Recombinant Rat Reelin (Reln), partial

Product Details

Purity
>85% (SDS-PAGE)
Target Names
Reln
Uniprot NO.
Species
Rattus norvegicus (Rat)
Source
Yeast
Expression Region
28-3462
Target Protein Sequence
ATG YYPRFSPFFF LCTHHGELEG DGEQGEVLIS LHIAGNPTYY VPGQEYHVTI STSTFFDGLL VTGLYTSTSI QSSQSIGGSS AFGFGIMSDH QFGNQFMCSV VASHVSHLPT TNLSFVWIAP PAGTGCVNFM ATATHRGQVI FKDALAQQLC EQGAPTEATA YSHLAEIHSD SVILRDDFDS YHQLELNPNI WAECSNCDTG EQCGTIMHGN AVTFCEPYGP RELTTTYLNT TTASVLQFSI GSGSCRFSYS DPSIIVSYAK NNTADWIQLE KIRAPSNVST IIHILYLPED AKGENVQFQW KQDSLHVGEV YEACWALDNI LVINSAHRQV ILEDSLDPVD TGNWLFFPGA TVKHSCQSDG NAIYFHGNEG SQLNFATTRD VDLSTEDIQE QWSEEFESQP TGWDILGAVV GSECGTIESG LSLVFLKDGE RKLCTPYMDT TGYGNLRFYF AMGGTCDPGD SHENDVILYA KIEGKKEHIA LDTLSYSSYK VPTLVSVVIN PELQTPATKF CLRQKNHQGH NQNVWAVDFF HVLPILPSTM SHMIQFSINL GCGTHQPGNS VSLEFSTNHG RSWSLLHTEC LPEICAGPHL PHSTIYSSEN YSGWNRVTIP LPNAALTRDT RIRWRQTGPI LGNMWAIDNV YIGPSCLKFC SGRGQCTRHG CKCDPGFSGP ACEMASQTFP MFISESFGSS RLSSYHNFYS IRGAEVSFGC GVLASGKALV FNKDGRRQLI TSFLDSSQSR FLQFTLRLGS KSVLSTCRAP DQPGEGVLLH YSYDNGITWK LLEHYSYLNY HEPRIISVEL PDDAKQFGIQ FRWWQPYHSS QGEDVWAIDE ILMTSVLFNS ISLDFTNLVE VTQSLGFYLG NIQPYCGHDW TLCFTGDSKL ASSMRYVETQ SMQIGASYMI QFSLVMGCGQ KYTPHMDNQV KLEYSTNHGL TWHLVQDECL PSMPSCQEFT SASIYHASEF TQWRRVTVIL PQKTWSGATR FRWSQSYYTA QDEWALDDIY IGQQCPNMCS GHGSCDHGVC RCDQGYQGTE CHPEAALPST IMSDFENPSS WDSDWQEVIG GEVVKPEQGC GVVSSGSSLY FSKAGKRQLV SWDLDTSWVD FVQFYIQIGG ESAACNKPDS REEGVLLQYS NNGGIQWHLL AEMYFSDFGK PRFVYLELPA AAKTPCTRFR WWQPVFSGED YDQWAVDDII ILSEKQKQVI PVVNPTLPQN FYEKPAFDYP INQMSVWLML ANEGMAKNDS FCATTPSAMV FGKSDGDRFA VTRDLTLKPG YVLQFKLNIG CASQFSSTAP VLLQYSHDAG MSWFLVKEGC FPASAGKGCE GNSRELSEPT VYYTGDFEEW TRVTIAIPRS LASSKTRFRW IQESSSQKNV PPFGLDGVYI SEPCPSYCSG HGDCISGVCF CDLGYTAAQG TCVSNIPNHS EMFDRFEGKL SPLWYKISGG QVGTGCGTLS DGRSLYFNGL GKREARTVPL DTRNIRLVQF YIQIGSKTSG ITCIKPRARN EGLVVQYSND NGILWHLLRE LDFLSFLEPQ IISIDLPREA KTPATAFRWW QPQHGKHSAQ WALDDVLIGV NDSSQTGFQD KFDGSIDLQA NWYRIQGGQV DIDCLSMDTA LIFTENIGKP RYAETWDFHV SASSFLQFDM SMGCSKPFSA THSVQLQYSL NNGKDWHPVT EECVPPTIGC VHYTESSTYT SERFQNWRRV TVYLPLATNS PRTRFRWIQA NYTMGADAWA IDNVLLASGC PWLCSGRGIC DSGRCVCDRG FGGPFCVPVV PLPSILKDDF NGNLHPDLWP EVYGAERGNL NGETIKSGTS LIFKGEGLRM LISRDLDCTN TMYVQFSLRF IAKGTPERSH SILLQSSING GVTWRLMDEF YFPQTTSILF INVPLPYSAQ TNATRFRLWQ PYNNGKKEEI WIIDDFIIDG DNLNNPVMLL DTFDFGPRED NWFFYPGGNI GLYCPYSSKG APEEDSAMVF VSNEIGEHSI TTRDLSVNEN TIIQFEINVG CSTDSSSADP VRLEFSRDFG ATWHLLLPLC YHSSSLVSSL CSTEHHPSST YYAGTTQGWR REVVHFGKLH LCGSVRFRWY QGFYPAGSQP VTWAIDNVYI GPQCEEMCCG HGSCVNGTKC ICDPGYSGPT CKISTKNPDF LKDDFEGQLE SDRFLLMSGG KPSRKCGILS SGNNLFFNED GLRMLVTRDL DLSHARFVQF FMRLGCGKGV PDPRSQPVLL QYSLNGGLSW SLLQEFLFSN SSNVGRYIAL EMPLKARSGS TRLRWWQPSE NGHFYSPWVI DQILIGGNIS GNTVLEDDFS TLDSRKWLLH PGGTKMPVCG STGDALVFIE KASTRYVVTT DIAVNEDSFL QIDFAASCSV TDSCYAIELE YSVDLGLSWH PLVRDCLPTN VECSRYHLQR ILVSDTFNKW TRITLPLPAY TRSQATRFRW HQPAPFDKQQ TWAIDNVYIG DGCLDMCSGH GRCIQGSCVC DEQWGGLYCD EPETSLPTQL KDNFNRAPSN QNWLTVNGGK LSTVCGAVAS GLALHFSGGC SRLLVTVDLN LTNAEFIQFY FMYGCLITPS NRNQGVLLEY SVNGGITWTL LMEIFYDQYS KPGFVNILLP PDAKEIGTRF RWWQPRHDGL DQNDWAIDNV LISGSADQRT VMLDTFSSAP VPQHERSPAD AGPVGRIAFD MFMEDKTSVN ENWVFHDDCT VERFCDSPDG VMLCGSHDGR EVYAVTHDLT PTENWIMQFK ISVGCKVPEK IAQNQIHVQF STDFGVSWSY LVPQCLPADP KCSGTVSQPS VFFPTKGWKR ITYPLPESLM GNPVRFRFYQ KYSDVQWAID NFYLGPGCLD NCGGHGDCLK EQCICDPGYS GPHCYLTHTL KTFLKERFDS EEIKPDLWMS LEGGSTCTEC GILAENTALY FGGSTVRQAI TQDLDLRGAK FLQYWGRIGS ENNMTSCHRP VCRKEGVLLD YSKDGGITWT LLHEMDFQKY ISVRHDYILL PEGALTNTTR LRWWQPFVIS NGLVVSGVER AQWALDNILI GGAEINPSQL VDTFDDEGSS HEENWSFYPN AVRTAGFCGN PSFHLYWPNK KKDKTHNALS SRELIIQPGY MMQFKIVVGC EATSCGDLHS VMLEYTKDAR SDSWQLVQTQ CLPSSSNSIG CSPFQFHEAT IYNAVNSSSW KRITIQLPDH VSSSATQFRW IQKGEETEKQ SWAIDHVYIG EACPRLCSGH GYCTTGAVCI CDESFQGDDC SVFSHELPSY IKDNFESARV TEANWETIQG GAIGSGCGQL APYAHGDSLY FNGCQIRQAA TKPLDLTRAS KIMFVLQIGS TAQTDSCNSD LSGPHTVDKA VLLQYSVNNG ITWHVIAQHQ PKDFTQAQRV SYNVPLEARM KGVLLRWWQP RHNGTGHDQW ALDHVEVVLV STRKQNYMMN FSRQHGLRHF YNRRRRSLRR YP
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
Partial
Tag Info
N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage
Store at -20°C, for extended storage, conserve at -20°C or -80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

 Customer Reviews

Target Background

Function(From Uniprot)
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.
Gene References into Functions
  1. Study found that reelin levels in the visual layers of the superior colliculus are the highest between the second and third postnatal weeks. Blocking reelin signaling with a neutralizing antibody (CR-50) from PND 7 to PND 14 induced a non-specific sprouting of ipsilateral retinocollicular axons outside their typical distribution of discrete patches of axon terminals. PMID:28602919
  2. Melatonin ameliorated the neurotoxiciy and astrocyte activation induced by Abeta1-42 in the cerebral cortex. Melatonin also blocked the reduction in Reelin and Dab1 expression induced by Abeta1-42. Using in vitro study, Reelin inactivation completely abolished the protective effect of melatonin against Abeta1-42-induced neurotoxicity. PMID:28385118
  3. These results indicate that reelin/ApoER2/PSD95 signaling is important for neuronal structure maintenance in mature neurons. PMID:27653801
  4. Golgi complex fragmentation and Reelin dysfunction are key contributors to neuronal cell death in the early stage of epilepsy pathophysiology. PMID:25790952
  5. we analyzed the effect of relin on the process morphology of primary rat astrocytes PMID:27168410
  6. Prenatal stress down-regulates Reelin expression by methylation of its promoter and induces adult behavioral impairments in rats PMID:25679528
  7. Study shows presence of reelin immunolabeling in brain endothelial cells, and particularly in caveolar vesicles within these cells, suggests that reelin and/or reelin peptides may be able to cross the blood-brain barrier PMID:25887698
  8. This study present a multimodal dataset on Reln-positive patch-clamped neurons in layers I-IV of rat somatosensory (barrel) cortex. PMID:23803971
  9. The results suggest that reelin promotes microtubule assembly, at least in part, by increasing microtubule plus end dynamics. PMID:22990595
  10. distribution of the cell-specific markers, calretinin and calbindin, in reelin-immunoreactive cells during postnatal rat and mouse neocortical development PMID:24134921
  11. we show that Reelin acts presynaptically, resulting in robust rapid enhancement of spontaneous neurotransmitter release PMID:24210904
  12. Data suggest that down-regulation of reelin expression in immature dentate granule cells/neurons plays role in the pathogenesis of major depression (in a rat model based on repeated exposure to the stress hormone corticosterone). PMID:23608736
  13. Hippocampal cytoarchitectural alterations and reelin deficiency may be involved in the development of remote cognitive impairments in this model PMID:23478644
  14. Data indicate that increased TIMP-1 levels inhibit the proteolytic processing of Reelin under epileptic conditions. PMID:23493620
  15. Reelin has important implications for the maternal-neonate interaction needed for normal brain development. PMID:23385810
  16. Reelin expressions in iodine-deficient & PTU-treated rats were significantly decreased on PND14 and 21. PMID:22595232
  17. These findings suggest that epigenetic regulation of DNA demethylation and histone acetylation of target genes, such as reelin, might underlie the mechanisms of synaptic plasticity and memory retention in the medial prefrontal cortex. PMID:22469747
  18. Reelin is expressed in distinct populations of pre-Botzinger complex neurons and inspiratory bulbospinal ventral respiratory group neurons. PMID:21858819
  19. Medial prefrontal cortex reelin signaling plays an important role in behavioral tasks with relevance to schizophrenia, for example. PMID:21784155
  20. These observations support a role for entorhinal reelin signaling in spatial learning, and suggest that an intact reelin signaling pathway is essential for synaptic integrity in the adult entorhinal cortex. PMID:21492744
  21. Maternal hypothyroidism-mediated cytoarchitecture defects including mispositioned neurons, altered morphology, and density of radial glia and loss of bipolarity of migrating neurons is attributed at least in part to reelin signaling cascade deficits. PMID:20368265
  22. secretion of Reelin is activity-independent and that proteolytic processing of Reelin is required for the maintenance of granule cell lamination in the dentate gyrus PMID:21148112
  23. This study suggested thatreduced reelin expression, emanating from layer II entorhinal neurons, may contribute to network dysfunction that occurs during memory loss in aging. PMID:20538740
  24. strong expression of estrogen receptor alpha was found in Cajal-Retzius (CR) cells, which regulate neuronal migration and synaptogenesis via the extracellular matrix protein reelin PMID:20421250
  25. Sustained increases of immature GABAergic interneurons synthesizing Reelin in the hilus could be a signature of compensatory regulation for impaired neurogenesis. PMID:20347957
  26. study found region-specific loss of reelin in the ventral dentate gyrus and its association with deficits in avoidance conditioning in adult animals that have been reared in isolation PMID:20438765
  27. investigation of reelin signalling system in intestinal mucosa; reelin protein was only observed in isolated intestinal fibroblasts & in a cell layer subjacent to the villus epithelium, which seems to be composed of myofibroblasts PMID:19946030
  28. Developmental emergence of neurobehavioural and reelin deficits in isolation reared animals is proposed to reflect maladaptive wiring within the medial prefrontal cortex during a critical maturation period of this circuitry. PMID:20035841
  29. reelin has a role in PI3-kinase signaling in neuronal growth cones, and in contributes to final neuron positioning in the mammalian brain by local modulation of protein kinase B and glycogen synthase kinase 3beta kinase activities PMID:12376533
  30. The presence of three reelin forms (full-length 420 kD, 310 kD, and 180 kD) has been demonstrated in rat cerebrospinal fluid. PMID:12645087
  31. A nucleotide insertion mutation in Reelin causes a translational frameshift and results in truncation of the Reelin protein. This removes the C-terminal region required for Reelin secretion and function. PMID:12670697
  32. Reelin signaling stimulates Dab1 binding to PI3 kinase and has a role in normal cortical lamination PMID:12882964
  33. High levels of reelin product are detected in the lateral marginal and ventral ventricular zones of spinal cord; this expression pattern is detected at all segmental spinal cord levels during embryonic development. PMID:14648677
  34. The Reelin-expressing cells in the commissure systems are GABAergic neurons. Reelin-expressing neurons in the anterior commissure had many conspicuous varicosities on their dendritic arbors and mimic to the interfascicular neurons. PMID:14757522
  35. differentiation factor for radial glial cells of dentate gyrus and as a positional cue for radial fiber orientation PMID:15459104
  36. reelin, which is expressed along the route of the migrating GnRH neurons, has an inhibitory role in guiding GnRH neurons to the basal forebrain PMID:16207762
  37. Modulates dentate granule cell(DGC) progenitor migration to maintain normal DGC integration in neonatal and adult dentate gyrus. Loss in epileptic adult hippocampus may contribute to ectopic chain migration and aberrant integration of newborn DGCs. PMID:17314278
  38. data show that Reelin is up-regulated in experimental liver cirrhosis and that its levels, thereby supporting that Reelin is involved in the pathogenesis of liver disease. PMID:18449964
  39. The present results suggest that reelin was affected by a number of different psychotropic medications commonly used to treat schizophrenia, bipolar disorder, major depression, and autism. PMID:19359144

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Subcellular Location
Secreted, extracellular space, extracellular matrix.
Protein Families
Reelin family
Tissue Specificity
Abundantly produced during brain ontogenesis by the Cajal-Retzius cells and other pioneer neurons located in the telencephalic marginal zone and by granule cells of the external granular layer of the cerebellum.
Database Links
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