Reelin Recombinant Protein | RELN recombinant protein

Recombinant Human Reelin

Cat. Num. AAA955157

• Gene Names: RELN; RL; ETL7; LIS2; PRO1598
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Reelin; Recombinant Human Reelin; RELN recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 26-254aa; Partial
• Sequence: AAGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSVQASQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFIWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTDVTVHPHLAEIHSDSIILRDDFDSYHQLQLNPNIWVECNNCETGEQCGAIMHGNAVTFCEPYGPRELITT
• Sequence Length: 254

• 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 [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for RELN recombinant protein

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.

Product Categories/Family for RELN recombinant protein

Cell adhesion

References

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)

NCBI and Uniprot Product Information

• NCBI GI #: 27436938
• NCBI GeneID: 5649
• NCBI Accession #: NP_005036.2
• NCBI GenBank Nucleotide #: NM_005045.3
• UniProt Accession #: P78509; Q86UJ0; Q86UJ8; Q8NDV0; Q9UDQ2; A4D0P9; A4D0Q0
• Molecular Weight: 26.9 kDa
• NCBI Official Full Name: reelin isoform a
• NCBI Official Synonym Full Names: reelin
• NCBI Official Symbol: RELN
• NCBI Official Synonym Symbols: RL; ETL7; LIS2; PRO1598
• NCBI Protein Information: reelin
• UniProt Protein Name: Reelin
• Protein Family: Reelin
• UniProt Gene Name: RELN
• UniProt Entry Name: RELN_HUMAN

NCBI Description

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]

Uniprot Description

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