Animal-Free CCL2 Protein, Pig (His)

CCL2 Protein serves as a ligand for CCR2, inducing chemotactic responses and calcium mobilization. It attracts monocytes and basophils but not neutrophils or eosinophils. Crucial in neuropathic pain and impacting NMDA-mediated synaptic transmission in dopamine neurons, CCL2 potentially engages in MAPK/ERK-dependent GRIN2B phosphorylation. Existing as a monomer or homodimer, it attaches to endothelial cells through glycosaminoglycan side chains and interacts with TNFAIP6 via its Link domain. Animal-Free CCL2 Protein, Pig (His) is the recombinant pig-derived animal-FreeCCL2 protein, expressed by E. coli, with N-His labeled tag. The total length of Animal-Free CCL2 Protein, Pig (His) is 76 a.a., with molecular weight of ~9.42 kDa.

CCL2 protein functions as a ligand for C-C chemokine receptor CCR2, initiating a potent chemotactic response and intracellular calcium mobilization through the binding and activation of CCR2. It exhibits chemotactic activity for monocytes and basophils while remaining inactive towards neutrophils or eosinophils. Playing a crucial role in mediating neuropathic pain induced by peripheral nerve injury, CCL2 also enhances NMDA-mediated synaptic transmission in dopamine D1 and D2 receptor-containing neurons, possibly involving MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B. Existing as a monomer or homodimer in equilibrium, it is tethered to endothelial cells by glycosaminoglycan (GAG) side chains of proteoglycans and interacts with TNFAIP6 through its Link domain.

Pig

E. coli

N-His

P42831 (Q24-P99)

397422  [NCBI]

QPDAINSPVTCCYTLTSKKISMQRLMSYRRVTSSKCPKEAVIFKTIAGKEICAEPKQKWVQDSISHLDKKNQTPKP

Approximately 9.42 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<0.1 EU per 1 μg of the protein by the LAL method.