NXPH1 Human, Sf9
Description
Production and Purification in Sf9 Cells
The Sf9-baculovirus system is favored for producing eukaryotic proteins requiring post-translational modifications . For NXPH1 Human, Sf9:
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Expression: Codon-optimized gene constructs are transfected into Sf9 cells, yielding soluble protein in culture supernatants .
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Purification: Achieved via immobilized metal affinity chromatography (IMAC) targeting the His-Tag, followed by size-exclusion chromatography .
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Formulation: 0.5 mg/mL in phosphate-buffered saline (pH 7.4) with 10% glycerol; carrier-free or with BSA for stability .
| Parameter | Specification |
|---|---|
| Purity | >90% (SDS-PAGE) |
| Storage | -20°C; avoid freeze-thaw cycles |
| Reconstitution | Sterile PBS at 100 μg/mL |
Functional and Mechanistic Insights
NXPH1 regulates synaptic adhesion by forming tight complexes with α-neurexins (K<sub>D</sub> ~nM range), competing with dystroglycan (DAG1) for binding . Key findings include:
Biological Roles
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Neuronal Signaling: Stabilizes inhibitory synapses in the cerebral cortex and cerebellum .
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Hematopoietic Inhibition: Suppresses proliferation of hematopoietic progenitor cells (HPCs) via NRXN1α binding, reversible by DAG1 .
Research Applications
NXPH1 Human, Sf9 is used in:
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Neuroscience Studies: Investigating synapse formation/plasticity .
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Hematopoiesis Models: Analyzing NRXN1α-DAG1 signaling in hematopoietic stem cells .
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Therapeutic Development: Targeting NXPH1-NRXN pathways in neurological disorders .
Comparative Analysis Across Species
NXPH1’s sequence conservation underpins its functional relevance:
| Species | Amino Acid Length | Molecular Weight (Da) | Sequence Identity vs. Human |
|---|---|---|---|
| Human | 271 | 31,082 | 100% |
| Mouse | 271 | 31,048 | 99% |
| Rat | 271 | 31,017 | 99% |
Data derived from recombinant protein analyses .
Key Considerations for Experimental Use
Product Specs
NXPH1, Nbla00697, NPH1 , Neurexophilin-1, Neurexophilin 1.
Sf9, Baculovirus cells.
ADPANLTNGG KSELLKSGSS KSTLKHIWTE SSKDLSISRL LSQTFRGKEN DTDLDLRYDT PEPYSEQDLW DWLRNSTDLQ EPRPRAKRRP IVKTGKFKKM FGWGDFHSNI KTVKLNLLIT GKIVDHGNGT FSVYFRHNST GQGNVSVSLV PPTKIVEFDL AQQTVIDAKD SKSFNCRIEY EKVDKATKNT LCNYDPSKTC YQEQTQSHVS WLCSKPFKVI CIYISFYSTD YKLVQKVCPD YNYHSDTPYF PSGHHHHHH.
Product Science Overview
When expressed in neuron-like cells, Neurexophilin 1 undergoes N-glycosylation and is processed to a smaller mature form through endoproteolytic cleavage . This processing is crucial for its function and interaction with neurexins. Notably, only recombinant neurexin Iα and IIIα, but not neurexin Iβ, interact with Neurexophilin 1 .
Neurexophilin 1 functions as a neuropeptide, signaling via α-neurexins. This interaction is essential for synaptic function and neuronal communication . Additionally, Neurexophilin 1 has been shown to suppress the proliferation of hematopoietic progenitor cells, indicating its role beyond the nervous system . This suppression occurs through its interaction with Neurexin Iα (NRXN1α) and is modulated by Dystroglycan (DAG1) .
The recombinant form of Neurexophilin 1, produced in Sf9 cells, is used for research purposes to study its structure, function, and interactions. Sf9 cells, derived from the fall armyworm (Spodoptera frugiperda), are commonly used in recombinant protein production due to their high expression levels and post-translational modification capabilities.
