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SDF-1α is a chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. SDF-1 α activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. SDF-1α acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. SDF-1α stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase.
Histidine Tag fused to the C- terminal end of the protein
Protein Format
Soluble
Purification
Sucrose gradient
Purity
>98% by SDS-Page and Coomassie Blue staining
Buffer
Tris 50mM, pH 7.5
Target
Target Protein
CXCL12
Full Name
C-X-C motif chemokine ligand 12
Introduction
This antimicrobial gene encodes a stromal cell-derived alpha chemokine member of the intercrine family. The encoded protein functions as the ligand for the G-protein coupled receptor, chemokine (C-X-C motif) receptor 4, and plays a role in many diverse cellular functions, including embryogenesis, immune surveillance, inflammation response, tissue homeostasis, and tumor growth and metastasis. Mutations in this gene are associated with resistance to human immunodeficiency virus type 1 infections. Multiple transcript variants encoding different isoforms have been found for this gene.