Reelin/RELN Protein, Human (P.pastoris, His)

Reelin/RELN is a secretory glycoprotein belonging to the extracellular matrix family. Reelin/RELN can bind to ApoER2/VLDLR to activate Src family kinase-mediated Dab1 phosphorylation, initiate PI3K/Akt/mTOR signaling to regulate neuronal migration and synaptic plasticity. Reelin/RELN also activates Rap1 to regulate the actin skeleton, and terminates Reelin/RELN signaling through Cul5/Rbx2/SOCS7 and ADAMTS-4/5. Reelin/RELN abnormalities are closely related to diseases such as lissencephaly caused by RELN mutations, autism, schizophrenia, and Alzheimer's disease. Reelin/RELN Protein, Human (P. pastoris, His) is a recombinant human Reelin/RELN protein expressed from P. pastoris with an N-6*His tag.

Reelin/RELN is a large secreted glycoprotein belonging to the extracellular matrix protein family. Reelin/RELN binds to the receptors ApoER2 and VLDLR, induces Dab1 tyrosine phosphorylation through Src family kinases (Fyn/Src), activates downstream PI3K/Akt/mTor signaling, and regulates neuronal migration, dendrite growth, and synaptic plasticity. Reelin/RELN also enhances NMDA receptor-mediated calcium influx by regulating receptor clustering and subunit composition^[1][2].
Reelin/RELN activates Rap1 to regulate actin cytoskeleton reorganization (via N-cofilin phosphorylation) and neuronal polarity, and promotes epithelial-mesenchymal transition by downregulating E-cadherin. Reelin/RELN signaling is terminated by Dab1 ubiquitination (Cul5/Rbx2/SOCS7 complex) and Reelin proteolysis (ADAMTS-4/5, tPA), or impaired by ApoE4 through receptor recycling defects. Upstream regulators of Reelin/RELN include viral promoters; downstream targets include Dab1, PI3K, GSK-3β, and NMDA/AMPAR subunits^[1][2].
Reelin/RELN mutations may cause lissencephaly and are associated with autism (marked by reduced brain/blood Reelin levels) and schizophrenia (marked by promoter hypermethylation). Heterozygous reeler mice can mimic sensorimotor deficits1,5. Reelin/RELN deficiency accelerates Aβ plaque formation in Alzheimer's disease (AD), while Reelin/RELN replenishment rescues synaptic plasticity^[1][2].

Human

P. pastoris

N-6*His

P78509 (A26-T254)

5649  [NCBI]

Partial

AAGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSVQASQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFIWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTDVTVHPHLAEIHSDSIILRDDFDSYHQLQLNPNIWVECNNCETGEQCGAIMHGNAVTFCEPYGPRELITT

26-30 kDa

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 0.5 M NaCl, 3% trehalose, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
2.Lyophilized from a 0.22 μm filtered solution of PBS, 6% trehalose, pH 7.4.
Please refer to the lot-specific COA for specific buffer information.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Fatemi SH. Reelin glycoprotein: structure, biology and roles in health and disease. Mol Psychiatry. 2005 Mar;10(3):251-7.  [Content Brief]

  [2]. Jossin Y. Reelin Functions, Mechanisms of Action and Signaling Pathways During Brain Development and Maturation. Biomolecules. 2020 Jun 26;10(6):964.  [Content Brief]