Anti-ADAM22 (extracellular)

Antibodies

Disintegrin and metalloproteinase domain-containing protein 22, ADAM metallopeptidase domain 22, MDC2

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

Disintegrin and metalloproteinase domain-containing protein 22, ADAM metallopeptidase domain 22, MDC2 - A Rabbit Polyclonal Antibody to ADAM22

Rat, human - identical

Confirmed by amino acid analysis and mass spectrometry

0.8 mg/ml

Extracellular, N-terminus

Mouse

41116161

ADAMs (a disintegrin and metalloproteinases) are multi-domain transmembrane glycoproteins with diverse roles in physiology and disease. Notably, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.ADAM22 is a non-proteinase which acts as a post synaptic receptor for the secreted neurotransmission modulator LGI-1 at neural synapses. ADAM22 is a compact four-leaf clover with the metalloproteinase-like domain (Domain M) held in the concave face of a rigid module formed by the disintegrin (Domain D), cysteine-rich (Domain C), and epidermal growth factor-like domains (Domain E). The largest domain in the four-leaf clover, domain M, is distal to the cell membrane. Following domain M, domain D and domain C zigzag to domain E in a compact, but not extended fashion. A 15-amino acid linker, leads the C terminus of domain E to the membrane. The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain. The extracellular domain of ADAM22 interacts with LGI-1, whereas its cytoplasmic PDZ-binding motif recruits PSD-95. The link of ADAM22 and LGI-1 to AMPA receptors establishes their roles in glutamate neurotransmission1.Mutations that impair LGI-1 binding to ADAM22 are implicated in the pathogenesis of Autosomal dominant lateral temporal epilepsy (ADTLE), a focal epilepsy syndrome characterized by focal seizures with prominent auditory or aphasic symptoms, normal magnetic resonance imaging, and usually benign evolution2.