BotA (AA 1280-1292), (C-Term) anticorps

N° du produit ABIN7232852

L’anticorps anti-BotA Monoclonal Souris est utilisé pour la détection de BotA dans des échantillons de Clostridium botulinum. Il a été validé pour ELISA, IF/ICC et RIA.

Aperçu rapide pour BotA (AA 1280-1292), (C-Term) anticorps (ABIN7232852)

Antigène: BotA

Reactivité: Clostridium botulinum

Hôte: Souris

Clonalité: Monoclonal

Conjugué: Inconjugué

Application: ELISA, Immunofluorescence (fixed cells) (IF/ICC), Radioimmunoassay (RIA)

Clone: B364M

Détail du produit

Épitope: AA 1280-1292, C-Term

Fonction: Anti-Clostridium botulinum Toxin A Mouse Monoclonal Antibody

Specificité: This antibody recognizes C. botulinum Toxin A. It does not cross-react with Toxin B, C, E, or F.

Réactivité croisée: Clostridium botulinum

Purification: Whole Antiserum

Immunogène: Synthetic peptide corresponding to aa 1280-1292 (Cys-Ser-Trp-Glu-Phe-Ile-Pro-Val- Asp-Asp-Gly-Trp-Gly-COOH) at the C-terminus of Clostridium botulinum Toxin A.

Isotype: IgM

Information d'application

Indications d'application: ELISA, Immunocytochemistry, Immunofluorescence
End users should determine optimal dilutions for their applications.

Restrictions: For Research Use only

Stockage

Format: Liquid

Reconstitution: Dilute in PBS or medium that is identical to that used in the assay system.

Concentration: Lot specific

Buffer: Hybridoma culture supernatant, cell free media

Stock: -20 °C,-80 °C

Stockage commentaire: This antibody is stable for at least one (1) year at -20° to -70°C. Store product in appropriate aliquots to avoid multiple freeze-thaw cycles.

Détail du antigène

Antigène: BotA

Sujet: Botulinum neurotoxin type A,[Botulinum neurotoxin type A]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure (PubMed:8103915). Precursor of botulinum neurotoxin A which has 2 coreceptors, complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins of synaptic vesicles (By similarity). Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them (PubMed:19476346). Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway (By similarity). When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol (By similarity). Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). {UniProtKB:P0DPI0, PubMed:19476346, PubMed:8103915}., [Botulinum neurotoxin A light chain]: Has proteolytic activity (PubMed:8103915, PubMed:8294407). In vitro the whole toxin is reduced to release LC (PubMed:8103915, PubMed:8294407). After translocation into the eukaryotic host cytosol, LC hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP25, blocking neurotransmitter release (PubMed:8103915, PubMed:8294407). {PubMed:8103915, PubMed:8294407, PubMed:19476346}., [Botulinum neurotoxin A heavy chain]: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains, the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD) (PubMed:9783750, PubMed:17173035). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously rUniProtKB:P0DPI0, PubMed:17173035, PubMed:19476346, PubMed:21849494, PubMed:9783750}.,Clostridium botulinum, an anaerobic, gram-positive, spore-forming rod commonly found on plants, in soil, water, and the intestinal tracts of animals, produces eight antigenically distinguishable exotoxins (A, B, C1, C2, D, E, F and G). Type A is the most potent toxin, followed by types B and F. All botulinum neurotoxins are produced as single polypeptide chains of ~150 kDa comprised of a heavy (H) chain and a light (L) chain of roughly 100 and 50 kDa, respectively, linked by a disulfide bond. The heavy (H) chain of the toxin binds selectively and irreversibly to high affinity receptors at the presynaptic surface of cholinergic neurones, and the toxin-receptor complex is taken up into the cell by endocytosis where the disulfide bond between the two chains is cleaved. The light (L) chain interacts with different proteins in the nerve terminals to prevent fusion of acetylcholine vesicles with the cell membrane.,[Botulinum neurotoxin A light chain]: Secreted, Host cytoplasm, host cytosol, Host cell junction, host synapse, host presynaptic cell membrane, Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane, Multi-pass membrane protein

UniProt: P0DPI1