Recombinant Human Reticulon-4(RTN4) ,partial

Code CSB-YP878853HU
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Source Yeast
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Code CSB-EP878853HU
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Source E.coli
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Code CSB-EP878853HU-B
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Source E.coli
Conjugate 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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Code CSB-BP878853HU
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Source Baculovirus
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Code CSB-MP878853HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names RTN4
Uniprot No. Q9NQC3
Alternative Names 1110020G17Rik; AA407876; AA409940; AA960376; ASY; C130026I10Rik; Foocen; Glut4 vesicle 20 kDa protein; Human NogoA; Kiaa0886; KIAA4153; MGC116054; MGC139261; mKIAA0886; mKIAA4153; My043 protein; Nbla00271; Nbla10545; Neurite growth inhibitor 220; Neurite Growth Inhibitor 220, included; Neurite outgrowth inhibitor; Neuroendocrine-specific protein; Neuroendocrine-specific protein C homolog; NI-250; NI220/250; Nogo A; NOGO; Nogo B; Nogo C; Nogo protein; NOGOC; NSP; NSP-CL; rat N; Reticulon 4; Reticulon 5; Reticulon-4; Reticulon-5; RTN X; RTN-x; Rtn4; Rtn4 reticulon 4; RTN4-A; RTN4-B1; RTN4-B2; RTN4-C; RTN4_HUMAN; Vp20
Species Homo sapiens (Human)
Protein Length Partial
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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.
Form 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 before Lyophilization 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℃/-80℃. 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/-80°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.
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.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

Function
Required to induce the formation and stabilization of endoplasmic reticulum (ER) tubules. They regulate membrane morphogenesis in the ER by promoting tubular ER production. They influence nuclear envelope expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins. However each isoform have specific functions mainly depending on their tissue expression specificities (Probable).; Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex. Acts as a negative regulator of central nervous system angiogenesis. Inhibits spreading, migration and sprouting of primary brain microvascular endothelial cells (MVECs). Also induces the retraction of MVECs lamellipodia and filopodia in a ROCK pathway-dependent manner.; Mainly function in endothelial cells and vascular smooth muscle cells, is also involved in immune system regulation (Probable). Modulator of vascular remodeling, promotes the migration of endothelial cells but inhibits the migration of vascular smooth muscle cells. Regulates endothelial sphingolipid biosynthesis with direct effects on vascular function and blood pressure. Inhibits serine palmitoyltransferase, SPTLC1, the rate-limiting enzyme of the novo sphingolipid biosynthetic pathway, thereby controlling production of endothelial sphingosine-1-phosphate (S1P). Required to promote macrophage homing and functions such as cytokine/chemokine gene expression involved in angiogenesis, arteriogenesis and tissue repair. Mediates ICAM1 induced transendothelial migration of leukocytes such as monocytes and neutrophils and acute inflammation. Necessary for immune responses triggered by nucleic acid sensing TLRs, such as TLR9, is required for proper TLR9 location to endolysosomes. Also involved in immune response to LPS. Plays a role in liver regeneration through the modulation of hepatocytes proliferation. Reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. With isoform C, inhibits BACE1 activity and amyloid precursor protein processing.; Regulates cardiomyocyte apoptosis upon hypoxic conditions. With isoform B, inhibits BACE1 activity and amyloid precursor protein processing.
Gene References into Functions
  1. This review aims at presenting our current knowledge on the role of Nogo-A in the visual system and to discuss how its therapeutic targeting may promote visual improvement in ophthalmic diseases. PMID: 28408340
  2. CAA and TATC Insertion/Deletion Genetic Polymorphisms of RTN4 3'-UTR are associated with Hepatocellular Carcinoma PMID: 28144881
  3. Nogo-B was shown to play an important negative role in apoptotic signaling through its interaction with c-FLIP in colorectal cancer cells. PMID: 29684585
  4. NOGO-B/RTN4B and NOGO-A/RTN4A are simultaneously expressed in cultured epithelial, fibroblast and neuronal cells. Morphological analysis of cells with manipulated levels of NOGO-B/RTN4B revealed that it is required for maintenance of normal endoplasmic reticulum shape. PMID: 27786289
  5. Nogo-B is expressed aberrantly in HCCs and plays an oncogenic role. These findings support that Nogo-B may be a novel anti-HCC therapeutic target. PMID: 28628795
  6. observations suggest that Rtn4A counteracts the Nrdp1-mediated degradation of ErbB3 by sequestering the ubiquitin ligase into ER tubules. PMID: 27353365
  7. NOGO-A/B may be a negative prognostic factor of malignant melanoma. PMID: 27354599
  8. LILRA3 significantly reversed Nogo-66-mediated inhibition of neurite outgrowth and promoted synapse formation in primary cortical neurons through regulation of the ERK/MEK pathway. PMID: 26826187
  9. Nogo-B expression is down-regulated in intrahepatic cholangiocarcinoma, the implication of which, however, remains to be investigated. PMID: 26656426
  10. Data show that the mean peak serum neuroglobin and Nogo-A concentrations were both significantly higher in patients with an unfavorable outcome at 6 months after traumatic brain injury (TBI). PMID: 26472601
  11. RTN4-C knockdown blocks cell cycle progression and cell growth in colorectal cancer cell lines. PMID: 25847052
  12. Epithelial RTN-4B/NOGO-B was downregulated in human and experimental inflammatory bowel disease PMID: 25907690
  13. The Nogo-B-PirB axis controls macrophage-mediated vascular remodeling. PMID: 24278366
  14. a novel mechanism that functionally couples cAMP signaling with the proteolytic turnover of NOGO-A, positively impacting on neurite outgrowth in mammalian brain. PMID: 25331889
  15. The RTN4 del allele could significantly increase NSCLC risk. PMID: 25040983
  16. Identify Nogo-C as a tumor suppressor gene in hepatocellular carcinoma and B-raf as a novel interacting protein. PMID: 24966913
  17. the present study found that Nogo-A depletion was capable of inhibiting HCC SMMC-7721 cell proliferation by promoting G2/M cell cycle arrest and apoptosis. PMID: 24626842
  18. The expression of Nogo-B, in arterial intima, is impeded in the early stages of atherosclerosis. Macrophage infiltration is not accompanied by Nogo-B expression in atherosclerotic arteries. PMID: 24372562
  19. Nogo-A/B expression decreased with increasing squamous cell carcinoma malignancy grade (p=0.026). PMID: 25075030
  20. Neither migration speed, nor cell proliferation, or layer area sizes were influenced by Nogo-A deletion, hence suggesting another role for early postnatal Nogo-A expression in the premigratory zone of the external granule layer. PMID: 24401759
  21. knockdown of NgR enhanced invasion and adhesion but increased cell apoptosis in C6 cells, suggesting that Nogo-66/NgR might have complex effects on glioma cells. PMID: 23982337
  22. Studied premenopausal women with uterine leiomyoma. No significant association was observed between the TATC in/del polymorphism and UL risk, but increased UL risk was associated with CAA in/del polymorphism in the recessive and codominant model. PMID: 23479081
  23. Overexpression of Nogo-B promotes the epithelial-mesenchymal transition in cervical cancer via Fibulin-5. PMID: 23042479
  24. The absence of Nogo-B enhances apoptosis of hepatic stellate cells in experimental cirrhosis. PMID: 23313137
  25. The results demonstrate a significant change in the expression of Nogo-A during the development of the human brain PMID: 23146900
  26. CAA and TATC insertion/deletion polymorphisms of RNT4 gene may not be a useful marker to predict the susceptibility of ASD in Chinese Han population PMID: 22313113
  27. genetic variation in RTN4 3'-UTR contributes to the susceptibility to CSCC PMID: 22320844
  28. The presence of Nogo-A in diseased human muscle biopsies is not limited to ALS, therefore it cannot be the standard for ALS diagnosis. PMID: 21503119
  29. Nogo-A is a useful marker for the diagnosis of oligodendroglioma and for identifying 1p19q codeletion PMID: 21835431
  30. Nogo receptor 3, a paralog of NgR1,functions as a NgR1 co-receptor for Nogo-66. PMID: 22133682
  31. The data identify, for the first time, an effect of Nogo B in the brain and specifically show that its expression is increased in conditions where synaptic plasticity is compromised. PMID: 21111015
  32. Data showd that Nogo-B, a regulator of ER structure, was induced by hypoxia in pulonary artery smooht muscle cells but not the systemic vasculature through activation of the ER stress-sensitive transcription factor ATF6. PMID: 21697531
  33. A multi-domain fragment of Nogo-A protein is a potent inhibitor of cortical axon regeneration via Nogo receptor 1. PMID: 21454605
  34. No significant differences in 3'UTR TATC and CAA insertion/deletion polymorphism genotype and allele frequencies were observed between the ventricular septal defect patients and controls. PMID: 21166502
  35. Nogo-A is highly expressed in oligodendroglial tumors; however, it does not serve as a definite marker specific for oligodendroglial tumors PMID: 20487307
  36. Endogenous Nogo-B, which may exert its effects through ARPC 2/3 and MYL-9, is necessary for the migration and contraction of airway smooth muscle cells. PMID: 21251247
  37. Using leukocytes and endothelial cells, we show mechanistically that the silencing of Nogo-B with siRNA impairs the transmigration of neutrophils and reduces ICAM-1-stimulated phosphorylation of VE-cadherin. PMID: 21183689
  38. These results suggest a role for neuronal Nogo-A in maintaining a spine phenotype in neocortical pyramidal cells PMID: 20938157
  39. Nogo-B may regulate macrophage recruitment after unilateral ureteral obstruction, although it does not greatly affect the degree of tissue injury or fibrosis in this model. PMID: 20971739
  40. Reticulons, the only molecular so far to participate in all three apoptosis signaling pathways, may be a novel player in the progress of atherosclerosis. PMID: 20717916
  41. Epithelial reticulon 4B (Nogo-B) is an endogenous regulator of Th2-driven lung inflammation. PMID: 20975041
  42. Fibulin-5, a secreted extracellular matrix protein, was identified as a binding partner of Nogo-B. PMID: 20599731
  43. verified the molecular interaction of Nogo-A with 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNP), which could act as a conformational stabilizer for the intrinsically unstructured large segment of Amino-Nogo PMID: 19508346
  44. identified Akt1 as a new signaling component of the amino-Nogo pathway. Akt1 phosphorylation is decreased by amino-Nogo. PMID: 20018888
  45. An RTN4-C mutant lacking the C-terminal domain bound to BACE1 comparably to wild-type RTN4-C & reduced Abeta40 & Abeta42 secretion by cells expressing Swedish mutant APP. PMID: 19405102
  46. The alteration in Nogo gene expression in muscle biopsy represents a potential diagnostic tool for the early stages of amyotrophic lateral sclerosis. PMID: 12270696
  47. Elevated expression of Nogo mRNA in schizophrenia was confirmed by RT-PCR. Nogo mRNA was found to contain a CAA insert polymorphism in the 3'-untranslated region. PMID: 12425946
  48. results describe the regulation of nogo expression through its promoter region PMID: 12488097
  49. ASY may be multi-functional, regulating apoptosis, tumor development, and neuronal regeneration [review] PMID: 12510146
  50. ER stress of highly overexpressed Nogo-B may lead to aversive cellular reactions under particular conditions. Our data do not support a function of Nogo-B as a physiological pro-apoptotic protein in certain types of cancer. PMID: 12618765

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Subcellular Location [Isoform A]: Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein; Cytoplasmic side.; [Isoform B]: Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein; Extracellular side. Cell junction.; [Isoform C]: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue Specificity Isoform A: is specifically expressed in brain and testis and weakly in heart and skeletal muscle. Isoform B: widely expressed except for the liver. Highly expressed in endothelial cells and vascular smooth muscle cells, including blood vessels and mesente
Database Links

HGNC: 14085

OMIM: 604475

KEGG: hsa:57142

STRING: 9606.ENSP00000337838

UniGene: Hs.637850

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