Recombinantmouseaquaporin-4 (AQP4) Protein (His)

Name: Recombinantmouseaquaporin-4 (AQP4) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02299P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Mus musculus (Mouse) Aqp4.

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Product Overview

Description	Recombinantmouseaquaporin-4 (AQP4) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P55088
Target Symbol	AQP4
Synonyms	Aqp4Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	CPDVELKRRLKEAFSKAAQQTKGSYMEVEDNRSQVETEDLILKPGVVHVIDIDRGEEKKGKDSSGEVLSSV
Expression Range	253-323aa
Protein Length	Partial
Mol. Weight	9.9kDa
Research Area	Others
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	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.
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
Database References	KEGG: mmu:11829 STRING: 10090.ENSMUSP00000078088 UniGene: PMID: 18284610 Aquaporin 4 mislocalization away from astroglia and glia limitans delays the onset of brain edema PMID: 12232046 AQP4 and alpha1-syntrophin colocalized frequently at the astrocyte membrane, especially at the perivascular astrocyte endfoot processes PMID: 12233788 plays a critical role in inner ear fluid homeostasis and hearing PMID: 12359252 role of accumulation in astroglial end-feet in dissipation of bidirectional water flow between blood and brain PMID: 12578959 AQP-4 provides the principal route for water transport in astrocytes. PMID: 14576087 water flux through perivascular AQP4 is needed to sustain efficient removal of K+ after neuronal activation PMID: 14597704 AQP4 is expressed in brain endothelial cells & in the perivascular membranes of astrocyte endfeet. There are 3 distinct & serially coupled pools of AQP4 at the brain-blood interface. PMID: 14734638 Sarcolemma vesicles from mdx mice show AQP4 loss from the plasma membrane & a big reduction in water permeability, implying a major role for aquaporins in skeletal muscle physiology & involvement of AQP4 in molecular changes in muscles of DMD patients. PMID: 15033928 higher-order organization of AQP4 increases single-channel osmotic water permeability by one order of magnitude and that differential cellular expression levels of the two isoforms could regulate this organization. PMID: 15149973 AQP4-mediated transcellular water movement is crucial for fluid clearance in vasogenic brain edema. PMID: 15208268 a novel role for AQP4 as a regulator of brain extracellular space PMID: 15371505 AQP4 deletion in mice is neuroprotective in a transient ischemia model of retinal injury, suggesting the possible use of AQP4 inhibitors in retinal vascular occlusive and ischemic diseases. PMID: 15557457 AQP4-labeled astrocytic processes surround blood vessels, neuronal perikarya and processes, and both asymmetric and symmetric synapses: the protein may be involved in the regulation of water fluxes around both inhibitory and excitatory synapses. PMID: 15789430 Data show that the sustained inhibition of gastric secretion due to tumours producing PYY/enteroglucagon in transgenic mice is associated with an increase in AQP4 expression and a down-regulation of H(+)/K(+)-ATPase in parietal cells. PMID: 15898955 aquaporin-4 has species-specific roles in astrocytes and a functional relationship with Connexin43 PMID: 16103109 Protective effect of AQP4 on brain swelling in bacterial abscess. AQP4 induction may reduce vasogenic edema associated with cerebral infection. PMID: 16181429 Lead exposure induced a significant, 40%, increase in water permeability in astrocytes expressing AQP4, but had no effect on permeability in astrocytes not expressing AQP4. May contribute to acute lead intoxication. PMID: 16203098 The lack of AQP4 expression is accompanied by sex- and region-specific alterations in brain amino acid and monoamine metabolism in mice. PMID: 16237719 the involvement of aquaporin-4 in astroglial cell migration, which occurs during glial scar formation in brain injury, stroke, tumor and focal abscess. PMID: 16303850 These results implicate AQP4 in the expression and termination of seizure activity and support the hypothesis that AQP4 is coupled to potassium homeostasis in vivo. PMID: 16470808 These results suggest that AQP4, but not AQP1 or AQP9, may play an important role in water movement associated with the pathophysiology of edema after transient cerebral ischemia in the mouse. PMID: 16511868 Modulation of AQP4 expression or function may be a novel therapeutic strategy for a variety of cerebral disorders including stroke, tumor, infection, hydrocephalus, epilepsy, and traumatic brain injury. PMID: 16564496 A significant increase in the expression levels of AQP1 and AQP4 was found in mice at 270 dpi, the time corresponding with the appearance of PrP(res) immunoreactivity in Western blots and typical spongiform lesions in the brain. PMID: 16871401 These findings provide direct evidences for the first time that aquaporin-4 plays an important role in the function of glutamate transporters. PMID: 17074507 These findings reveal for the first time that AQP4 regulates not only water and ion homeostasis but also the functions of ovarian hormone and neurotransmitter. PMID: 17196551 AQP4 showed a heterogeneous distribution in the central nervous system, but in some areas, an inverse correlation between AQP4 and extracellular matrix components has been observed, suggesting a complementary role for maintenance of water homeostasis PMID: 17349777 This study demonstrates that AQP4 is important in the MPTP neurotoxic process and indicates that the therapeutic strategy targeted to astrocytic modulation with AQP4 may offer a great potential for the development of new treatment for PD. PMID: 17353068 In conclusion, AQP4 mediates bidirectional transport of water across astrocytes during HI and reoxygenation. AQP4 manipulation may serve as a novel therapeutic strategy during different periods of hypoxic-ischemic brain edema in neonates. PMID: 17437301 Evidence against functionally significant AQP4 modulation of Muller cell Kir4.1 potassium channel functionin retinal Muller cells. PMID: 17525153 aquaporin-4 participates in the regulation of neurotransmitter release induced by depolarizing stimuli. PMID: 17611025 A marked increase in AQP4 was observed in mice at the terminal stage of BSE, when they had a wide range of clinical signs, whereas no increase could be observed in the early stage before the onset of the clinical signs. PMID: 17868659 This study report multiple lines of evidence against functionally significant AQP4-Kir4.1 interactions. PMID: 17869537 Palmitoylated dystrobrevin restored alpha-syntrophin and aquaporin-4 (AQP4) to the mdx sarcolemma but was unable to recruit beta-dystroglycan or the sarcoglycans PMID: 18057022 AQP4 is essential for the maintenance of blood-brain barrier integrity. PMID: 18281883 Muller glial cells respond to excessive light with an alteration in the localization of aquaporin-4 protein; this alteration is thought to be a response to the edema in the outer retina and may support the resolution of edema. PMID: 18328627 AQP4 deficiency alleviates proinflammatory cytokine release from astrocytes, in association with the SPHK1/MAPK/AKT pathway. PMID: 29956748 Low expression of AQP4 is associated with Human immunodeficiency virus-associated nephropathy. PMID: 29608911 This study demonstrated that the significant improvement in blood-brain barrier (BBB) permeability was observed in the AQP4-deficient ALS mouse model. PMID: 29154923 Brain water content decreased following treatment with 3% HS relative to the TBI group. This was accompanied by decreases in AQP4, TNF-alpha, and IL-1beta mRNA and protein levels. PMID: 29600800 Treatment with goreisan significantly decreased both brain water content and AQP4 expression in the ischemic brain at 24 hours after middle cerebral artery occlusion. PMID: 29153303 The findings of this study demonstrated a novel molecular mechanism involving the SUR1-TRPM4-AQP4 complex to account for bulk water influx during astrocyte swelling. PMID: 28906027 The findings of this study suggest that AQP4 KO leads to increased aggregation of Cx43 into gap junctions and provide a putative mechanistic basis for the enhanced tracer coupling in hippocampi of AQP4 KO mice. PMID: 28551776 Interaction of the IgG-AQP4 complex with FcgammaRs triggers coendocytosis of the excitatory amino acid transporter 2. PMID: 28461494 The diffusive and AQP4-independent solute transport in rodent brain parenchyma has been demonstrated. PMID: 28826498 Present study demonstrated that AQP4 depolarization is a widespread pathological condition and may contribute to motor neuron degeneration in ALS. PMID: 28627708 Dataindicate that astrocytes in the substantia nigra differ from those in neocortex by showing a higher level of aquaporin-4, particularly in those endfoot membrane domains that mediate water exchange between brain and blood. PMID: 28735099 AQP4-specific T cells contribute to AQP4-targeted CNS autoimmunity PMID: 27940915 AQP-4 expression was significantly elevated in the ipsilateral hemisphere in the first 24h following cerebral cortical injury in mice and this could be correlated with worsening of neurological function. Over the next 48h, there was a trend towards decrease in AQP-4 expression that was associated with partial recovery of neurological function. PMID: 28645746 Study shows that the size of the aquaporin-4 (Aqp4) pool differs considerably between brain regions, roughly mirroring regional differences in Aqp4 mRNA copy numbers. PMID: 27629271

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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.

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