Recombinant Rat Aquaporin-4 (Aqp4)

Code CSB-CF001964RA
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Source in vitro E.coli expression system
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Product Details

Target Names
Aqp4
Uniprot No.
Alternative Names
Aqp4; Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4
Species
Rattus norvegicus (Rat)
Expression Region
1-323
Target Protein Sequence
MSDGAAARRWGKCGPPCSRESIMVAFKGVWTQAFWKAVTAEFLAMLIFVLLSVGSTINWGGSENPLPVDMVLISLCFGLSIATMVQCFGHISGGHINPAVTVAMVCTRKISIAKSVFYITAQCLGAIIGAGILYLVTPPSVVGGLGVTTVHGNLTAGHGLLVELIITFQLVFTIFASCDSKRTDVTGSVALAIGFSVAIGHLFAINYTGASMNPARSFGPAVIMGNWENHWIYWVGPIIGAVLAGALYEYVFCPDVELKRRLKEAFSKAAQQTKGSYMEVEDNRSQVETEDLILKPGVVHVIDIDRGDEKKGKDSSGEVLSSV
Protein Length
Full length protein
Tag Info
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.
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
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.

Customer Reviews and Q&A

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Target Background

Function
Forms a water-specific channel. Plays an important role in brain water homeostasis and in glymphatic solute transport. Required for a normal rate of water exchange across the blood brain interface. Required for normal levels of cerebrospinal fluid influx into the brain cortex and parenchyma along paravascular spaces that surround penetrating arteries, and for normal drainage of interstitial fluid along paravenous drainage pathways. Thereby, it is required for normal clearance of solutes from the brain interstitial fluid, including soluble beta-amyloid peptides derived from APP. Plays a redundant role in urinary water homeostasis and urinary concentrating ability.
Gene References into Functions
  1. The hydrocephalus rat model was established successfully, and hydrocephalus rats showed a higher AQP4 level. Silencing AQP4 aggravated the hydrocephalus, with enlarged lateral ventricles and destruction of ependymal integrity and blood-brain barrier. PMID: 29921834
  2. These findings showed that eclamptic seizures induced cell death and that upregulation of AQP4 and AQP9 may play an important role in this pathophysiological process. PMID: 29351212
  3. HMGB1 upregulates AQP4 expression and promotes cell swelling in cultured spinal cord astrocytes after oxygen-glucose deprivation/reoxygenation PMID: 29178911
  4. down-regulation of AQP4 by lentiviral or shRNA vector reversed the brain edema and neurologic deficit induced by hypoxia-ischemia. PMID: 27726111
  5. Taken together, our results show that miR-145 plays an important role in protecting astrocytes from ischemic injury by downregulating AQP4 expression. These findings may highlight a novel therapeutic target in cerebral ischemic stroke. PMID: 29057271
  6. Interaction of the IgG-AQP4 complex with FcgammaRs triggers coendocytosis of the excitatory amino acid transporter 2. PMID: 28461494
  7. The diffusive and AQP4-independent solute transport in rodent brain parenchyma has been demonstrated. PMID: 28826498
  8. Lentivirus-mediated AQP4 inhibition accelerated motor function recovery after spinal cord injury, which was related to the up-regulation of NGF. This work reports the relationship between AQP4 and NGF in spinal cord injury for the first time. PMID: 28549966
  9. Spinal cord injury increases AQP4 expression in the spinal cord white matter and methylprednisolone diminishes this increase to baseline levels PMID: 28572712
  10. AQP4 forms protein complexes with GLT-1 and MOR in brain tissue and primary cultured astrocytes. Residues 252 to 323 is the site of AQP4 interaction with GLT-1. PMID: 28341892
  11. AQP4ex expression can be positively modulated by gentamicin treatment, demonstrating the possibility of regulating the AQP4 translational readthrough frequency PMID: 28206694
  12. Data suggest that AQP4 (aquaporin-4) and interleukin-1beta (IL1b) are involved in regulation of apoptosis; here, silencing AQP4 with small interfering RNA protects articular chondrocytes in culture from IL1b-induced apoptosis and stimulates cell proliferation. PMID: 29066483
  13. Results provide a novel, complement-dependent mechanism in neuromyelitis optica spectrum disorder by which AQP4-IgG binding to astrocytes injures surrounding oligodendrocytes, resulting in early and marked demyelination. PMID: 28567523
  14. Aquaporin 4 affects the dynamics of cell swelling and regulatory volume decrease in astrocytes exposed to hypo-osmotic conditions. PMID: 28978666
  15. The expressions of AQP4 were colocalized with GFAP. Protein levels of VEGF in the hyperglycemic rat retina were significantly higher than controls. FACS analyses showed that exposure to VEGF enlarged Muller cells, while exposure to TGN-020 suppressed the enlargement. PMID: 28303331
  16. interation of DG with laminin and dynamin is involved in the regulation of AQP4 internalization PMID: 27788222
  17. data propose that AQP4 belongs to the growing list of NH3-permeable water channels. PMID: 27435677
  18. this study shows that upregulation of AQP4 is associated with acute lung injury induced by intestinal ischemia reperfusion PMID: 27236300
  19. Age-related modulations of AQP4 and Caveolin-1 in the hippocampus predispose the toxic effect of Phoneutria nigriventer spider venom. PMID: 27886057
  20. AQP4 interference reduces CBT edema formation, and ADC value may predict TBI severity. PMID: 27930615
  21. The findings indicate that mRNA expression of AQP4 varies with age. PMID: 27525904
  22. AQP4 inhibition could weaken excitotoxicity in epileptogenesis by reducing proinflammatory cytokines in the hippocampus. PMID: 27706789
  23. The AQP4 protein in Sprague-Dawley (SD) rats was expressed after experimental intraventricular hemorrhage to investigate the possible pathogenesis of chronic posthemorrhagic hydrocephalus. PMID: 27188736
  24. Ulinastatin can effectively reduce the cardiac function damage caused by cardiopulmonary resuscitation, which could be related with the increased SSAT2 and decreased AQP4. PMID: 26617791
  25. The alteration of DG expression could regulate that of AQP4 expression after Traumatic Brain Injury . PMID: 26583111
  26. AQP4 may be involved in the occurrence of traumatic brain edema via changes in expression, which act as a defense response. PMID: 26459070
  27. These results suggest that the stressful short-period and slow-paced treadmill exercise suppressed NHE1 and AQP4 expression resulting in the amelioration of brain edema at least partly via the moderate increase in plasma corticosterone levels. PMID: 26724742
  28. AQP4 is overexpressed in glial cells, resulting in their swelling and adversely affecting cerebral homeostasis. Once PMID: 26385393
  29. The down-regulation of AQP4 was associated with crush-induced optic nerve edema. PMID: 25479407
  30. Findings shows that focal brain injury results in an early development of brain edema involving both cytotoxic and vasogenic components, a persistent blood-brain barrier breakdown and a temporary decrease in aquaporin 4. PMID: 25770057
  31. Aquaporin 4 expression decreased in response to ischemia/reperfusion in the remote ischemic post-conditioning (RIPC) group. RIPC could attenuate focal cerebral ischemia/reperfusion injury, and was related with the down-regulation of AQP4 in astrocytes. PMID: 25907740
  32. Phosphorylation at serine 276 is necessary for AQP4 translocation in response to changes of tonicity. PMID: 26013827
  33. Results show that AQP4 is up-regulated in both the rat hippocampus and the cortex during neurodegenerative processes triggered by trimethyltin chloride PMID: 24912027
  34. a role for beta-dystroglycan in targeting and stabilizing AQP4 channel in astrocytic cells, which may be critical for water homeostasis in brain. PMID: 25545558
  35. results indicate that ERK1/2 pathway down-regulates AQP4 expression in scratch-injured astrocytes, and ERK1/2 pathway might be a novel therapeutic target in reversing the effects of astrocytes that contribute to traumatic brain edema PMID: 25800444
  36. AQP4 and Cx43 had two distinct mechanisms underlying brain edema formation within and surrounding the glioma. PMID: 25373717
  37. Hypoxia triggers cortical release of CRF, which acts on CRFR1 to trigger signaling of cAMP/PKA in cortical astrocytes, leading to activation of AQP4 and cerebral edema. PMID: 25146699
  38. Lactuside B protected against cerebral edema and nerve cell damage caused by cerebral ischemic injury by decreasing the expression of AQP4 and TRPM7 mRNAs in the cerebral cortex of rats. PMID: 24817288
  39. Phosphorylation at COOH-terminal serine residues is not required for proper plasma localization of AQP4. PMID: 25231107
  40. MMP2/AQP4/AQP9 mRNA and protein expression. PMID: 24828425
  41. It is an water channel protein, involves in brain edema augmentation under ethanol consumption. PMID: 25223087
  42. The simulation studies showed a continuous movement of water in a single file across pore of unphosphorylated as well as phosphorylated rAQP4. PMID: 23651078
  43. The co-immunoprecipitation experiments showed a direct interaction between AQP4 and CFTR in cultured rat Sertoli cells. PMID: 24657265
  44. The correlations between ADC values and the brainstem AQP4 expression at different time points suggest that AQP4 expression follows an adaptative profile to the severity of brain edema. PMID: 24282821
  45. AQP4 expression was down-regulated during the angioedema attack, but AQP4 expression was upregulated during intracellular edema. PMID: 24238521
  46. Increased aquaporin-4 expression is observed in rat spinal cord following post-traumatic syringomyelia. PMID: 23441695
  47. The data of this study indicate a lack of phosphorylation of Ser(111) and of phosphorylation-dependent gating of AQP4. PMID: 23616425
  48. Mislocalization of AQP4 in a model of temporal lobe epilepsy reflects a loss of astrocyte polarization. PMID: 23357720
  49. AQP4 and NPY may be involved in the pathogenesis of intestinal dysfunction after traumatic brain injury. Increased NPY levels may be responsible for intestinal ischemia and hypoxia, and AQP4 may play an important role in intestinal edema. PMID: 23622727
  50. Silencing of AQP4 expression blocks astrocyte swelling after oxygen-glucose deprivation and reoxygenation. PMID: 23142737

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Subcellular Location
Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Endosome membrane. Cell membrane, sarcolemma; Multi-pass membrane protein. Cell projection.
Protein Families
MIP/aquaporin (TC 1.A.8) family
Tissue Specificity
Detected in cerebellum. Detected on pericapillary astrocyte endfeet in cerebellum, and in skeletal muscle. Detected in glial lamellae in the hypothalamus (at protein level). Abundant in mature brain cortex, cerebellum and spinal cord. Highly expressed in
Database Links
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