Chemokine (C-C Motif) Ligand 8 (CCL8) (AA 24-99) (Active) Protein

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Proteinname
  • HC14
  • MCP-2
  • MCP2
  • SCYA10
  • SCYA8
  • 1810063B20Rik
  • AB023418
  • Mcp2
  • Scya8
  • C-C motif chemokine ligand 8
  • chemokine (C-C motif) ligand 8
  • C-C motif chemokine 8
  • monocyte chemoattractant protein-2 precursor
  • CCL8
  • Ccl8
  • LOC101119572
  • MCP-2
Proteineigenschaft
AA 24-99
13
2
2
2
1
1
1
1
Spezies
Human
31
20
2
1
1
1
1
Quelle
Escherichia coli (E. coli)
44
3
2
1
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Applikation
Flow Cytometry (FACS), Immunoprecipitation (IP)
Optionen
Hersteller
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Hersteller Produkt- Nr.
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Reinheit > 98 % , as determined by Coomassie stained SDS-PAGE.
Sterilität 0.22 μm filtered
Endotoxin-Niveau

Less than 0.01 ng per μg cytokine as determined by the LAL method.

Proteinname Chemokine (C-C Motif) Ligand 8 (CCL8)
Hintergrund CCL8, also known as MCP-2, is a beta chemokine initially isolated from human MG-63 osteosarcoma cells stimulated with IL-1β. CCL8 (MCP-2) has structural and functional similarity with MCP-1 and MCP-3, and it is often co-induced with those chemokines in mononuclear cells. IFNγ is a strong inducer of CCL8 in monocytes and fibroblasts. CCL8 can be processed and secreted as a truncated chemokine CCL8 (6-75). This isoform does not chemoattract monocytes, but it binds to the CCR2 receptor and induces its internalization, as a result, CCL8 inhibits MCP-1 (CCL2) and MCP-2 (CCL8) ERK signaling and antagonizes the chemotactic activity of several CCR2 ligands (MCP-1/CCL2, MCP-2/CCL8, MCP-3/CCL7). CCL8 is highly expressed in the skin, and it serves as an agonist for the chemokine receptor CCR8, but not for CCR2. Therefore, it has been speculated that the CCL8-CCR8 interaction is a crucial regulator of Th2 cell homing, which drives IL-5-mediated chronic allergic inflammation. In addition, CCL8 binds CCR5 receptor with high affinity and inhibits the replication of human immunodeficiency virus type 1. CCL8 is highly expressed in different human diseases, and it is a potential biomarker for the diagnosis of graft-versus-host diseases and tuberculosis.
Molekulargewicht The 76 amino acid recombinant protein has a predicted molecular mass of approximately 8.9 kDa. The DTT-reduced protein migrates at approximately 11 kDa and non-reduced protein migrates at approximately 12 kDa by SDS-PAGE. The N-terminal amino acid is Gln.
Applikations-hinweise Optimal working dilution should be determined by the investigator.
Kommentare

Biological activity: Bioactivity was measured by its property to chemoattract human THP-1 cells in a dose dependent manner.

Beschränkungen Nur für Forschungszwecke einsetzbar
Format Liquid
Rekonstitution For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored from -20 °C to -70 °C. Stock solutions can also be prepared at 50-100 μg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2-1 % BSA or HSA and stored in working aliquots at -20 °C to -70 °C.
Buffer 0.22 μm filtered protein solution is in PBS.
Handhabung Avoid repeated freeze/thaw cycles.
Lagerung -20 °C
Informationen zur Lagerung Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for six months, or at -70°C for one year.
Allgemeine Veröffentlichungen Islam, Chang, Colvin, Byrne, McCully, Moser, Lira, Charo, Luster: "Mouse CCL8, a CCR8 agonist, promotes atopic dermatitis by recruiting IL-5+ T(H)2 cells." in: Nature immunology, Vol. 12, Issue 2, pp. 167-77, 2011 (PubMed).

Rom, Rom, Passiatore, Pacifici, Radhakrishnan, Del Valle, Piña-Oviedo, Khalili, Eletto, Peruzzi: "CCL8/MCP-2 is a target for mir-146a in HIV-1-infected human microglial cells." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 24, Issue 7, pp. 2292-300, 2010 (PubMed).

Struyf, Proost, Vandercappellen, Dempe, Noyens, Nelissen, Gouwy, Locati, Opdenakker, Dinsart, Van Damme: "Synergistic up-regulation of MCP-2/CCL8 activity is counteracted by chemokine cleavage, limiting its inflammatory and anti-tumoral effects." in: European journal of immunology, Vol. 39, Issue 3, pp. 843-57, 2009 (PubMed).

Dean, Cox, Bellac, Doucet, Starr, Overall et al.: "Macrophage-specific metalloelastase (MMP-12) truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating ..." in: Blood, Vol. 112, Issue 8, pp. 3455-64, 2008 (PubMed).

Hori, Naishiro, Sohma, Suzuki, Hatakeyama, Yamamoto, Sonoda, Mizue, Imai, Tsutsumi, Kokai: "CCL8 is a potential molecular candidate for the diagnosis of graft-versus-host disease." in: Blood, Vol. 111, Issue 8, pp. 4403-12, 2008 (PubMed).

Proost, Struyf, Couvreur, Lenaerts, Conings, Menten, Verhaert, Wuyts, Van Damme: "Posttranslational modifications affect the activity of the human monocyte chemotactic proteins MCP-1 and MCP-2: identification of MCP-2(6-76) as a natural chemokine inhibitor." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 160, Issue 8, pp. 4034-41, 1998 (PubMed).

Van Damme, Proost, Lenaerts, Opdenakker: "Structural and functional identification of two human, tumor-derived monocyte chemotactic proteins (MCP-2 and MCP-3) belonging to the chemokine family." in: The Journal of experimental medicine, Vol. 176, Issue 1, pp. 59-65, 1992 (PubMed).

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