ADAM22 antibody (Extracellular, N-Term)
Quick Overview for ADAM22 antibody (Extracellular, N-Term) (ABIN7884717)
Target
See all ADAM22 AntibodiesReactivity
Host
Clonality
Conjugate
Application
Grade
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Binding Specificity
- AA 715-729, Extracellular, N-Term
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Purpose
- A Rabbit Polyclonal Antibody to ADAM22
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Predicted Reactivity
- Rat,human - identical
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Purification
- Affinity purified on immobilized antigen.
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Immunogen
- (C)HNDDAKTGITLSGNG, corresponding to amino acid residues 715-729 of mouse ADAM22
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Isotype
- IgG
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Application Notes
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WB: 1:200
FC: The optimal concentration should be determined by the user
ICC: The optimal concentration should be determined by the user
IHC: 1:200
IP: The optimal concentration should be determined by the user
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Comment
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Negative Control: (ABIN7234619)
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Restrictions
- For Research Use only
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Format
- Lyophilized
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Reconstitution
- 0.2 mL double distilled water (DDW)
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Concentration
- 1 mg/mL
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Buffer
- PBS pH 7.4
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Preservative
- Without preservative
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Storage
- -20 °C
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Storage Comment
- The antibody ships as a lyophilized powder at room temperature. Upon arrival, it should be stored at -20°C
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- ADAM22 (ADAM Metallopeptidase Domain 22 (ADAM22))
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Alternative Name
- Disintegrin and metalloproteinase domain-containing protein 22
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Background
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Synonyms: Disintegrin and metalloproteinase domain-containing protein 22, ADAM metallopeptidase domain 22, MDC2
Description: 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.
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Gene ID
- 11496
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UniProt
- Q9R1V6
Target
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