protein

Recombinant Human Low-density lipoprotein receptor-related protein 2

MBS958530

0.05 mg (E-Coli)

180 USD

Recombinant Protein

Recombinant Human Low-density lipoprotein receptor-related protein 2

Low-density lipoprotein receptor-related protein 2

Glycoprotein 330; gp330; Megalin

low-density lipoprotein receptor-related protein 2; Low-density lipoprotein receptor-related protein 2; low-density lipoprotein receptor-related protein 2; LDL receptor related protein 2; Glycoprotein 330; gp330; Megalin

LRP2

LRP2; LRP2; DBS; GP330; LRP-2; gp330

LRP2_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1186-1389; Partial.

1389

NCTASQFKCASGDKCIGVTNRCDGVFDCSDNSDEAGCPT
RPPGMCHSDEFQCQEDGICIPNFWECDGHPDCLYGSDEH
NACVPKTCPSSYFHCDNGNCIHRAWLCDRDNDCGDMSDE
KDCPTQPFRCPSWQWQCLGHNICVNLSVVCDGIFDCPNG
TDESPLCNGNSCSDFNGGCTHECVQEPFGAKCLCPLGFL
LANDSKTCE

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Immunology

Acts together with cubilin to mediate HDL endocytosis. May participate in regulation of parathyroid-hormone and para-thyroid-hormone-related protein release.

Cloning and sequencing of human gp330, a Ca(2+) -binding receptor with potential intracellular signaling properties.Hjaelm G., Murray E., Crumley G., Harazim W., Lundgren S., Onyango I., Ek B., Larsson M., Juhlin C., Hellman P., Davis H., Aekerstroem G., Rask L., Morse B.Eur. J. Biochem. 239:132-137(1996) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Chromosomal localization of human genes for the LDL receptor family member glycoprotein 330 (LRP2) and its associated protein RAP (LRPAP1) .Korenberg J.R., Argraves K.M., Chen X.N., Tran H., Strickland D.K., Argraves W.S.Genomics 22:88-93(1994) A protein involved in calcium sensing of the human parathyroid and placental cytotrophoblast cells belongs to the LDL-receptor protein superfamily.Lundgren S., Hjaelm G., Hellman P., Ek B., Juhlin C., Rastad J., Klareskog L., Aakerstroem G., Rask L.Exp. Cell Res. 212:344-350(1994) Identification of glycoprotein 330 as an endocytic receptor for apolipoprotein J/clusterin.Kounnas M.Z., Loukinova E.B., Stefansson S., Harmony J.A.K., Brewer B.H., Strickland D.K., Argraves W.S.J. Biol. Chem. 270:13070-13075(1995) Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin.Oleinikov A.V., Zhao J., Makker S.P.Biochem. J. 347:613-621(2000) Functional interaction of megalin with the megalin-binding protein (MegBP) , a novel tetratrico peptide repeat-containing adaptor molecule.Petersen H.H., Hilpert J., Militz D., Zandler V., Jacobsen C., Roebroek A.J.M., Willnow T.E.J. Cell Sci. 116:453-461(2003) The adaptor disabled-2 binds to the third psi xNPxY sequence on the cytoplasmic tail of megalin.Gallagher H., Oleinikov A.V., Fenske C., Newman D.J.Biochimie 86:179-182(2004) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) Mutations in LRP2, which encodes the multiligand receptor megalin, cause Donnai-Barrow and facio-oculo-acoustico-renal syndromes.Kantarci S., Al-Gazali L., Hill R.S., Donnai D., Black G.C.M., Bieth E., Chassaing N., Lacombe D., Devriendt K., Teebi A., Loscertales M., Robson C., Liu T., MacLaughlin D.T., Noonan K.M., Russell M.K., Walsh C.A., Donahoe P.K., Pober B.R.Nat. Genet. 39:957-959(2007) Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma.Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.Nature 469:539-542(2011)

126012573

NP_004516.2

NM_004525.2

P98164

24.2kD

Hedgehog Signaling Pathway (83063); Hedgehog Signaling Pathway (474); Metabolism Pathway (1269956); Metabolism Of Fat-soluble Vitamins Pathway (1339147); Metabolism Of Vitamins And Cofactors Pathway (1270144); Retinoid Metabolism And Transport Pathway (1269624); Signal Transduction Pathway (1269379); Signaling Events Mediated By The Hedgehog Family Pathway (137950); Thyroid Hormone Synthesis Pathway (835410); Thyroid Hormone Synthesis Pathway (839541)

The protein encoded by this gene, low density lipoprotein-related protein 2 (LRP2) or megalin, is a multi-ligand endocytic receptor that is expressed in many different tissues but primarily in absorptive epithilial tissues such as the kidney. This glycoprotein has a large amino-terminal extracellular domain, a single transmembrane domain, and a short carboxy-terminal cytoplasmic tail. The extracellular ligand-binding-domains bind diverse macromolecules including albumin, apolipoproteins B and E, and lipoprotein lipase. The LRP2 protein is critical for the reuptake of numerous ligands, including lipoproteins, sterols, vitamin-binding proteins, and hormones. This protein also has a role in cell-signaling; extracellular ligands include parathyroid horomones and the morphogen sonic hedgehog while cytosolic ligands include MAP kinase scaffold proteins and JNK interacting proteins. Recycling of this membrane receptor is regulated by phosphorylation of its cytoplasmic domain. Mutations in this gene cause Donnai-Barrow syndrome (DBS) and facio-oculoacoustico-renal syndrome (FOAR).[provided by RefSeq, Aug 2009]

LRP2: Acts together with cubilin to mediate HDL endocytosis. May participate in regulation of parathyroid- hormone and para-thyroid-hormone-related protein release. Defects in LRP2 are the cause of Donnai-Barrow syndrome (DBS); also known as faciooculoacousticorenal syndrome (FOAR syndrome). DBS is a rare autosomal recessive disorder characterized by major malformations including agenesis of the corpus callosum, congenital diaphragmatic hernia, facial dysmorphology, ocular anomalies, sensorineural hearing loss and developmental delay. The FOAR syndrome was first described as comprising facial anomalies, ocular anomalies, sensorineural hearing loss, and proteinuria. DBS and FOAR were first described as distinct disorders but the classic distinguishing features between the 2 disorders were presence of proteinuria and absence of diaphragmatic hernia and corpus callosum anomalies in FOAR. Early reports noted that the 2 disorders shared many phenotypic features and may be identical. Although there is variability in the expression of some features (e.g. agenesis of the corpus callosum and proteinuria), DBS and FOAR are now considered to represent the same entity. Belongs to the LDLR family. Protein type: Receptor, misc.; Motility/polarity/chemotaxis; Membrane protein, integral. Chromosomal Location of Human Ortholog: 2q31.1. Cellular Component: apical plasma membrane; brush border membrane; coated pit; endocytic vesicle; endoplasmic reticulum; endosome; Golgi apparatus; integral to membrane; lysosomal membrane; lysosome; plasma membrane; receptor complex. Molecular Function: calcium ion binding; protein binding; SH3 domain binding. Biological Process: cell proliferation; endocytosis; fat-soluble vitamin metabolic process; forebrain development; lipid metabolic process; phototransduction, visible light; protein amino acid glycosylation; receptor-mediated endocytosis; retinoid metabolic process; vitamin D metabolic process; vitamin metabolic process. Disease: Donnai-barrow Syndrome

0.05 mg (E-Coli)

180 USD

0.05 mg (Yeast)

260

0.2 mg (E-Coli)

490

0.2 mg (Yeast)

600

0.5 mg (E-Coli)

715