Anti-MANF

Antibodies

Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich mutated in early stage tumors, ARP

Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C

Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4

Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich mutated in early stage tumors, ARP - A Rabbit Polyclonal Antibody to MANF

Rat, mouse - identical

Confirmed by amino acid analysis and mass spectrometry

0.8 mg/ml

Mature MANF protein

Human

41116161

The novel protein mesencephalic astrocyte-derived neurotrophic factor (MANF) is a survival molecule (alternatively referred to as arginine-rich, mutated in early stage tumors, or ARMET) that has high selectivity for dopaminergic neurons of the midbrain1, 2. There, it induces proliferative and protective effects against neurodegeneration (usually caused by 6-hydroxydopamine); its therapeutic potential in dopamine-related neurodegenerative disorders such as Parkinson's disease is therefore promising3, 4.MANF is also expressed cardiac tissues. As was recently suggested, it induces cardioprotection in the heart and anti-hypertrophic effects via reducing endoplasmic reticulum stress in ischemic conditions in both the heart and the brain. Thus, its effects stretch beyond rescue and protection of dopaminergic neurons alone1, 5.Generally, neurotrophic factors (NTFs) provide support, protection, and regulation for neurons - with each group of neurons having their own unique NTFs - both during development and at adulthood. Other noticeable NTFs include neurotrophin-3 and -4 (NT3 and NT4), nerve growth factor (NGF), brain derived neurotrophic factor (BDNF), and glial cell derived neurotrophic factor (GDNF)6.MANF is considered to be evolutionary conserved within Mammalia and beyond (including distant species such as nematode and fruit fly - the latter shares more than 50% identity with human MANF gene) and is highly mutative in many tumors. It is mostly composed of alpha helices and random coils; its structure essentially differs from any other neurotrophic factor. It is suggested that the protein initiates intracellular signaling cascade by binding to cell-surface lipids and membranes via its cysteine-rich N-terminal. Together with its C-terminal which contains a disulfide bridge that endows a cytoprotective response against ER stress, MANF is implied to be bi-functional3, 7.