Recombinant Human Aquaporin 1 / AQP1 Protein

Beta LifeScience SKU/CAT #: BLA-12189P

Recombinant Human Aquaporin 1 / AQP1 Protein

Beta LifeScience SKU/CAT #: BLA-12189P
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Product Overview

Host Species Human
Accession P29972
Synonym AQP 1 AQP CHIP AQP-1 AQP1 AQP1_HUMAN aquaporin 1 (channel-forming integral protein, 28kDa, CO blood group) aquaporin 1 (Colton blood group) Aquaporin CHIP Aquaporin-1 Aquaporin-CHIP Aquaporin1 Channel forming integral protein 28kDa Channel like integral membrane protein 28 kDa CHIP 28 CHIP28 CO Colton blood group Growth factor induced delayed early response protein MGC26324 Urine water channel Water channel protein CHIP 29 Water channel protein CHIP29 Water channel protein for red blood cells and kidney proximal tubule
Description Recombinant Human Aquaporin 1 / AQP1 Protein was expressed in Wheat germ. It is a Full length protein
Source Wheat germ
AA Sequence MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNV KVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYI IAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQ LVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARS FGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKV WTSGQVEEYDLDADDINSRVEMKPK
Molecular Weight 56 kDa including tags
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.
Subcellular Location Cell membrane; Multi-pass membrane protein.
Protein Families MIP/aquaporin (TC 1.A.8) family
Database References
Tissue Specificity Detected in erythrocytes (at protein level). Expressed in a number of tissues including erythrocytes, renal tubules, retinal pigment epithelium, heart, lung, skeletal muscle, kidney and pancreas. Weakly expressed in brain, placenta and liver.

Gene Functions References

  1. Case-control analyses reveal significant overrepresentation of rare variants in ATP13A3, AQP1 and SOX17, and provide independent validation of a critical role for GDF2 in heritable pulmonary arterial hypertension. PMID: 29650961
  2. Study demonstrated that a region upstream of the AQP1 gene (- 2300 to - 2200 bp) contains an enhancer required for pH-mediated regulation of AQP1 gene expression. PMID: 29554889
  3. H19 acted as AQP1 ceRNA in regulating miR-874. PMID: 30021355
  4. Data show that miR-320 negatively regulates aquaporin 1 (AQP1) expression by targeting its 3' untranslated regions (3'-UTR). PMID: 29538612
  5. The present study represents further confirmation of the hypothesized prognostic role of AQP1, which seems a reliable prognostic indicator. PMID: 29495596
  6. AQP1 may serve a role in glioblastoma multiforme migration, invasion and vasculogenic mimicry formation PMID: 29257313
  7. Adenovirus-mediated human AQP1 expression in hepatocytes improves lipopolysaccharide-induced cholestasis in rats. PMID: 29087027
  8. AQP1 may interact with VEGFA and play a role in vasculogenic mimicry, especially under hypoxic conditions, but the heterogeneity of malignant mesothelioma cells may result in different dominant pathways between patients. PMID: 29104239
  9. AQP1, 3 and 5 expression through the stages of human salivary gland morphogenesis, was examined. PMID: 28766180
  10. AQP1 was elevated in the majority of ovarian cancer tissues. Notably, the present study, to the best of our knowledge, suggests for the first time that AQP1 exhibits a key role in the viability, apoptosis, migration and invasion of ovarian cancer cells. PMID: 28849036
  11. AQP1 is expressed in atherosclerotic lesion neovasculature in human and mouse arteries and AQP1 deficiency augments lesion development in angiotensin II-promoted atherosclerosis in mice. PMID: 28129470
  12. Strong aquaporin 1 protein expression was an independent adverse prognosticator in hilar cholangiocarcinoma. PMID: 27143047
  13. Findings suggest that a defined population of AQP4- and AQP1-expressing reactive astrocytes may modify alpha-syn deposition in the neocortex of patients with Parkinson's Disease. PMID: 26919570
  14. The BRAF V600 mutations were significantly associated with AQP1 expression (P=0.014). Long-term follow-up indicated a reduced progression-free survival (P=0.036) and overall survival (P=0.017) for the AQP1-positive cutaneous melanoma patients. PMID: 26848795
  15. The expression of AQP1 and 3 is a manifestation of physiological adaptation of functionally mature chondrocytes able to respond to the change of their internal environment influenced by extracellular matrix. PMID: 28708257
  16. function of AQP1 in tonicity response could be coupled or correlated to its function in band 3-mediated CO2/HCO3(-) exchange PMID: 28596233
  17. Data show that the expression of aquaporin (AQP) 1, AQP3, AQP5, epithelial Na+ channel (ENaC) and sodium potassium ATPase (Na-K-ATPase) are altered in patients with acute respiratory failure (ARF) due to diffuse alveolar damage (DAD), and the cause of DAD does not seem to influence the level of impairment of these channels. PMID: 27835672
  18. The native AQP1 gene, normally latent in human salivary gland cells, can be activated by both promoter-independent artificial transcription and epigenetic editing of the promoter. PMID: 28072927
  19. data suggest an important functional role of AQP1 in the pathobiology of hypoxia-induced pulmonary hypertension PMID: 28409279
  20. We demonstrated that AQP1-like immunoreactivity and expression are significantly increased in plaques of Peyronie's disease patients Vs controls, implying that AQP1 overexpression might be the consequence of a localized maladaptive response of the connective tissue to repeated mechanical trauma PMID: 26972451
  21. AQP-1 overexpression is associated with prostate cancer progression. PMID: 27817002
  22. Study provides evidence that Mef2c cooperated with Sp1 to activate human AQP1 transcription by binding to its proximal promoter in human umbilical cord vein endothelial cells indicating that AQP1 is a direct target of Mef2c in regulating angiogenesis and vasculogenesis of endothelial cells. PMID: 26923194
  23. AQP1 was overexpressed in cystic cholangiocytes of patients with polycystic liver disease. A tendency of increased AQP1 protein expression in correlation with the cyst size was also found. PMID: 26838488
  24. Aquaporin1 overexpression restored anti-cell proliferation and metastatic effect of si-Gli1. PMID: 27157540
  25. AQP1 expression was significantly lower in hereditary spherocytosis patients and silent carriers than in the simultaneously processed normal control, while no AQP1 decrease was detected in the autoimmune hemolytic anemia sample. The decreased AQP1 expression could contribute to explain variable degrees of anemia in hereditary spherocytosis. PMID: 27465156
  26. High cytoplasmic expression of AQP1 is associated with breast cancer progression. PMID: 26812884
  27. Suggest that sputum AQP1 and AQP5 could be used as diagnostic markers in mild-to-moderate adult-onset asthma. PMID: 26823734
  28. the downregulation of AQP1 impedes extracellular to intracellular fluid transportation. PMID: 26549133
  29. Based on a comparative mutagenic analysis of AQP1, AQP 3, and AQP 4, the results suggest that loop D interactions may provide a general structural framework for tetrameric assembly within the AQP family. PMID: 26786101
  30. The role of AQP1 in malignant pleural mesothelioma. PMID: 26773069
  31. Urinary AQP1 is significantly lower in patients with clear cell renal carcinoma than in controls. Urinary AQP1 increases after nephrectomy in clear cell renal carcinoma patients. PMID: 27295912
  32. AQP1 knockdown can effectively inhibit cell proliferation, adhesion, invasion and tumorigenesis by targeting TGF-beta signaling pathway and focal adhesion genes. PMID: 26176849
  33. These data provide support for a continuous role of KLF2 in stabilizing the vessel wall via co-temporal expression of eNOS and AQP1 both preceding and during the pathogenesis of atherosclerosis. PMID: 26717516
  34. The study demonstrated the abnormal expression pattern of AQP1, AQP2, AQP3, and AQP4 in the kidney tissues of patients with nephrotic syndrome, providing a basis for an improved understanding of the role of aquaporins in the pathogenesis of this disease. PMID: 26261083
  35. The results suggest that AQP1 may facilitate lung cancer cell proliferation and migration in an MMP-2 and-9-dependent manner PMID: 26151179
  36. PBEF regulates the expression of inflammatory factors and AQP1 through the MAPK pathways. PMID: 26178576
  37. the benign subependymomas aquaporins 1 and 4 are dramatically redistributed and upregulated. PMID: 26115524
  38. AQP1 was found to be a marker of a subgroup of aggressive basaloid-like squamous cell carcinomas PMID: 26074259
  39. High AQP1 expression is associated with recurrence in bladder uroepithelial cell carcinoma . PMID: 25987071
  40. The AQP1 rs1049305 single nucleotide polymorphism is associated with running performance, but not relative body weight change, during South African Ironman Triathlons. PMID: 25495276
  41. The data suggest that the increased expression of AQP1 and AQP3 in pterygial tissues may be involved in the pathogenesis of pterygia PMID: 23974882
  42. CAII increases water conductance through AQP1 by a physical interaction between the two proteins. PMID: 25609088
  43. Aquaporin 1 and 3 were upregulated in cervical cancer compared to mild cervicitis and cervical intraepithelial neoplasia 2-3 (P<0.05). PMID: 24918928
  44. Through molecular genotyping we also identified polymorphisms in RhCE, Kell, Duffy, Colton, Lutheran and Scianna loci in donors and patients. PMID: 25582271
  45. Study found a significant correlation between AQP1, AQP3, and AQP5 overexpression and lymph node metastasis in patients with surgically resected colon cancer. PMID: 25721378
  46. the reduction of aquaporins 1 and 3 may be a factor resulting in lumbar intervertebral disc degeneration. PMID: 25299207
  47. AQP1 over-expression effectively inhibited cell proliferation and induced cell growth arrest in G1 phase of K562 cells. PMID: 25252847
  48. Aquaporin-1 is induced in leukocytes of patients with sepsis and exhibits higher expression in septic shock. PMID: 24028651
  49. Report is the first to establish astrocytic water channel loss in a subset of human central pontine myelinolysis (CPM) cases and suggests AQP1 and AQP4 may be involved in the pathogenesis of CPM PMID: 24252214
  50. Aquaporin-1 is associated with arterial capillary proliferation and hepatic sinusoidal transformation contributing to portal hypertension in primary biliary cirrhosis. PMID: 23949237

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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