protein

Recombinant Human Reelin

MBS955157

0.05 mg (Yeast)

185 USD

Recombinant Protein

Recombinant Human Reelin

Reelin

reelin isoform a; Reelin; reelin; reelin

RELN

RELN; RELN; RL; ETL7; LIS2; PRO1598

RELN_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

26-254

3460

AAGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGN
PTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSVQASQS
IGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLS
FIWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQG
APTDVTVHPHLAEIHSDSIILRDDFDSYHQLQLNPNIWV
ECNNCETGEQCGAIMHGNAVTFCEPYGPRELITT

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.

Cell Adhesion

Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it ses to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation.

The human reelin gene isolation, sequencing, and mapping on chromosome 7.DeSilva U., D'Arcangelo G., Braden V.V., Chen J., Miao G.G., Curran T., Green E.D.Genome Res. 7:157-164(1997) 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) Human chromosome 7 DNA sequence and biology.Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.Science 300:767-772(2003) Evolutionarily conserved, alternative splicing of reelin during brain development.Lambert de Rouvroit C., Bernier B., Royaux I., de Bergeyck V., Goffinet A.M.Exp. Neurol. 156:229-238(1999) A decrease of reelin expression as a putative vulnerability factor in schizophrenia.Impagnatiello F., Guidotti A.R., Pesold C., Dwivedi Y., Caruncho H., Pisu M.G., Uzunov D.P., Smalheiser N.R., Davis J.M., Pandey G.N., Pappas G.D., Tueting P., Sharma R.P., Costa E.Proc. Natl. Acad. Sci. U.S.A. 95:15718-15723(1998) Autosomal recessive lissencephaly with cerebellar hypoplasia is associated with human RELN mutations.Hong S.E., Shugart Y.Y., Huang D.T., Shahwan S.A., Grant P.E., Hourihane J.O.B., Martin N.D.T., Walsh C.A.Nat. Genet. 26:93-96(2000) ErratumHong S.E., Shugart Y.Y., Huang D.T., Shahwan S.A., Grant P.E., Hourihane J.O.B., Martin N.D.T., Walsh C.A.Nat. Genet. 27:225-225(2001) Reelin gene alleles and haplotypes as a factor predisposing to autistic disorder.Persico A.M., D'Agruma L., Maiorano N., Totaro A., Militerni R., Bravaccio C., Wassink T.H., Schneider C., Melmed R., Trillo S., Montecchi F., Palermo M., Pascucci T., Puglisi-Allegra S., Reichelt K.-L., Conciatori M., Marino R., Quattrocchi C.C., Baldi A., Zelante L., Gasparini P., Keller F.Mol. Psychiatry 6:150-159(2001) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009)

27436938

NP_005036.2

NM_005045.3

P78509

29kD

ECM-receptor Interaction Pathway (83068); ECM-receptor Interaction Pathway (479); Focal Adhesion Pathway (198795); Focal Adhesion Pathway (83067); Focal Adhesion Pathway (478); Lissencephaly Gene (LIS1) In Neuronal Migration And Development Pathway (137984); PI3K-Akt Signaling Pathway (692234); PI3K-Akt Signaling Pathway (692979); Reelin Signaling Pathway (137980)

This gene encodes a large secreted extracellular matrix protein thought to control cell-cell interactions critical for cell positioning and neuronal migration during brain development. This protein may be involved in schizophrenia, autism, bipolar disorder, major depression and in migration defects associated with temporal lobe epilepsy. Mutations of this gene are associated with autosomal recessive lissencephaly with cerebellar hypoplasia. Two transcript variants encoding distinct isoforms have been identified for this gene. Other transcript variants have been described but their full length nature has not been determined. [provided by RefSeq, Jul 2008]

reelin: Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation. Defects in RELN are the cause of lissencephaly type 2 (LIS2); also known as lissencephaly with cerebellar hypoplasia or Norman-Roberts syndrome. LIS2 is a classic type lissencephaly associated with abnormalities of the cerebellum, hippocampus and brainstem. Individuals with LIS2 are severely ataxic, mentally retarded and suffer from epilepsy. Belongs to the reelin family. 3 isoforms of the human protein are produced by alternative splicing. Protein type: Cell adhesion; Secreted; EC 3.4.21.-; Motility/polarity/chemotaxis; Secreted, signal peptide; Protease; Cell development/differentiation. Chromosomal Location of Human Ortholog: 7q22. Cellular Component: cytoplasm; dendrite; extracellular space; proteinaceous extracellular matrix. Molecular Function: metal ion binding; protein serine/threonine/tyrosine kinase activity; serine-type peptidase activity. Biological Process: activation of CREB transcription factor; associative learning; axon guidance; brain development; cell adhesion; cellular morphogenesis during differentiation; central nervous system development; cerebral cortex tangential migration; dendrite development; glial cell differentiation; hippocampus development; layer formation in the cerebral cortex; long-term memory; neuron migration; peptidyl-tyrosine phosphorylation; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of protein kinase activity; positive regulation of small GTPase mediated signal transduction; positive regulation of synaptic transmission, glutamatergic; positive regulation of TOR signaling pathway; proteolysis; regulation of behavior; regulation of synaptic transmission; response to pain; spinal cord patterning; ventral spinal cord development. Disease: Epilepsy, Familial Temporal Lobe, 1; Epilepsy, Familial Temporal Lobe, 7; Lissencephaly 2

0.05 mg (Yeast)

185 USD

0.2 mg (Yeast)

420

0.5 mg (Yeast)

680

1 mg (Yeast)

1070