18-aa peptide near the C-terminus of rat g-synuclein. The rat peptide sequence is 100% conserved in mouse g-synuclein. No significant sequence homology is seen with either human g-synuclein or synucleins-alpha or beta) or other proteins. Alzheimers Disease (AD) is a neurodegenerative disorder characterized by progressive loss of memory and cognition in the elderly. One of the most important and initial step involves proteolytic cleavage of amyloid precursor protein (APP, chromosome 21) releasing short 40, 42 & 43 aa peptides (beta amyloid1-40, 1-42, and 1-43). Polymerization of b-amyloid (Ab) and subsequent neuronal deposit (amyloid) leads to the degeneration of neurons involved in memory and cognition. Ab deposits have also been found to contain 2 additional proteins termed a-synuclein and b-synuclein. The 140 aa a-synucleins is identical with non-Ab component (NACP) of AD. The 134 aa b-synuclein is homologous to 14kD bovine phosphoneuroprotein 14. Mutations in a-synuclein gene causing a replacement of alanine with a threonine has the potential to cause the protein to misfold. Synucleins are primarily expressed in the brain. At least 3 forms, two large (140 aa SYN-1 & 149 aa SYN-2) and a small form (SYN-3, 42 aa) are produced by alternative splicing. Recently a new isoform, termed g-synuclein (SNCG) or breast cancer gene 1 (BCG1) has been cloned (human 127 aa, rat/mouse 123 aa). All three synucleins shown ~40% identity. g-synuclein is primarily expressed in brain (substantia nigra), and over expressed in advanced infiltrating carcinoma of breast, and in ovarian cancer. Storage and Stability: Lyophilized powder may be stored at -20C. Stable for 12 months at -20C. Reconstitute with sterile buffer or ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Reinheit:
Purified
Formulierung:
Supplied as a lyophilized powder from PBS, 0.05% sodium azide.
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