Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease caused by the death of motor neurons in the brain and spinal cord. The loss of neuronal input leads to progressive paralysis and patient mortality within 2-5 years from diagnosis. ALS likely arises from a combination of genetic susceptibility and environmental exposures, although it is recognized that ALS is a complex, multi-system disease.
Mutations in several genes can cause familial ALS and contribute to the development of sporadic ALS. The C9orf72, SOD1, TARDBP, and FUS genes are key to the normal functioning of motor neurons and other cells. Mutations in the C9orf72 gene account for 30 to 40 percent of familial ALS in the United States and Europe. Worldwide, SOD1 gene mutations cause 15 to 20 percent of familial ALS, and TARDBP and FUS gene mutations each account for about 5 percent of cases. The other genes that have been associated with familial ALS each account for a small proportion of cases.
No single biochemical abnormality is specific to the diagnosis of ALS. Some have been evaluated as specific and sensitive markers of the disease, although none has proven to be robust. These have included CSF studies, such as measures of protein content, amino acids, and glutamate. Some markers of oxidative injury are elevated in the CSF of patients with ALS, including indices of DNA oxidative injury, protein oxidation, and lipid peroxides. Other reported biochemical changes include increased serum levels of lipid peroxides in sporadic ALS, and increased serum levels of matrix metalloproteinase-9 and transforming growth factor-1.
It is not yet known when the initial pathological changes of ALS begin, but it seems likely that the clinical manifestations occur significantly downstream of what may be rapidly irreversible primary events at the cellular level. Earlier diagnosis would permit introduction of therapies nearer to these initiating events.
The astrocytic glutamate transporter EAAT2 is responsible for the clearance of synaptic glutamate, and its knockout in transgenic mice results in neuronal death. Reduced levels of spinal cord EAAT2 protein have been noted in end-stage rodent transgenic models of ALS, with abnormalities of EAAT2 protein expression demonstrable in up to 80% of human post mortem brain and spinal cord tissue.
| Cat. No | Product Name | Reactivity | Application |
| CABT-38279MH | Anti-SLC1A2 monoclonal antibody, clone OTF | H | WB, ELISA |
| DCABH-6469 | Anti-Human GLT-1 monoclonal antibody, clone 0I0M28 | H, M, R | ICC, IF, WB |
| DPAB-DC2882 | Anti-SLC1A2 (aa 160-239) polyclonal antibody | H | WB, ELISA |
Oxidative stress arises from an alteration in the balance between the generation of reactive oxygen species (ROS) and their removal, together with the ability of the biological system to remove or repair ROS induced damage. The mutations in SOD1, which encodes a major anti-oxidant defence protein, accounted for approximately 20% of cases of familial ALS. Indices of oxidative damage are also present in cellular and murine models of SOD1 -related ALS.
| Cat. No | Product Name | Reactivity | Application |
| CABT-54815MS | Anti-SOD1 monoclonal antibody, clone 2F5 | H, M, B | IHC-Fr, ELISA, IHC-P |
| CABT-37098RH | Anti-SOD1 monoclonal antibody, clone KG2116 | H, R | WB, ICC/IF, IHC, FC |
| DCABH-9035 | Anti-SOD1 monoclonal antibody, clone FQ2838Z | H, R | WB, FC, IHC-P, ICC/IF |
| DCABH-13554 | Anti-SOD1 monoclonal antibody, clone 7G6 | H, M | WB, IF, ELISA, FC |
Inflammatory mechanisms and immune reactivity are hypothesized to play a role in the pathogenesis of ALS. Studies in patients with ALS have found elevated markers of inflammation (CRP, interleukin-6 and 13, macrophage chemotactic protein-1 (MCP-1)). Levels of MCP-1 and other chemokines have also been detected in the CSF of ALS patients. Such proteins may contribute to the amplification or possibly initiation of inflammation during ALS.
| Cat. No | Product Name | Reactivity | Application |
| CABT-WN1745 | Anti-CCL2 monoclonal antibody, clone 3I6 | H, M, R | WB, IHC, ELISA(Cap), ELISPOT |
| DCABH-4176 | Anti-Human MCP-1 monoclonal antibody, clone 30I97M67 | H | ICC, IF, WB |
| DPAB-DC2789 | Anti-CCL2 (aa 24-99) polyclonal antibody | H | WB, ELISA |
TAR DNA-binding protein 43 (TDP-43, transactive response DNA binding protein 43 kDa), is a protein that in humans is encoded by the TARDBP gene. In spinal motor neurons TDP-43 has also been shown in humans to be a low molecular weight neurofilament (hNFL) mRNA-binding protein. A hyper-phosphorylated, ubiquitinated and cleaved form of TDP-43—known as pathologic TDP43—is the major disease protein in ubiquitin-positive, tau-, and alpha-synuclein-negative frontotemporal dementia (FTLD-TDP, previously referred to as FTLD-U[21]) and in amyotrophic lateral sclerosis (ALS).
| Cat. No | Product Name | Reactivity | Application |
| CABT-B1772 | Anti-TDP-43 polyclonal antibody | H | WB, ICC |
| DPABH-04106 | Anti-TARDBP (aa 1-289) polyclonal antibody | H, M, R | WB, IHC-P, ICC/IF |
| DPABH-15906 | Anti-Human TARDBP polyclonal antibody | H, M | WB, IP, IHC |
Species: H Human; M Mouse; R Rat; Z Zebrafish; X Xenopus laevis; B Bovine; C Cow; D Dog; P Pig; Q Quail
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