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company name :
MyBioSource
product type :
protein
product name :
Recombinant Human Aquaporin-1
catalog :
MBS948542
quantity :
0.05 mg (E-Coli)
price :
190 USD
more info or order :
product information
catalog number :
MBS948542
products type :
Recombinant Protein
products full name :
Recombinant Human Aquaporin-1
products short name :
Aquaporin-1
products name syn :
Aquaporin-CHIP; Urine water channel; Water channel protein for red blood cells and kidney proximal tubule
other names :
aquaporin-1 isoform 2; Aquaporin-1; aquaporin-1; aquaporin 1 (Colton blood group); Aquaporin-CHIP; Urine water channel; Water channel protein for red blood cells and kidney proximal tubule
products gene name :
AQP1
other gene names :
AQP1; AQP1; CO; CHIP28; AQP-CHIP; CHIP28; AQP-1
uniprot entry name :
AQP1_HUMAN
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
220-269, Partial
sequence length :
269
sequence :
GALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDAD
DINSRVEMKPK
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Transport
products description :
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.
products references :
Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons member of an ancient channel family.Preston G.M., Agre P.Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991) The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization.Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.J. Biol. Chem. 268:15772-15778(1993) Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium.Ruiz A.C., Bok D.Biochim. Biophys. Acta 1282:174-178(1996) The water channel gene in human uterus.Li X., Yu H., Koide S.S.Biochem. Mol. Biol. Int. 32:371-377(1994) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) SeattleSNPs variation discovery resourceHuman protein factory for converting the transcriptome into an in vitro-expressed proteome.Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.Nat. Methods 5:1011-1017(2008) The DNA sequence of human chromosome 7.Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.Nature 424:157-164(2003)
ncbi gi num :
297307116
ncbi acc num :
NP_001171989.1
ncbi gb acc num :
NM_001185060.1
uniprot acc num :
P29972
ncbi mol weight :
21.6kD
ncbi pathways :
Aquaporin-mediated Transport Pathway (1269944); Bile Secretion Pathway (193146); Bile Secretion Pathway (193095); Erythrocytes Take Up Carbon Dioxide And Release Oxygen Pathway (1270224); Erythrocytes Take Up Oxygen And Release Carbon Dioxide Pathway (1270225); Metabolism Pathway (1269956); O2/CO2 Exchange In Erythrocytes Pathway (1270223); Passive Transport By Aquaporins Pathway (1269945); Proximal Tubule Bicarbonate Reclamation Pathway (144182); Proximal Tubule Bicarbonate Reclamation Pathway (144027)
ncbi summary :
Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). This gene encodes an aquaporin which functions as a molecular water channel protein. It is a homotetramer with 6 bilayer spanning domains and N-glycosylation sites. The protein physically resembles channel proteins and is abundant in erythrocytes and renal tubes. The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2010]
uniprot summary :
AQP1: 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. Belongs to the MIP/aquaporin (TC 1.A.8) family. Protein type: Transporter, aquaporin family; Membrane protein, multi-pass; Transporter; Membrane protein, integral. Chromosomal Location of Human Ortholog: 7p14. Cellular Component: apical part of cell; apical plasma membrane; basal plasma membrane; basolateral plasma membrane; brush border; brush border membrane; cytoplasm; integral to plasma membrane; nerve terminal; nuclear membrane; nucleus; plasma membrane; sarcolemma. Molecular Function: ammonium transmembrane transporter activity; ephrin receptor binding; glycerol channel activity; glycerol transmembrane transporter activity; intracellular cGMP activated cation channel activity; nitric oxide transporter activity; potassium channel activity; potassium ion transmembrane transporter activity; protein binding; transmembrane transporter activity; water channel activity; water transporter activity. Biological Process: adrenocorticotropin hormone secretion; ammonium transport; bicarbonate transport; camera-type eye morphogenesis; carbon dioxide transport; cell volume homeostasis; cellular homeostasis; cellular response to stress; cerebrospinal fluid secretion; cGMP biosynthetic process; establishment and/or maintenance of actin cytoskeleton polarity; glomerular filtration; glycerol transport; hyperosmotic salinity response; lateral ventricle development; lipid digestion; multicellular organismal water homeostasis; negative regulation of apoptosis; negative regulation of caspase activity; nitric oxide transport; odontogenesis; pancreatic juice secretion; positive regulation of angiogenesis; positive regulation of fibroblast proliferation; positive regulation of saliva secretion; potassium ion transport; renal water homeostasis; renal water transport; response to drug; response to estrogen stimulus; secretory granule organization and biogenesis; sensory perception of pain; transmembrane transport; water transport; wound healing. Disease: Blood Group--colton
size1 :
0.05 mg (E-Coli)
price1 :
190 USD
size2 :
0.2 mg (E-Coli)
price2 :
460
size3 :
0.5 mg (E-Coli)
price3 :
750
size4 :
0.05 mg (Baculovirus)
price4 :
775
size5 :
0.05 mg (Mammalian-Cell)
price5 :
1000
more info or order :
company information
MyBioSource
P.O. Box 153308
San Diego, CA 92195-3308
sales@mybiosource.com
https://www.mybiosource.com
1-888-627-0165
headquarters: USA
MyBioSource, LLC was orginally founded in Vancouver by three enthusiastic scientists who are passionate about providing the world with the best reagents available. Together, they form a company with a big vision known as MyBioSource. MyBioSource is now located in San Diego, California, USA.

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