MCP-1/CCL2 Protein, Human (Biotinylated, HEK293, His-Avi)

MCP-1/CCL2 Protein, Human (Biotinylated, HEK293, His-Avi) is a cytokine belonging to the CC chemokine family that interacts with the CCR2 chemokine receptor on the cell surface to mediate inflammatory immune responses, viral infections, and tumorigenesis. MCP-1/CCL2 Protein MCP-1/CCL2 Protein, Human (Biotinylated, HEK293, His-Avi) is a biotinylated recombinant human MCP-1/CCL2 (Q24-T99) expressed by HEK293 with His and Avi tags at the C-terminus^[1].

CCL2, also known as monocyte chemotactic protein 1 (MCP1), is a small cell factor belonging to the CC chemokine family. The CCL2 gene, located in the q11.2-q12 region of human chromosome 17, encodes a monomeric polypeptide with a molecular weight of 9-15 kDa, depending on the level of glycosylation. CCL2 is mainly secreted by monocytes, macrophages and dendritic cells. It is secreted by monocytes, macrophages and dendritic cells, and platelet-derived growth factor is the main inducer of the CCL2 gene. Astrocytes and microglia are also thought to be the source of CCL2^[1]. CCL2 signals through binding to and activation of CCR2 and induces a strong chemotactic response and intracellular mobilization of calcium ions. Among other things, CCL2/CCR2 can regulate cell adhesion and chemotaxis of macrophages by activating the β1 integrin and p38-MAPK signaling pathways. In addition to acting as a chemoattractant, CCL2 can also regulate brain endothelial permeability in vitro by altering tight junction (TJ) proteins and regulating the expression of endothelial adhesion molecules and leukocyte integrins as well as cytokine production. In addition, the CCL2-CCR2 signaling axis has been implicated in many inflammatory and neurodegenerative diseases, acting to recruit inflammatory cells into the CNS^[2].  Originally described as a "tumor-derived chemokine", CCL2 has been shown to be a potent chemokine for many types of immune cells and a potential target for the treatment of many diseases, such as atherosclerosis, multiple sclerosis, asthma, neuropathic pain, diabetic nephropathy, and cancer^[3].

CCL2 (10 ng/mL, 24 h) is secreted from tumor-associated macrophages (TAMs) co-cultured with MCF10A human breast epithelial cells, induces ERO1-α, leading to MMP-9 upregulation and an invasive phenotype of MCF10A cells^[4].
CCL2 (1-100 ng/mL, 96 h) can induce PC-3 and VCaP cell migration, proliferation, and Akt phosphorylation in a dose-dependent manner. In addition, CCL2 stimulates phosphorylation of p70-S6 kinase (a downstream target of Akt) and induces actin rearrangement^[5].

Human

HEK293

C-Avi;C-6*His

P13500 (Q24-T99)

6347  [NCBI]

Full Length of Mature Protein

Biotin

QPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT

13-20 kDa

≥ 95%, as determined by Bis-Tris PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Qiongyu Hao, et al.  CCL2/CCR2 signaling in cancer pathogenesis. Cell Commun Signal. 2020 May 29;18(1):82.  [Content Brief]

  [2]. Svetlana M Stamatovic, et al. Monocyte chemoattractant protein-1 regulation of blood-brain barrier permeability. J Cereb Blood Flow Metab. 2005 May;25(5):593-606.  [Content Brief]

  [3]. Rachel N Gomes, et al. Bacterial clearance in septic mice is modulated by MCP-1/CCL2 and nitric oxide. Shock. 2013 Jan;39(1):63-9.  [Content Brief]

  [4]. Seungeun Lee, et al. Tumor-associated macrophages secrete CCL2 and induce the invasive phenotype of human breast epithelial cells through upregulation of ERO1-α and MMP-9. Cancer Lett. 2018 Nov 28;437:25-34.  [Content Brief]

  [5]. Robert D Loberg, et al. CCL2 is a potent regulator of prostate cancer cell migration and proliferation. Neoplasia. 2006 Jul;8(7):578-86.  [Content Brief]