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Cadherin-1 (CDH1) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS718414

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with thselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating… More details

$385 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Cadherin-1 (CDH1), Recombinant Protein
Full Product Name
Recombinant Human Cadherin-1
Product Gene Name
Product Synonym Names
CAM 120/80; Epithelial cadherin; E-cadherin; Uvomorulin; CD324
Sequence
DWVIPPISCP ENEKGPFPKN LVQIKSNKDK EGKVFYSITG QGADTPPVGV FIIERETGWL KVTEPLDRER IATYTLFSHA VSSNGNAVED PMEILITVTD QNDNKPEFTQ EVFKGSVMEG ALPGTSVMEV TATDADDDVN TYNAAIAYTI LSQDPELPDK NMFTINRNTG VISVVTTGLD RESFPTYTLV VQAADLQGEG LSTTATAVIT VTDTNDNPPI FNPTTYKGQV PENEANVVIT TLKVTDADAP NTPAWEAVYT ILNDDGGQFV VTTNPVNNDG ILKTAKGLDF EAKQQYILHV AVTNVVPFEV SLTTSTATVT VDVLDVNEAP IFVPPEKRVE VSEDFGVGQE ITSYTAQEPD TFMEQKITYR IWRDTANWLE INPDTGAIST RAELDREDFE HVKNSTYTAL IIATDNGSPV ATGTGTLLLI LSDVNDNAPI PEPRTIFFCE RNPKPQVINI IDADLPPNTS PFTAELTHGA SANWTIQYND PTQESIILKP KMALEVGDYK INLKLMDNQN KDQVTTLEVS VCDCEGAAGV CRKAQPVEAG LQI
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
64.4 kDa
Sequence Positions
155-707aa; Partial
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
137215
3D Structure
ModBase 3D Structure for P12830
Production Note
Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to support@mybiosource.com for more details.

Product Categories/Family for CDH1 recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for CDH1 recombinant protein

Molecular cloning and characterization of the human E-cadherin cDNA.Bussemakers M.J.G., Mees S.G.M., van Bokhoven A., Debruyne F.M.J., Schalken J.A.Mol. Biol. Rep. 17:123-128(1993) E-cadherin gene mutations in human gastric carcinoma cell lines.Oda T., Kanai Y., Oyama T., Yoshiura K., Shimoyama Y., Birchmeier W., Sugimura T., Hirohashi S.Proc. Natl. Acad. Sci. U.S.A. 91:1858-1862(1994) Molecular cloning of human E-cadherin suggests a novel subdivision of the cadherin superfamily.Rimm D.L., Morrow J.S.Biochem. Biophys. Res. Commun. 200:1754-1761(1994) Calcium influx triggers the sequential proteolysis of extracellular and cytoplasmic domains of E-cadherin, leading to loss of beta-catenin from cell-cell contacts.Ito K., Okamoto I., Araki N., Kawano Y., Nakao M., Fujiyama S., Tomita K., Mimori T., Saya H.Oncogene 18:7080-7090(1999) Mutant E-cadherin.Shibamoto S., Fukudome Y., Yanagihara K.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) NIEHS SNPs programThe sequence and analysis of duplication-rich human chromosome 16.Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.Nature 432:988-994(2004) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.Transcriptional regulation of the human E-cadherin gene in human prostate cancer cell lines characterization of the human E-cadherin gene promoter.Bussemakers M.J.G., Giroldi L.A., van Bokhoven A., Schalken J.A.Biochem. Biophys. Res. Commun. 203:1284-1290(1994) Silencing of the E-cadherin invasion-suppressor gene by CpG methylation in human carcinomas.Yoshiura K., Kanai Y., Ochiai A., Shimoyama Y., Sugimura T., Hirohashi S.Proc. Natl. Acad. Sci. U.S.A. 92:7416-7419(1995) Type I gamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct interaction with mu 1B adaptin.Ling K., Bairstow S.F., Carbonara C., Turbin D.A., Huntsman D.G., Anderson R.A.J. Cell Biol. 176:343-353(2007) Cloning and characterization of the human invasion suppressor gene E-cadherin (CDH1) .Berx G., Staes K., van Hengel J., Molemans F., Bussemakers M.J.G., van Bokhoven A., van Roy F.Genomics 26:281-289(1995) Characterization and chromosomal localization of the gene encoding the human cell adhesion molecule uvomorulin.Mansouri A., Spurr N., Goodfellow P.N., Kemler R.Differentiation 38:67-71(1988) Frixen U.H. E-cadherin gene mutations provide clues to diffuse type gastric carcinomas.Becker K.-F., Atkinson M.J., Reich U., Becker I., Nekarda H., Siewert J.R., Hoefler H.Cancer Res. 54:3845-3852(1994) A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions.Marambaud P., Shioi J., Serban G., Georgakopoulos A., Sarner S., Nagy V., Baki L., Wen P., Efthimiopoulos S., Shao Z., Wisniewski T., Robakis N.K.EMBO J. 21:1948-1956(2002) Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule.Ozawa M., Ringwald M., Kemler R.Proc. Natl. Acad. Sci. U.S.A. 87:4246-4250(1990) Distinct cadherin-catenin complexes in Ca(2+) -dependent cell-cell adhesion.Butz S., Kemler R.FEBS Lett. 355:195-200(1994) Cleavage and shedding of E-cadherin after induction of apoptosis.Steinhusen U., Weiske J., Badock V., Tauber R., Bommert K., Huber O.J. Biol. Chem. 276:4972-4980(2001) Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex.Baki L., Marambaud P., Efthimiopoulos S., Georgakopoulos A., Wen P., Cui W., Shioi J., Koo E., Ozawa M., Friedrich V.L., Robakis N.K.Proc. Natl. Acad. Sci. U.S.A. 98:2381-2386(2001) Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat.Makagiansar I.T., Nguyen P.D., Ikesue A., Kuczera K., Dentler W., Urbauer J.L., Galeva N., Alterman M., Siahaan T.J.J. Biol. Chem. 277:16002-16010(2002) Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells.Laprise P., Viel A., Rivard N.J. Biol. Chem. 279:10157-10166(2004) Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells.Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A., Baumann R., Starzinski-Powitz A.Mol. Biol. Cell 15:397-406(2004) Cadherins mediate both the association between PS1 and beta-catenin and the effects of PS1 on beta-catenin stability.Serban G., Kouchi Z., Baki L., Georgakopoulos A., Litterst C.M., Shioi J., Robakis N.K.J. Biol. Chem. 280:36007-36012(2005) Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin.Lock J.G., Stow J.L.Mol. Biol. Cell 16:1744-1755(2005) The cytoplasmic sequence of E-cadherin promotes non-amyloidogenic degradation of A beta precursors.Agiostratidou G., Muros R.M., Shioi J., Marambaud P., Robakis N.K.J. Neurochem. 96:1182-1188(2006) Induction of the LRP16 gene by estrogen promotes the invasive growth of Ishikawa human endometrial cancer cells through the downregulation of E-cadherin.Meng Y.G., Han W.-D., Zhao Y.-L., Huang K., Si Y.-L., Wu Z.-Q., Mu Y.-M.Cell Res. 17:869-880(2007) Germline E-cadherin mutations in familial lobular breast cancer.Masciari S., Larsson N., Senz J., Boyd N., Kaurah P., Kandel M.J., Harris L.N., Pinheiro H.C., Troussard A., Miron P., Tung N., Oliveira C., Collins L., Schnitt S., Garber J.E., Huntsman D.J. Med. Genet. 44:726-731(2007) Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD.Zhou F., Su J., Fu L., Yang Y., Zhang L., Wang L., Zhao H., Zhang D., Li Z., Zha X.Glycoconj. J. 25:727-740(2008) EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt.Abe K., Takeichi M.Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) Structure and biochemistry of cadherins and catenins.Shapiro L., Weis W.I.Cold Spring Harb. Perspect. Biol. 1:A3053-A3053(2009) Armus is a Rac1 effector that inactivates Rab7 and regulates E-cadherin degradation.Frasa M.A., Maximiano F.C., Smolarczyk K., Francis R.E., Betson M.E., Lozano E., Goldenring J., Seabra M.C., Rak A., Ahmadian M.R., Braga V.M.Curr. Biol. 20:198-208(2010) DDR1 regulates the stabilization of cell surface E-cadherin and E-cadherin-mediated cell aggregation.Eswaramoorthy R., Wang C.K., Chen W.C., Tang M.J., Ho M.L., Hwang C.C., Wang H.M., Wang C.Z.J. Cell. Physiol. 224:387-397(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Slit-Robo signaling induces malignant transformation through Hakai-mediated E-cadherin degradation during colorectal epithelial cell carcinogenesis.Zhou W.J., Geng Z.H., Chi S., Zhang W., Niu X.F., Lan S.J., Ma L., Yang X., Wang L.J., Ding Y.Q., Geng J.G.Cell Res. 21:609-626(2011) Acetylation-dependent regulation of Skp2 function.Inuzuka H., Gao D., Finley L.W., Yang W., Wan L., Fukushima H., Chin Y.R., Zhai B., Shaik S., Lau A.W., Wang Z., Gygi S.P., Nakayama K., Teruya-Feldstein J., Toker A., Haigis M.C., Pandolfi P.P., Wei W.Cell 150:179-193(2012) Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin.Mukherjee M., Chow S.Y., Yusoff P., Seetharaman J., Ng C., Sinniah S., Koh X.W., Asgar N.F., Li D., Yim D., Jackson R.A., Yew J., Qian J., Iyu A., Lim Y.P., Zhou X., Sze S.K., Guy G.R., Sivaraman J.EMBO J. 31:1308-1319(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin.Schubert W.-D., Urbanke C., Ziehm T., Beier V., Machner M.P., Domann E., Wehland J., Chakraborty T., Heinz D.W.Cell 111:825-836(2002) Mutations of the human E-cadherin (CDH1) gene.Berx G., Becker K.-F., Hoefler H., van Roy F.3.0.CO;2-D>Hum. Mutat. 12:226-237(1998) The crystal structure of human E-cadherin domains 1 and 2, and comparison with other cadherins in the context of adhesion mechanism.Parisini E., Higgins J.M., Liu J.H., Brenner M.B., Wang J.H.J. Mol. Biol. 373:401-411(2007) Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition.Li Y., Hofmann M., Wang Q., Teng L., Chlewicki L.K., Pircher H., Mariuzza R.A.Immunity 31:35-46(2009) Point mutation of the E-cadherin gene in invasive lobular carcinoma of the breast.Kanai Y., Oda T., Tsuda H., Ochiai A., Hirohashi S.Jpn. J. Cancer Res. 85:1035-1039(1994) Mutations of the E-cadherin gene in human gynecologic cancers.Risinger J.I., Berchuck A., Kohler M.F., Boyd J.Nat. Genet. 7:98-102(1994) E-cadherin gene mutations in signet ring cell carcinoma of the stomach.Muta H., Noguchi M., Kanai Y., Ochiai A., Nawata H., Hirohashi S.Jpn. J. Cancer Res. 87:843-848(1996) Inactivation of the E-cadherin gene in primary gastric carcinomas and gastric carcinoma cell lines.Tamura G., Sakata K., Nishizuka S., Maesawa C., Suzuki Y., Iwaya T., Terashima M., Saito K., Satodate R.Jpn. J. Cancer Res. 87:1153-1159(1996) E-cadherin gene alterations are rare events in thyroid tumors.Soares P., Berx G., van Roy F., Sobrinho-Simoes M.3.0.CO;2-7>Int. J. Cancer 70:32-38(1997) E-cadherin germline mutations in familial gastric cancer.Guilford P.J., Hopkins J.B.W., Harraway J., McLeod M., McLeod N., Harawira P., Taite H., Scoular R., Miller A., Reeve A.E.Nature 392:402-405(1998) Germline mutations of E-cadherin gene in Korean familial gastric cancer patients.Yoon K.-A., Ku J.-L., Yang H.-K., Kim W.H., Park S.Y., Park J.-G.J. Hum. Genet. 44:177-180(1999) The E-cadherin gene (CDH1) variants T340A and L599V in gastric and colorectal cancer patients in Korea.Kim H.C., Wheeler J.M.D., Kim J.C., Ilyas M., Beck N.E., Kim B.S., Park K.C., Bodmer W.F.Gut 47:262-267(2000) Association of E-cadherin germ-line alterations with prostate cancer.Ikonen T., Matikainen M., Mononen N., Hyytinen E.R., Helin H.J., Tommola S., Tammela T.L., Pukkala E., Schleutker J., Kallioniemi O.-P., Koivisto P.A.Clin. Cancer Res. 7:3465-3471(2001) A germline E-cadherin mutation in a family with gastric and colon cancer.Salahshor S., Hou H., Diep C.B., Loukola A., Zhang H., Liu T., Chen J., Iselius L., Rubio C., Lothe R.A., Aaltonen L., Sun X.F., Lindmark G., Lindblom A.Int. J. Mol. Med. 8:439-443(2001) Screening E-cadherin in gastric cancer families reveals germline mutations only in hereditary diffuse gastric cancer kindred.Oliveira C., Bordin M.C., Grehan N., Huntsman D., Suriano G., Machado J.C., Kiviluoto T., Aaltonen L., Jackson C.E., Seruca R., Caldas C.Hum. Mutat. 19:510-517(2002) E-cadherin gene variants in gastric cancer families whose probands are diagnosed with diffuse gastric cancer.Yabuta T., Shinmura K., Tani M., Yamaguchi S., Yoshimura K., Katai H., Nakajima T., Mochiki E., Tsujinaka T., Takami M., Hirose K., Yamaguchi A., Takenoshita S., Yokota J.Int. J. Cancer 101:434-441(2002) Identification of CDH1 germline missense mutations associated with functional inactivation of the E-cadherin protein in young gastric cancer probands.Suriano G., Oliveira C., Ferreira P., Machado J.C., Bordin M.C., De Wever O., Bruyneel E.A., Moguilevsky N., Grehan N., Porter T.R., Richards F.M., Hruban R.H., Roviello F., Huntsman D., Mareel M., Carneiro F., Caldas C., Seruca R.Hum. Mol. Genet. 12:575-582(2003) Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas.Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.-L.Breast Cancer Res. 9:R5-R5(2007) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of CDH1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for CDH1 purchase

MBS718414 is a recombinant protein targeting CDH1. Also known as Recombinant Human Cadherin-1. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for CDH1. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
cadherin-1 isoform 1 preproprotein
NCBI Official Synonym Full Names
cadherin 1
NCBI Official Symbol
CDH1
NCBI Official Synonym Symbols
UVO; CDHE; ECAD; LCAM; Arc-1; CD324
UniProt Protein Name
Cadherin-1
UniProt Synonym Protein Names
CAM 120/80; Epithelial cadherin; E-cadherin
UniProt Gene Name
CDH1
UniProt Synonym Gene Names
CDHE; UVO; E-cadherin
UniProt Entry Name
CADH1_HUMAN
NCBI Protein Information
cadherin-1

NCBI Summary for CDH1

This gene encodes a classical cadherin of the cadherin superfamily. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate the mature glycoprotein. This calcium-dependent cell-cell adhesion protein is comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Mutations in this gene are correlated with gastric, breast, colorectal, thyroid and ovarian cancer. Loss of function of this gene is thought to contribute to cancer progression by increasing proliferation, invasion, and/or metastasis. The ectodomain of this protein mediates bacterial adhesion to mammalian cells and the cytoplasmic domain is required for internalization. This gene is present in a gene cluster with other members of the cadherin family on chromosome 16. [provided by RefSeq, Nov 2015]
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UniProt Comments for CDH1

CDH1: a single-pass type I membrane protein, and calcium dependent cell adhesion proteins. It is a ligand for integrin alpha-E/beta-7, and it colocalizes with DLG7 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Defects in CDH1 are involved in dysfunction of the cell-cell adhesion system, triggering cancer invasion (gastric, breast, ovary, endometrium and thyroid) and metastasis. Has a potent invasive suppressor role.

Protein type: Membrane protein, integral; Motility/polarity/chemotaxis; Ubiquitin ligase; Cell adhesion

Chromosomal Location of Human Ortholog: 16q22.1

Cellular Component: actin cytoskeleton; apical junction complex; catenin complex; cell junction; cell-cell adherens junction; cortical actin cytoskeleton; cytoplasm; endosome; extracellular region; flotillin complex; focal adhesion; integral to membrane; internal side of plasma membrane; lamellipodium; lateral plasma membrane; perinuclear region of cytoplasm; plasma membrane; trans-Golgi network

Molecular Function: ankyrin binding; beta-catenin binding; calcium ion binding; cell adhesion molecule binding; gamma-catenin binding; glycoprotein binding; GTPase activating protein binding; protein binding

Biological Process: apoptosis; cell structure disassembly during apoptosis; cell-cell adhesion; extracellular matrix disassembly; extracellular matrix organization and biogenesis; homophilic cell adhesion; intercellular junction assembly and maintenance; negative regulation of cell-cell adhesion; neurite development; pituitary gland development; positive regulation of transcription factor import into nucleus; positive regulation of transcription, DNA-dependent; programmed cell death; regulation of immune response; response to drug; response to toxin; small GTPase mediated signal transduction; synaptogenesis

Disease: Breast Cancer; Endometrial Cancer; Gastric Cancer, Hereditary Diffuse; Ovarian Cancer; Prostate Cancer
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

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