The Cancer-associated Growth Factor Antibody Sampler Kit provides an economical means of detecting selected growth factors that have been shown to influence tumor development. The kit includes enough antibodies to perform two western blot experiments with each primary antibody.
Specificity / Sensitivity
Each antibody in the Cancer-associated Growth Factor Antibody Sampler Kit detects endogenous levels of its total target protein. VEGF-A Antibody recognizes endogenous levels of all isoforms of total VEGF-A protein. This antibody also detects a 47 kDa band of unknown identity. TGF-β (56E4) Rabbit mAb detects endogenous levels of TGF-β precursor proteins. The antibody preferentially detects TGF-β1 and TGF-β3 proteins, as determined by western blot analysis of recombinant proteins. HBEGF (E5L5T) Rabbit mAb recognizes endogenous levels of total proHBEGF and mature HBEGF protein. This antibody also detects a 58 kDa band of unknown origin. MIF (E7T1W) Rabbit mAb recognizes endogenous levels of total MIF protein. Non-specific staining by MIF (E7T1W) Rabbit mAb was observed in mouse brain by immunohistochemistry. EREG (D4O5I) Rabbit mAb recognizes endogenous levels of proepiregulin and the C-terminal propeptide of the EREG protein. It does not recognize the mature form of EREG.
Source / Purification
Monoclonal antibodies are produced by immunizing animals with recombinant protein specific to the mature full-length human basic FGF protein, with recombinant protein fragment specific to human mature HBEGF protein, with recombinant protein specific to the carboxy terminus of human HGF protein, with synthetic peptides corresponding to residues surrounding Ser83 of human IGF-I protein, Tyr100 of human MIF protein, and Glu155 of human EREG protein, and with synthetic peptides corresponding to a region in the carboxy terminus of TGF-β1 protein.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptides corresponding to residues surronding His38 of human VEGFA protein and Asp200 of human angiopoietin-2 protein. Antibodies are purified by peptide affinity chromatography.
The tumor microenvironment (TME) is composed of a heterogenous mixture of tumor cells, blood vessels, fibroblasts, stromal cells, infiltrating immune cells, and extracellular matrix (ECM) components, whose collective interactions play important roles in tumor development (1). Cells in the TME secrete a variety of bioactive molecules, including growth factors, cytokines, ECM proteins, and proteases (e.g., MMPs), many of which play critical roles in regulating growth and development of the tumor (2,3). Growth factors play particularly important roles in the TME, serving as cellular messengers that trigger activation or suppression of signaling pathways that govern tumor development, either directly via the tumor cells, or indirectly by way of effects on the TME. Binding of growth factors to their cognate receptors leads to activation of intracellular signaling pathways, resulting in changes in the expression of target genes that regulate cell behavior. Many growth factors (e.g., IGFs, HGFs, FGFs, HBEGF, EREG) are known to promote tumor development by way of direct effects on tumor cells; other growth factors can affect tumor development indirectly, through effects in the TME that influence tumor angiogenesis (e.g., VEGFs, angiopoietins), ECM deposition (TGF-β), or immune cell signaling (e.g., TGF-β, HBEGF, MIF) (4). The diverse and complex role played by growth factors in promoting tumorigenesis makes them important therapeutic targets in oncology, while elucidating the functions of specific growth factors in the context of tumor development remains an active area of cancer research (5).