MCP-1/CCL2 Protein, Cynomolgus (HEK293, His)

MCP-1/CCL2 protein activates CCR2 and induces chemotaxis and calcium ion mobilization. It attracts monocytes and basophils, not neutrophils or eosinophils. It also contributes to neuropathic pain and enhances synaptic transmission in dopamine neurons. MCP-1/CCL2 exists as a monomer or homodimer and binds to endothelial cells through proteoglycans. It interacts with TNFAIP6 via its Link domain. MCP-1/CCL2 Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived MCP-1/CCL2 protein, expressed by HEK293, with C-His labeled tag. The total length of MCP-1/CCL2 Protein, Cynomolgus (HEK293, His) is 76 a.a., with molecular weight of 13-16 kDa.

MCP-1/CCL2 protein acts as a ligand for C-C chemokine receptor CCR2, leading to the activation and binding of CCR2 and subsequently inducing a strong chemotactic response and mobilization of intracellular calcium ions. It displays chemotactic activity specifically for monocytes and basophils, but not for neutrophils or eosinophils. Additionally, MCP-1/CCL2 plays a crucial role in mediating neuropathic pain resulting from peripheral nerve injury. It enhances NMDA-mediated synaptic transmission in dopamine D1 and D2 receptor-containing neurons, potentially through MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B. MCP-1/CCL2 exists as a monomer or homodimer, with its presence on endothelial cells facilitated by glycosaminoglycan (GAG) side chains of proteoglycans. Furthermore, it interacts with TNFAIP6 through its Link domain.

Cynomolgus

HEK293

C-His

P61274 (Q24-P99)

102135739  [NCBI]

13-16 kDa

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

<1 EU/μg, determined by LAL method.