Recombinant Mouse Reticulon-4(Rtn4) ,partial

Code CSB-YP860001MO
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Source Yeast
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Code CSB-EP860001MO
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Source E.coli
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Code CSB-EP860001MO-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-BP860001MO
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Source Baculovirus
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Code CSB-MP860001MO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Rtn4
Uniprot No. Q99P72
Alternative Names Rtn4; Kiaa0886; Nogo; Reticulon-4; Neurite outgrowth inhibitor; Nogo protein
Species Mus musculus (Mouse)
Protein Length Partial
Tag Info The following tags are available.
N-terminal His-tagged
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.
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

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.; 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. Nogo-A and NgR1 interactions may contribute to axonal branching in lateral olfactory tract development PMID: 28000762
  2. 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
  3. The results of this study showed the Nogo-B is expressed in the floor plate of mouse embryo, which probably mediates axon crossing in the spinal cord by repelling axons out of the midline when they start upregulate NgR. PMID: 28543060
  4. induction of hepatic NgBR expression by atorvastatin mainly depended on inactivation of extracellular signal-regulated kinases 1/2 (ERK1/2) and protein kinase B (Akt). Taken together, our study demonstrates that statins inhibit NAFLD mainly through activation of NgBR expression. PMID: 29217477
  5. We show here that Nogo-A is highly expressed not only in excitatory, but also in inhibitory, Parvalbumin positive neurons in the adult hippocampus. By this means our current and previous data indicate that Nogo-A loss-of-function positively influences spatial learning by priming the neuronal structure to a higher plasticity level. PMID: 27349794
  6. Nogo-A signaling in the adult nervous system modulates the spine actin cytoskeleton within minutes to control structural plasticity at dendritic spines of CA3 pyramidal neurons. Acute Nogo-A loss-of-function transiently increases F-actin stability and results in an increase in dendritic spine density and length. Nogo-A acutely restricts AMPAR insertion and membrane potential amplitude at hippocampal synaptic sites. PMID: 26748478
  7. deregulation of Nogo-C by miRNA may be a potential therapeutic target for ischemia-related heart diseases. PMID: 27763637
  8. stimulated angiogenesis upon Nogo-A gene deletion results in the insertion of complete capillary micro-networks and not just single vessels into existing vascular networks. PMID: 27927704
  9. The increase of Nogo-A expression can selectively influence the distribution of inwardly rectifying potassium channel 4.1 in glia but is not essential for inwardly rectifying potassium channel 4.1-mediated potassium conductance at the plasma membrane in physiological conditions. PMID: 27276652
  10. Nogo-A restricts visual experience-driven plasticity of the optokinetic response and plays a role in the segregation and maintenance of retinal projections to the brain. PMID: 25284126
  11. The Ad-Nogo-B-treated mice also had less severe lung injury, less alveolar protein exudation, and a higher number of macrophages but less neutrophil infiltration compared with Ad-RFP-treated mice. PMID: 26174362
  12. Nogo knockdown (KD) in non-transformed and Ras-transformed cells both enhanced virus-induced IFN response, suggesting that both cleaved and uncleaved Nogo can suppress IFN response. PMID: 25946643
  13. the Nogo/NgR signal might be involved in multiple processes in various inflammation-associated CNS diseases. PMID: 26472924
  14. identifies Nogo-B as a key inhibitor of local sphingolipid synthesis PMID: 26301690
  15. The findings indicate a critical role of Nogo-B and GRAMD4 in trafficking of TLR9. PMID: 25917084
  16. Epithelial RTN-4B/NOGO-B was downregulated in human and experimental inflammatory bowel disease PMID: 25907690
  17. study represents the first side-by-side comparison between PTEN deletion and Nogo deletion on Corticospinal tract regeneration and sprouting. PMID: 25904793
  18. the downregulation of Nogo-A protein might have a role in the altered synaptic plasticity during aging. PMID: 25078756
  19. Nogo receptor inhibition enhances functional recovery following lysolecithin-induced demyelination in mouse optic chiasm. PMID: 25184636
  20. The Nogo-B-PirB axis controls macrophage-mediated vascular remodeling. PMID: 24278366
  21. These results indicate that during maturation of cultured midbrain (dopaminergic) neurons, intracellular Nogo-A supports neurite growth initiation and branch formation. PMID: 24157929
  22. The sphingolipid receptor S1PR2 is a receptor for Nogo-a repressing synaptic plasticity. PMID: 24453941
  23. a direct correlation between ER morphology and SOCE and highlight the importance of RTN4 in cellular Ca(2+) homeostasis PMID: 24558039
  24. the association of RhoGDIalpha with TROY contributed to TROY-dependent RhoA activation and neurite outgrowth inhibition after Nogo-66 stimulation. PMID: 24129566
  25. Nogo-A is closely involved in the neuronal response to hypoxic and oxidative stress. PMID: 23909438
  26. These findings identify Nogo-A as an important negative regulator of developmental angiogenesis in the CNS. PMID: 23625008
  27. The absence of Nogo-B enhances apoptosis of hepatic stellate cells in experimental cirrhosis. PMID: 23313137
  28. Reticulon 4B (Nogo-B) facilitates hepatocyte proliferation and liver regeneration in mice. PMID: 23299899
  29. Data from knockout/diabetic mice suggest that down-regulation of Nogo-A up-regulates insulin secretion in beta cells and improves glucose clearance; Nogo-A is expressed in pancreatic islets and is involved in exocrine function/glucose homeostasis. PMID: 23274909
  30. findings reveal a new function for Nogo-A and NgR1 in the homeostatic regulation of the pace of neurogenesis and neuroblast migration. PMID: 23223298
  31. Nogo-A appears as a negative regulator of Purkinje cell (PC) input synapses, which orchestrates cerebellar connectivity through regulation of synapse morphology and the size of the PC dendritic tree. PMID: 23277570
  32. Noga-A and Nogo receptor are actively regulated in experimental autoimmune encephalomyelitis (EAE) lesions, indicating a specific time window for localized axonal regeneration in the acute phase of EAE. PMID: 22964785
  33. Nogo-A overexpression in RGCs in vivo or in the neuronal cell line F11 in vitro promoted regeneration, demonstrating a positive, cell-autonomous role for neuronal Nogo-A in the modulation of axonal regeneration. PMID: 22193546
  34. Nogo-A establishes spatial segregation and extent of oligodendrocyte myelination in the developing central nervous system. PMID: 22160722
  35. increased Nogo-A expression and ultrastructural changes of the endoplasmic reticulum PMID: 21980529
  36. 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
  37. a novel mechanism by which PIR-B-mediated regulation is achieved differentially but competitively via MHCI and Nogo in cells of the immune system PMID: 21636572
  38. A multi-domain fragment of Nogo-A protein is a potent inhibitor of cortical axon regeneration via Nogo receptor 1. PMID: 21454605
  39. Nogo-B regulates liver fibrosis, at least in part, by facilitating the TGFbeta/Smad2 signaling pathway in myofibroblasts. PMID: 21480333
  40. 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
  41. NogoA could thus serve as an important negative regulator of functional and structural plasticity in mature neuronal networks. PMID: 21262805
  42. use 2 models of inflammation to show that endothelial Nogo-B regulates leukocyte transmigration and intercellular adhesion molecule-1 (ICAM-1)-dependent signaling PMID: 21183689
  43. These results suggest a role for neuronal Nogo-A in maintaining a spine phenotype in neocortical pyramidal cells. PMID: 20938157
  44. Nogo-mediated inhibition of neuritic sprouting contributes to the disease progression in an APP transgenic model of Alzheimer's disease in a way that is mechanistically distinct from what has been proposed for Rtn3 or NgR. PMID: 20433905
  45. Epithelial reticulon 4B (Nogo-B) is an endogenous regulator of Th2-driven lung inflammation. PMID: 20975041
  46. This study suggested that Nogo-A and its receptor complex play a role in the interplay of adhesive and repulsive cell interactions in radial migration during cortical development. PMID: 20093372
  47. In a study of in vitro slice cultures of neonatal hippocampus, Nogo-A plays a major role in stabilizing and maintaining the architecture of pyramidal neurons. PMID: 20926648
  48. Nogo-A is a 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 PMID: 20573699
  49. Data show the increased expression of Nogo-A mRNA and Nogo-A protein in brain tissue of neonatal mice with ischemic-hypoxic brain damage. PMID: 17229389
  50. While Nogo may modulate axon sprouting, it does not play a major role in central nervous system axon regeneration failure. PMID: 20547125

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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: highly expressed in brain but not deteceted in aorta, femoral and carotid arteries. Isoform A: main isoform in neurons but isoforms B and C are also expressed. Isoform D is expressed at very low levels. Isoform B is highly expressed in endothel
Database Links

KEGG: mmu:68585

STRING: 10090.ENSMUSP00000099907

UniGene: Mm.192580

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