JAM2 Human, Sf9
Description
Functional Roles and Mechanisms
JAM2 is integral to maintaining tight junctions in endothelial and epithelial cells, with roles in:
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Immune Cell Trafficking: Mediates lymphocyte adhesion and transmigration via interactions with leukocyte integrins (e.g., LFA-1) .
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Neurovascular Homeostasis: Highly expressed in brain endothelial cells and astrocytes; loss-of-function mutations cause primary familial brain calcification (PFBC) .
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Cell Polarity Regulation: Collaborates with claudins and occludin to stabilize tight junctions, influencing paracellular permeability .
Expression and Purification
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Host System: Sf9 cells infected with recombinant baculovirus .
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Advantages: High yield (~0.5 mg/mL), scalability, and eukaryotic post-translational modifications .
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Formulation: 50% glycerol, 1 mM DTT, PBS (pH 7.4); stabilized with carrier proteins (e.g., HSA/BSA) .
Comparison with Alternative Expression Systems
Pathological Implications
Biallelic JAM2 mutations are linked to severe neurovascular disorders:
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Primary Familial Brain Calcification (PFBC): Patients exhibit cortical and basal ganglia calcifications, parkinsonism, and dysarthria .
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Mechanistic Insights: Mutations (e.g., p.L48*, p.W168C) disrupt JAM2 plasma membrane localization, impairing cell adhesion and blood-brain barrier integrity .
Research Applications
JAM2 Human, Sf9 is utilized in:
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Immune Migration Studies: Blocking JAM2 with antibodies or soluble ligands inhibits leukocyte transendothelial migration .
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Neurovascular Disease Models: Used to study PFBC pathogenesis and screen therapeutic candidates .
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Structural Biology: Crystallization efforts to map ligand-binding domains (e.g., JAM3 interaction sites) .
Key Research Findings
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In Vivo Relevance: JAM2 knockout mice show brain calcification and neuroinflammation, mirroring human PFBC .
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Therapeutic Targeting: Soluble JAM2 fragments reduce autoimmune inflammation in preclinical models .
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Comparative Biology: JAM2’s role in tight junctions is evolutionarily conserved, with homologs in Drosophila and zebrafish .
Product Specs
Junctional Adhesion Molecule 2, Vascular Endothelial Junction-Associated Molecule, C21orf43, VE-JAM, JAM-2, JAM-B, VEJAM, Junctional Adhesion Molecule B, JAM-IT/VE-JAM, CD322 Antigen, PRO245, CD322, JAMB, Junctional adhesion molecule B.
Sf9, Baculovirus cells.
ADPFSAPKDQ QVVTAVEYQE AILACKTPKK TVSSRLEWKK LGRSVSFVYY QQTLQGDFKN RAEMIDFNIR IKNVTRSDAG KYRCEVSAPS EQGQNLEEDT VTLEVLVAPA VPSCEVPSSA LSGTVVELRC QDKEGNPAPE YTWFKDGIRL LENPRLGSQS TNSSYTMNTK TGTLQFNTVS KLDTGEYSCE ARNSVGYRRC PGKRMQVDDL NISLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
Product Science Overview
Junctional Adhesion Molecule 2 (JAM2) is a type I membrane protein that belongs to the immunoglobulin superfamily. It is primarily localized at the tight junctions of both epithelial and endothelial cells. JAM2 plays a crucial role in regulating paracellular permeability and leukocyte transmigration, making it a significant molecule in the context of cellular adhesion and immune response.
JAM2 consists of an extracellular domain with two immunoglobulin-like loops, a single-pass transmembrane region, and a short cytoplasmic tail. The extracellular domain is responsible for homophilic interactions, which are critical for its adhesive functions. JAM2 functions as an adhesive ligand, interacting with various immune cell types, and may have a role in lymphocyte homing to secondary lymphoid organs .
The recombinant form of Human JAM2 is produced in Sf9 Baculovirus cells. This recombinant protein is a single, glycosylated polypeptide chain containing 452 amino acids, with a molecular mass of approximately 50.7 kDa . The use of Sf9 cells, derived from the fall armyworm Spodoptera frugiperda, is a common practice for producing recombinant proteins due to their high efficiency in post-translational modifications.
JAM2’s localization at tight junctions and its role in leukocyte transmigration highlight its importance in maintaining the integrity of cellular barriers and facilitating immune surveillance. The homophilic binding of JAM2 is essential for its function in adhesive interactions and junctional organization. This binding is regulated by serine phosphorylation, which moderates its localization and interaction with other tight junction proteins like PAR-3 and ZO-1 .
Recombinant Human JAM2 produced in Sf9 cells is used in various research applications, including studies on cell adhesion, immune response, and tight junction dynamics. It serves as a valuable tool for investigating the molecular mechanisms underlying cellular interactions and barrier functions.
