The BOTA Antibody (PAC034194) is a polyclonal antibody designed for research involving the CD300A protein, a cell surface molecule implicated in immune regulation. This antibody is highly reactive with human samples and has been validated for use in Western blot applications. By binding to CD300A, the antibody enables detection and analysis in various cell types, making it an ideal tool for studies in immunology and cancer research.CD300A, also known as an immune inhibitory receptor, plays a crucial role in immune homeostasis by regulating inflammation and inhibiting allergic reactions. Its significance in immune response modulation makes it a valuable target for research into diseases such as cancer, autoimmune disorders, and chronic inflammatory conditions.
Understanding the activity of CD300A is essential for developing therapies that harness or modulate immune function in these contexts.The BOTA Antibody is a valuable research tool for investigating the role of CD300A in immune regulation and its potential implications in disease pathogenesis. With its high reactivity and validation for Western blot applications, this antibody is well-suited for researchers exploring the intricate workings of the immune system and its impact on various health conditions.
Antibody Name:
botA Antibody (PACO34194)
Antibody SKU:
PACO34194
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA
Recommended Dilutions:
Species Reactivity:
Clostridium botulinum
Immunogen:
Recombinant Clostridium botulinum Botulinum neurotoxin type A protein (1-436AA)
Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln- |-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure.
Synonyms:
Botulinum neurotoxin type A (BoNT/A) (EC 3.4.24.69) (Bontoxilysin-A) (BOTOX) [Cleaved into: Botulinum neurotoxin A light chain; Botulinum neurotoxin A heavy chain], botA, atx bna
UniProt Protein Function:
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:15394302, PubMed:7578132). Precursor of botulinum neurotoxin A which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins of synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. 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 (PubMed:17666397, PubMed:19096517). 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. Toxin activity requires polysialylated gangliosides; GT1b supports activity better than GD1a (PubMed:12089155). Binds to host peripheral neuronal presynaptic membranes via the synaptic vesicle glycoproteins SV2A, SV2B and SV2C (PubMed:16543415). It binds directly to the largest lumenal (intravesicular) loop of SV2A, SV2B and SV2C that is transiently exposed outside of cells during exocytosis; gangliosides enhance binding (PubMed:16543415, PubMed:16545378, PubMed:18815274). Recognizes an N-linked glycan on SV2 proteins (PubMed:18815274, PubMed:27294781). May also use FGFR3 as a receptor (PubMed:23696738). Toxin uptake into neural cells requires stimulation (incubation with K+ to stimulate receptor exposure) to be internalized by receptor-mediated endocytosis (PubMed:16543415, PubMed:19650874, PubMed:21632541, PubMed:21832053). Subsequently the toxin colocalizes with its receptor in host cells (PubMed:16543415, PubMed:19650874). Toxin uptake can be blocked by the appropriate SV2 protein fragments in cell culture (PubMed:16543415).