Recombinant Human Aquaporin-5 (AQP5) Protein (His-KSI)

Name: Recombinant Human Aquaporin-5 (AQP5) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-00149P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Aquaporin-5 (AQP5) Protein (His-KSI) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	P55064
Target Symbol	AQP5
Synonyms	(AQP-5)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	LFPNSLSLSERVAIIKGTYEPDEDWEEQREERKKTMELTTR
Expression Range	225-265aa
Protein Length	Partial
Mol. Weight	20.3 kDa
Research Area	Signal Transduction
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 fluid secretion in salivary glands. Required for TRPV4 activation by hypotonicity. Together with TRPV4, controls regulatory volume decrease in salivary epithelial cells. Seems to play a redundant role in water transport in the eye, lung and in sweat glands.
Subcellular Location	Apical cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein.
Protein Families	MIP/aquaporin (TC 1.A.8) family
Database References	HGNC: 638 OMIM: 600231 KEGG: hsa:362 STRING: 9606.ENSP00000293599 UniGene: PMID: 29951954 these results suggest that AQP5 silencing enhances the sensitivity of colorectal cancer (CRC) cells to 5-FU, and the underlying mechanism is related to inhibition of the Wnt-beta-catenin pathway. AQP5 could be a useful therapeutic target for CRC treatment. PMID: 29390193 Structural basis for mutations in human AQP5 associated with keratoderma has been described. PMID: 29799470 The urea transporter subtypes, UT-A1 and UT-B1, were expressed in the skin basal cell layer and exocrine sweat glands. The abundance of UT-A1 and UT-B1 in uremic sweat glands was significantly increased in UP, while the expression of AQP5 was decreased. PMID: 29279852 we demonstrated that AQP5 gene silencing could inhibit the proliferation, reduce the migration and promote the apoptosis of human glioma cells by suppressing EGFR/ERK/p38 MAPK signaling pathway PMID: 28404978 Data suggest that urine AQP5/creatinine ratio is significantly higher in patients with diabetic nephropathy than in control subjects, subjects diabetes, or subjects with nephropathy of unknown etiology; urine AQP5/creatinine ratio increases with stage of diabetic nephropathy; this biomarker may improve clinical models in distinguishing diabetic nephropathy from normal controls and subjects with type 2 diabetic alone. PMID: 27103565 We present the first Danish family diagnosed with autosomal dominant palmplantar ketratoderma of Bothnian type resulting from c.562C>T, p.Arg188Cys in the AQP5 gene. PMID: 27255181 Findings show that overexpression of aquaporin 5 (AQP5) activated epithelial-mesenchymal transition (EMT) in colorectal cancer (CRC) cells. PMID: 28833571 RAQP5 protein expression in breast cancer.Rac1 is a potential downstream signaling partner of AQP5 in breast cancer. PMID: 28958942 The AQP5 genotype may influence survival following lipopolysaccharides by altering neutrophil cell migration. PMID: 27871297 Mucins and AQP5 gene expression were significantly higher in patients with OME relative to controls. A 2-fold increase in AQP5 correlated with increased effusion viscosity (1.94 mL/mg; 95% CI, 0.08-3.80 mL/mg). PMID: 28594978 The severity of preterm infants with acute respiratory distress syndrome was associated with the plasma level of AQP5; the more severe of the disease, the higher levels of plasma AQP5. PMID: 25877715 AQP5 is up-regulated in hepatocellular carcinoma (HCC) cell line. AQP5 promotes hepatocellular carcinoma metastasis via NF-kappa B-regulated epithelial-mesenchymal transition. PMID: 28619511 Double IF showed the co-localization of AQP5 and LC3B on BafA1-treated heated cells. In conclusion, we demonstrated that heat shock decreased AQP5 on cellular membranes and in the cytoplasm by activating autophagic degradation, and heat shock and AQP5 knockdown exerted similar anticancer effects, suggesting that heat shock exerts anticancer effects via the autophagic degradation of AQP5. PMID: 28358429 we analyzed the urine excretion of AQP5 and AQP2 via exosomes, in 35 diabetic patients: 12 normoalbuminuric with normal renal function (DM), 11 with proteinuric nondiabetic nephropathy (NDN), and 12 with histological diagnosis and classification of DN. urinary AQP5 and AQP2 were significantly increased in DN patients. PMID: 28246612 this study shows that S-allylmercapto-l-cysteine can suppress AQP5 secretion using the cell model of chronic obstructive pulmonary disease PMID: 27517516 The current study suggests AQP5 rs1964676 as a new potential prognostic marker in patients with EBC involved in AQP5 expression PMID: 27978515 Adjusting AQP5 protein levels could be considered a therapeutic strategy for the treatment of acute pulmonary edema induced by H2S and other hazardous gases PMID: 28088675 nuclear matrix protein 4 overexpression increased Aquaporin 5 mRNA expression by 2.5-fold in HEK293 cells PMID: 27058007 The findings presented here add further support to mutations in AQP5 being responsible for this particular subtype of NEPPK and also have implications for the optimal initial genetic screening of other British individuals with this clinical diagnosis. PMID: 26032342 AQP5 plasma membrane abundance in transfected HEK293 cells is rapidly and reversibly regulated by at least three independent mechanisms involving phosphorylation at Ser156, protein kinase A activity and extracellular tonicity. PMID: 26569106 AQP5 can be both overexpressed and lost in subgroups of prostate cancers PMID: 26614400 AQP5 defined a subset of patients with Bcl-2-negative and p16-negative tumours with a poor clinical outcome. PMID: 26074259 Histamine downregulates AQP5 production in human nasal epithelial cells by inhibiting cyclic adenosine monophosphate-responsive element binding protein (CREB) phosphorylation at serine 133. PMID: 25781725 Aquaporin-5 is expressed in adipocytes with implications in adipose differentiation. PMID: 25631586 These results indicate that NFAT5 plays important roles in proliferation and migration of human lung adenocarcinoma cells through regulating AQP5 expression, providing a new therapeutic option for lung adenocarcinoma therapy. PMID: 26299924 The hyperosmotic induction of AQP5 and VEGF in retinal pigment epithelial cells was in part dependent on activation of NFAT5. PMID: 25878490 AQP5 was strongly localized in the apical membrane and weakly localized in the cytoplasm of secretory epithelial cells. PMID: 25218052 The AQP5 protein is up-regulated in prostate cancer and is closely related to advanced stage, lymph node metastasis, and poor prognosis. AQP5 expression was associated with cell proliferation and migration. PMID: 25217331 In colorectal adenocarcinoma, 31.1% had high levels of expression of AQP5, 64.4% exhibited a moderate level of staining, and 4.4% had an absence of AQP5 staining. AQP5 was only occasionally detected in para-neoplastic (6.67%) and normal tissues (6.67%). PMID: 25109507 Down-regulated aquaporin 5 inhibits proliferation and migration of human epithelial ovarian cancer 3AO cells. PMID: 25298246 These findings indicate that AQP5-mediated regulation of microtubule dynamics modulates airway epithelial barrier properties and epithelial function. PMID: 22715407 Survival of patients with a high AQP-5/PTEN coexpression was longer than that of patients with a low coexpression (p = 0.003). PMID: 24217644 High AQP5 expression is associated with breast cancer. PMID: 24114055 So these results indicate that AQP5 is associated with drug resistance of colon cancer, and that the AQP5-P38 MAPK pathway may represent a potential drug target to improve drug resistance of colon cancer cells. PMID: 24752576 We described a Chinese family with palmoplantar keratoderma Bothnia type in which we identified a gain-of-function mutation in AQP5. PMID: 23867895 By directing cellular localization of TRPC1 and AQP5 channels and by selectively regulating the functional assembly TRPC1-STIM1 channels, Cav1 is a crucial determinant of SG fluid secretion. PMID: 23203809 AQP5-L51R does not exhibit the H2O or CO2 permeability of the wild-type protein. PMID: 23842530 Mutations in AQP5 cause autosomal-dominant diffuse nonepidermolytic palmoplantar keratoderma. PMID: 23830519 The regulated AQP5 translocation may contribute to sweat secretion by increasing the water permeability of apical plasma membranes of sweat glands. PMID: 23473857 AQP5 polymorphism A(-1364)C is associated with peritumoral brain edema in meningioma patients PMID: 23392848 Our findings clearly indicate that binding of anti-M3R autoantibodies to the receptor, which was verified by immunoprecipitation, suppresses AQP5 trafficking to the membrane and contribute to impaired fluid secretion in SjS. PMID: 23382834 Overexpression of AQP5 is associated with lymphatic Metastasis in gastric carcinoma. PMID: 23436048 These observations suggest that AQP5 plays a key role in cervical cancer PMID: 22048942 These observations suggest that sialadenosis is associated with a different AQP5 expression and distribution pattern in salivary acinar cells. PMID: 23160677 A lipid, phosphatidylserine, is bound to AQP5 in the central pore, totally occluding it and inhibits the function of the central pore with an IC(50) in the micromolar range. PMID: 23176748 The variant G allele of AQP5 polymorphism rs3736309 reduces the risk of Meniere's disease. PMID: 23352976 AQP5 is a significant component of lens fiber cell membranes, representing the second most abundant water channel in these cells. PMID: 23313152 The potential functions of AQP2 and AQP5 are in the resorption and secretion of endolymph. (Review) PMID: 22732097 TNF-alpha inhibition of AQP5 expression in human salivary gland acinar cells is due to the epigenetic mechanism by suppression of acetylation of histone H4. PMID: 21973049

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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