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Parkinson`s disease is predominantly a movement disorder resulting from degeneration of dopaminergic neurons in the substantia nigra. The cause of the disease is unknown, but substantial evidence suggests that the aggregation of α-synuclein is a critical step in the etiology of Parkinson`s disease (PD). α-Synuclein is an abundant brain protein of 140 residues that is present in high concentration at presynaptic terminals and is found in both soluble and membrane-associated fractions of the brain. Several possible functions have been suggested for α-synuclein, and it also appears to be involved in vesicle release and trafficking. In vitro incubation in the presence of a specific amount of salt (i.e. 0.1M NaCl) with agitation shows α-synuclein forming fibrilous structure.

Myelin Oligodendrocyte Glycoprotein (MOG) is a member of the immunoglobulin superfamily and is expressed exclusively in the central nervous system (CNS). Although MOG protein constitutes only 0.01-0.05% of the CNS myelin proteins, it was demonstrated that MOG protein is a crucial autoantigen for multiple sclerosis in humans and experimental autoimmune encephalomyelitis (EAE) in rodents and monkeys The sequence (Accession #CAE84068) corresponding to the extracellular domain of rat MOG along with a 6x His tag was expressed in E. coli. The recombinant rat MOG (R-rMOG) was purified from urea denatured bacterial lysate using immobilized metal affinity chromatography (IMAC). The molecular mass of the recombinant rat MOG is 14.2 kDa.

Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-9 (92-kDa gelatinase, collagenase-IV) is involved in a number of diseases such as cancer, angiogenesis, alopecia, and metastasis. MMP-9 is secreted as zymogen with prodomain, gelatin-binding domain consisting of three contiguous fibronectin type II units, catalytic domain, proline-rich linker region, and C-terminal hemopexin-like domain. It can degrade a variety of substrates, including gelatin, collagens type IV, V, XIV, a2-macroglobulin, elastin, vitronectin, and proteoglycans The sequence (Accession # NP_038627) corresponding to the catalytic domain (aa 112-445) of Mouse MMP-9 was expressed in E. coli. The recombinant mouse MMP-9 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Mouse MMP-9 Catalytic Domain is ~38 kDa.