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company name :
MyBioSource
product type :
protein
product name :
Recombinant Human Protein Wnt-3a
catalog :
MBS1265206
quantity :
0.05 mg (E-Coli)
price :
190 USD
more info or order :
product information
catalog number :
MBS1265206
products type :
Recombinant Protein
products full name :
Recombinant Human Protein Wnt-3a
products short name :
Wnt-3a
other names :
protein Wnt-3a; Protein Wnt-3a; protein Wnt-3a; wingless-type MMTV integration site family member 3A
products gene name :
WNT3A
other gene names :
WNT3A; WNT3A
uniprot entry name :
WNT3A_HUMAN
host :
E Coli
sequence positions :
19-351, Partial. (The full length is 19-352aa).
sequence length :
351
sequence :
SYPIWWSLAVGPQYSSLGSQPILCASIPGLVPKQLRFCR
NYVEIMPSVAEGIKIGIQECQHQFRGRRWNCTTVHDSLA
IFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGTAAI
CGCSSRHQGSPGKGWKWGGCSEDIEFGGMVSREFADARE
NRPDARSAMNRHNNEAGRQAIASHMHLKCKCHGLSGSCE
VKTCWWSQPDFRAIGDFLKDKYDSASEMVVEKHRESRGW
VETLRPRYTYFKVPTERDLVYYEASPNFCEPNPETGSFG
TRDRTCNVSSHGIDGCDLLCCGRGHNARAERRREKCRCV
FHWCCYVSCQECTRVYDVHTC
purity :
Greater than 90% as determined by SDS-PAGE.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Signal Transduction
products description :
Ligand for mbers of the frizzled family of seven transmembrane receptors. Wnt-3 and Wnt-3a play distinct roles in cell-cell signaling during morphogenesis of the developing neural tube.
products references :
Molecular cloning and characterization of WNT3a and WNT14 clustered in human chromosome 1q42 region.Saitoh T., Hirai M., Katoh M.Biochem. Biophys. Res. Commun. 284:1168-1175(2001) 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) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Differential expression of human Wnt genes 2, 3, 4, and 7B in human breast cell lines and normal and disease states of human breast tissue.Huguet E.L., McMahon J.A., McMahon A.P., Bicknell R., Harris A.L.Cancer Res. 54:2615-2621(1994) Wntless, a conserved membrane protein dedicated to the secretion of Wnt proteins from signaling cells.Baenziger C., Soldini D., Schuett C., Zipperlen P., Hausmann G., Basler K.Cell 125:509-522(2006) Reconstitution of a frizzled8.Wnt3a.LRP6 signaling complex reveals multiple Wnt and Dkk1 binding sites on LRP6.Bourhis E., Tam C., Franke Y., Bazan J.F., Ernst J., Hwang J., Costa M., Cochran A.G., Hannoush R.N.J. Biol. Chem. 285:9172-9179(2010) WLS-dependent secretion of WNT3A requires Ser209 acylation and vacuolar acidification.Coombs G.S., Yu J., Canning C.A., Veltri C.A., Covey T.M., Cheong J.K., Utomo V., Banerjee N., Zhang Z.H., Jadulco R.C., Concepcion G.P., Bugni T.S., Harper M.K., Mihalek I., Jones C.M., Ireland C.M., Virshup D.M.J. Cell Sci. 123:3357-3367(2010) APCDD1 is a novel Wnt inhibitor mutated in hereditary hypotrichosis simplex.Shimomura Y., Agalliu D., Vonica A., Luria V., Wajid M., Baumer A., Belli S., Petukhova L., Schinzel A., Brivanlou A.H., Barres B.A., Christiano A.M.Nature 464:1043-1047(2010) Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling.Doubravska L., Krausova M., Gradl D., Vojtechova M., Tumova L., Lukas J., Valenta T., Pospichalova V., Fafilek B., Plachy J., Sebesta O., Korinek V.Cell. Signal. 23:837-848(2011) Disulfide bond requirements for active wnt ligands.MacDonald B.T., Hien A., Zhang X., Iranloye O., Virshup D.M., Waterman M.L., He X.J. Biol. Chem. 289:18122-18136(2014) Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine.Gao X., Hannoush R.N.Nat. Chem. Biol. 10:61-68(2014) Notum deacylates Wnt proteins to suppress signalling activity.Kakugawa S., Langton P.F., Zebisch M., Howell S.A., Chang T.H., Liu Y., Feizi T., Bineva G., O'Reilly N., Snijders A.P., Jones E.Y., Vincent J.P.Nature 0:0-0(2015)
ncbi gi num :
14916475
ncbi acc num :
NP_149122.1
ncbi gb acc num :
NM_033131.3
uniprot acc num :
P56704
ncbi mol weight :
41.4kD
ncbi pathways :
Basal Cell Carcinoma Pathway (83113); Basal Cell Carcinoma Pathway (525); Canonical Wnt Signaling Pathway (138032); Cardiac Progenitor Differentiation Pathway (712094); Class B/2 (Secretin Family Receptors) Pathway (1269570); DNA Damage Response (only ATM Dependent) Pathway (198827); Disassembly Of The Destruction Complex And Recruitment Of AXIN To The Membrane Pathway (1269601); Disease Pathway (1268854); Diseases Of Signal Transduction Pathway (1268855); GPCR Ligand Binding Pathway (1269544)
ncbi summary :
The WNT gene family consists of structurally related genes which encode secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family. It encodes a protein which shows 96% amino acid identity to mouse Wnt3A protein, and 84% to human WNT3 protein, another WNT gene product. This gene is clustered with WNT14 gene, another family member, in chromosome 1q42 region. [provided by RefSeq, Jul 2008]
uniprot summary :
WNT3A: Ligand for members of the frizzled family of seven transmembrane receptors. Wnt-3 and Wnt-3a play distinct roles in cell-cell signaling during morphogenesis of the developing neural tube. Interacts with PORCN. Interacts with APCDD1 and WLS. Component of the Wnt-Fzd-LRP5-LRP6 signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts directly in the complex with LRP6. Moderately expressed in placenta and at low levels in adult lung, spleen, and prostate. Belongs to the Wnt family. Protein type: Secreted; Secreted, signal peptide. Chromosomal Location of Human Ortholog: 1q42. Cellular Component: cell surface; early endosome membrane; endoplasmic reticulum lumen; extracellular region; extracellular space; Golgi lumen; plasma membrane; proteinaceous extracellular matrix. Molecular Function: frizzled binding; frizzled-2 binding; protein binding; protein domain specific binding; receptor agonist activity; receptor binding; transcription coactivator activity. Biological Process: axon guidance; cell proliferation in forebrain; cell proliferation in midbrain; dorsoventral neural tube patterning; extracellular matrix organization and biogenesis; heart looping; hemopoiesis; hippocampus development; in utero embryonic development; inner ear morphogenesis; mammary gland development; negative regulation of axon extension involved in axon guidance; negative regulation of fat cell differentiation; negative regulation of neurogenesis; neuron differentiation; osteoblast differentiation; palate development; paraxial mesodermal cell fate commitment; positive regulation of B cell proliferation; positive regulation of caspase activity; positive regulation of cell proliferation; positive regulation of collateral sprouting in the absence of injury; positive regulation of cytokine production; positive regulation of mesodermal cell fate specification; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of protein binding; positive regulation of receptor internalization; positive regulation of skeletal muscle development; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; signalosome assembly; spinal cord association neuron differentiation; synaptogenesis; Wnt receptor signaling pathway in forebrain neuroblast division; Wnt receptor signaling pathway through beta-catenin
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 :
1 mg (E-Coli)
price4 :
1180
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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