Recombinant Human MIP-1α (CCL3) 0 ComentariosSubmit a Review Detalles del Producto Nùmero de Catalogo 300-08 Descripcion Both MIP-1α and MIP-1β are structurally and functionally related CC chemokines. They participate in host response to invading bacterial, viral, parasite and fungal pathogens by regulating the trafficking and activation state of selected subgroups of inflammatory cells (e.g. macrophages, lymphocytes and NK cells). While both MIP-1α and MIP-1β exert similar effects on monocytes, their effect on lymphocytes differ; with MIP-1α selectively attracting CD8+ lymphocytes, and MIP-1β selectively attracting CD4+ lymphocytes. Additionally, MIP-1α and MIP-1β have also been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. Both human and murine MIP-1α and MIP-1β are active on human and murine hematopoietic cells. Recombinant Human MIP-1α is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines. Source: E.coli Synonyms: Macrophage Inflammatory Protein-1α, CCL3, LD78α AA Sequence: ASLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPGV IFLTKRSRQV CADPSEEWVQ KYVSDLELSA Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses. Biological Activity: Determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml. Calculated Molecular Weight: 7.8 kDa Accession Number: P10147 Gene ID: 6348 Endotoxin: Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug) crossreactivity: Bacteria, Cow, Frog, Hamster, Human, Human + Mouse, Human + Rat, Monkey, Mouse, Rat References PubMed SDS Búsqueda del CoA Product Line Country Of Origin: USA Not for human use. Research Interest AIDS/HIV Angiogenesis/Cardiovascular Chemotaxis Immune System Inflammation Neurobiology Wound Healing Transplantation product.subtitle.recentcitations Primer autor Du, Y Titulo Chemokines form nanoparticles with DNA and can superinduce TLR-driven immune inflammation. Citar The Journal of Experimental Medicine; 219(7) PudMed id 35640018 Primer autor Lee, A W Titulo A knottin scaffold directs the CXC-chemokine-binding specificity of tick evasins. Citar The Journal of Biological Chemistry; 294(29) pg11199-11212 PudMed id 31167786 Primer autor Chan, L C Titulo IL-6/JAK1 pathway drives PD-L1 Y112 phosphorylation to promote cancer immune evasion. Citar The Journal of Clinical Investigation; 129(8) pg3324-3338 PudMed id 31305264