrin/Radixin/Moesin, and L-selectin PMID: 19129194
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相关疾病:Deafness, autosomal recessive, 24 (DFNB24)
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亚细胞定位:Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell projection, microvillus. Note=Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.
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数据库链接:
HGNC: 9944
OMIM: 179410
KEGG: hsa:5962
STRING: 9606.ENSP00000342830
UniGene: Hs.263671
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