Recombinant Human Reelin (RELN) Protein (His)

Name: Recombinant Human Reelin (RELN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03380P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Reelin (RELN) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P78509
Target Symbol	RELN
Synonyms	LIS2; PRO1598; Reeler; Reelin; RELN; RELN_HUMAN; RL
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	AAGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSVQASQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFIWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTDVTVHPHLAEIHSDSIILRDDFDSYHQLQLNPNIWVECNNCETGEQCGAIMHGNAVTFCEPYGPRELITT
Expression Range	26-254aa
Protein Length	Partial
Mol. Weight	28.9kDa
Research Area	Cell Adhesion
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target Function	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.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Protein Families	Reelin family
Database References	HGNC: 9957 OMIM: 257320 KEGG: hsa:5649 STRING: 9606.ENSP00000392423 UniGene: PMID: 29753726 A two-hit loss involving VHL predicted for clear-cell renal cell carcinoma(ccRCC ) and a better prognosis, whereas mutations in PTEN, TP53, or RELN predicted for Sarcomatoid clear-cell renal cell carcinoma and worse prognosis. PMID: 28710314 we determined that Reelin protein and mRNA levels increased in CJD human samples and in mouse models of human prion disease in contrast to murine models of prion infection. However, changes in Reelin expression appeared only at late terminal stages of the disease, which prevent their use as an efficient diagnostic biomarker. PMID: 27726110 In primary-culture fetal astrocytes, streptozotocin down-regulated the expression of Reelin 410 and 180 kDa , while alpha-boswellic acid upregulated it. Interruption in astroglial Reelin/Akt/Tau signaling pathways may have a role in Alzheimer disease. PMID: 27567921 In frontal cortex extracts, an increase in Reelin mRNA, and in soluble and insoluble (guanidine-extractable) Reelin protein, was associated with late Braak stages of Alzheimer's disease (AD), while expression of its receptor, ApoER2, did not change. PMID: 27531658 This study detected significant reductions in the mRNAs associated with RELN and GAD1 in the frontal cortex (FC) of autism spectrum disorder. PMID: 28229923 There results suggest that reelin played essential roles in the development of lymphoma and might be a potential drug target in lymphoma PMID: 28498462 This review addresses recent advances in the field of nonneuronal reelin signaling. PMID: 27739126 methylation status of the promoter proximal cytosine-phospho-guanine dinucleotides determines the expression of RELN in myeloma cells. PMID: 27245998 Meta-analyses of 12 RELN gene single nucleotide polymorphisms (SNPs) and related neuropsychiatric disorders (schizophrenia, autistic spectrum disorders, attention-deficit hyperactivity disorder, Alzheimer's disease and bipolar disorders) with subgroup analyses based on ethnicity. Findings suggest a role of RELN SNPs in psychiatric diseases. PMID: 28506622 review of role in Alzheimer's disease PMID: 27031488 Significant association between rs17458357 , rs2572683,rs12555895 within the RELN gene and accelerated decline in Cognition performance in Chinese elderly male Gout population. PMID: 28953682 This study demonstrated that RELN DNA methylation might contribute to the pathogenesis of schizophrenia. PMID: 28086126 The present investigation, performed on a study sample from a population with one of the highest suicide rates in the world, indicated an association between rs2965087 in the reelin gene and the expression of suicidal threats a month before suicide in contrast to other symptoms of depression. PMID: 27537376 Reelin is was low in primary breast cancer tissue, but higher in Her2(+) breast cancers (but not triple-negative ones) metastasizing to the brain, especially in the tumor periphery adjacent to surrounding astrocytes. In the neural niche, astrocytes epigenetically regulate Reelin expression and its interaction with Her2 leading to increased proliferation and survival fitness. PMID: 28210910 Heterozygous RELN mutations cause a typical Autosomal Dominant Lateral Temporal Lobe Epilepsy syndrome, indistinguishable from that associated with LGI1 mutations. PMID: 28142128 We screened for mutations in RELN or VLDLR and compared the phenotype of these patients with that of previously reported patients. differences in clinical severity, involvement of the cerebellar hemispheres, together with the severity of the neocortical defect, enables RELN-mutated patients to be distinguished from VLDLR-mutated patients. PMID: 27000652 Reelin signaling is a critical player in the modulation of synaptic function. PMID: 27994051 Reelin was expressed by human hepatic stellate cells/myofibroblasts and the number of these cells increased significantly in the lobule as the liver fibrosis progressed, suggesting a role for Reelin in the activation of hepatic stellate cells/myofibroblasts during liver injury. PMID: 28348420 The presence of reelin was elevated in junctional areas as in dysplastic nevi. VLDLR presented positive values in 16 cases (16/ 32) and ApoER2 was weak positive in 7 cases. PMID: 28255385 common variants of GABRG2, RELN and NRG3 and the GABRG2-RELN-PTCH1 interaction networks might confer altered susceptibility to Hirschsprung disease. PMID: 27889765 RELN is mapped at 7q22, which had been identified as a candidate region for autism by early genetic linkage study. PMID: 26285919 reelin promotes multiple myeloma cell adhesion, survival, and drug resistance via activation of integrin alpha5beta1. PMID: 26848618 These findings suggest that circulating Reelin promotes atherosclerosis by increasing vascular inflammation, and that reducing or inhibiting circulating Reelin may present a novel approach for the prevention of cardiovascular disease. PMID: 26980442 Reelin thus plays a role in restraining RAS and PI3-kinase promotion of cell motility and potentially tumour metastasis. PMID: 27071537 Among men, but not in women certain genotypes of the RELN gene were significantly associated with the susceptibility to Alzheimer's disease. PMID: 26384575 Report demonstrated that the reelin subregion R5-6 consisting of 747 amino acids in the 5th and 6th repeats was sufficient for apoER2 and VLDLR binding, and inhibiting lipoprotein-induced cholesterol accumulation in macrophages. PMID: 26317415 The features of reelin expression in the brain of fetuses and newborns at 22-40 weeks' gestation with internal HC should be considered as morphological differential and diagnostic criteria for the disease in relation to its etiology. PMID: 26978229 Study shows that early neural cells transiently express Reelin at the time they leave the presumptive olfactory/vomeronasal epithelium and that Dab 1 is present in the migratory cell mass and in the presumptive ensheathing cells in the absence of reelin. PMID: 26270645 the reelin protein blood concentration might be a relevant signal with respect to the pathophysiology of schizophrenia. PMID: 26305216 These findings suggest a central AKT-FOXG1-reelin signaling pathway in focal malformations of cortical development and support pathway inhibitors as potential treatments or therapies for some forms of focal epilepsy. PMID: 26523971 rs7341475 (A/G) and rs262355 (A/T) polymorphisms in RELN gene are inversely associated with SZ risk. PMID: 26455866 RELN SNPs were associated with Alzheimer disease and mild cognitive impairment. GG genotype at rs2299356 was associated with risk of AD. RELN-rs528528 CT genotype was protective for MCI. PMID: 24384746 pThis study roposed that RELN mutations contribute to the genetic heterogeneity of myoclonus-dystonia. PMID: 25648840 Heterozygous reelin mutations cause autosomal-dominant lateral temporal epilepsy. PMID: 26046367 serum reelin may be considered an additional useful parameter for monitoring the progression of hepatic fibrosis in HCV-infected patients specially in those with active rheumatological conditions which result in an increase in serum hyaluronic acid PMID: 24803609 RELN expression in the cerebral cortex of subjects with autism is not a consequence of decreased numbers of RELN-expressing neurons PMID: 25067827 RELN gene polymorphism rs7341475 C>T is associated with the risk of paranoid schizophrenia in Russians and Tatars. PMID: 25842846 The results of this study demonstrated the presence of reelin, its receptors VLDLR and ApoER2 as well as Dab1 in the ENS and might indicate a novel role of the reelin system in regulating neuronal plasticity and pre-synaptic functions in the ENS. PMID: 24844606 Results indicate that aging- and disease-associated changes in Reelin levels and proteolytic processing might play a role in the formation of corpora amylacea by altering cytoskeletal dynamics PMID: 24252415 The g.504742G>A polymorphic variant in the RELN gene might affect subjects susceptibility toward autism in Chinese Han population. PMID: 23287318 Lack of association for RELN is that RELN could be associated with a specific otosclerosis-like phenotype that is different from the histologically confirmed phenotype of the patients in this study. PMID: 24643032 In this population, the pathogenic link between the rs39335 variant and otosclerosis was excluded. PMID: 24227897 Data indicate taht reelin interacts with amyloid beta-protein(1-42) and is sequestered by fibrils. PMID: 24599114 the RELN rs362691, rather than rs736707 or GGC repeat variant, might contribute significantly to Autism spectrum disorder risk PMID: 24453138 Data suggest that PS1/gamma-secretase-dependent processing of the reelin receptor ApoER2 inhibits reelin expression and may regulate its signaling. PMID: 24344333 reelin expression is altered by Abeta leading to impaired reelin signaling. PMID: 23951306 In this review, the signaling protein Reelin, expressed along olfactory and limbic pathways is involved in the early stages of Alzheimer's disease. PMID: 23632168 Data indicate that Reelin is up-regulated during erythroid differentiation of erythroleukemic K562 cells. PMID: 24239537 moderate risk of bias show a statistically significant association with the ACE gene, AGT gene, OTSC2, RELN gene, TGFB1 gene, 11q13.1, OTSC2, OTSC5, OTSC8, and OTSC10. [Review] PMID: 24170657

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.