ADAM22 Antikörper (Extracellular, N-Term)
Kurzübersicht für ADAM22 Antikörper (Extracellular, N-Term) (ABIN7884717)
Target
Alle ADAM22 Antikörper anzeigenReaktivität
Wirt
Klonalität
Konjugat
Applikation
Güteklasse
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Bindungsspezifität
- AA 715-729, Extracellular, N-Term
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Verwendungszweck
- A Rabbit Polyclonal Antibody to ADAM22
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Homologie
- Rat,human - identical
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Aufreinigung
- 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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Isotyp
- IgG
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Applikationshinweise
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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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Kommentare
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Negative Control: (ABIN7234619)
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Beschränkungen
- Nur für Forschungszwecke einsetzbar
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Format
- Lyophilized
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Rekonstitution
- 0.2 mL double distilled water (DDW)
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Konzentration
- 1 mg/mL
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Buffer
- PBS pH 7.4
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Konservierungsmittel
- Without preservative
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Lagerung
- -20 °C
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Informationen zur Lagerung
- 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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Andere Bezeichnung
- Disintegrin and metalloproteinase domain-containing protein 22
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Hintergrund
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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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Gen-ID
- 11496
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UniProt
- Q9R1V6
Target
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