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Anti-Cytochrome b-245/p22phox, clone 44.1, Cat. No. MABS2192, is a mouse monoclonal antibody that detects Cytochrome b-245 light chain and is tested for use in Flow Cytometry and Western Blotting.
More>>Anti-Cytochrome b-245/p22phox, clone 44.1, Cat. No. MABS2192, is a mouse monoclonal antibody that detects Cytochrome b-245 light chain and is tested for use in Flow Cytometry and Western Blotting. Less<<
Cytochrome b-245 light chain (UniProt: P13498; also known as Cytochrome b(558) alpha chain, Cytochrome b558 subunit alpha, Neutrophil cytochrome b 22 kDa polypeptide, Superoxide-generating NADPH oxidase light chain subunit, p22 phagocyte B-cytochrome, p22-phox, p22phox) is encoded by the CYBA gene (Gene ID: 1535) in human. Cytochrome b-245 is a heterodimeric integral membrane protein that is composed of a heavily glycosylated large beta subunit (gp91phox) and a small alpha subunit (p22phox) that serves as the central, catalytic core of the NADPH oxidase complex. The N-terminal half of beta subunit contains six potential transmembrane helices with conserved histidine residues that coordinate the two heme prosthetic groups and its C-terminal, cytosolic domain shows sequence homology with the ferredoxin-NADP+ oxidoreductase (FNR) enzyme family and coordinates the FAD and NADPH cofactors that serve as redox centers for the generation of superoxide anion. The primary sequence of alpha subunit is highly conserved. It contains three or four transmembrane domains. The cytoplasmic domain of alpha subunit contains a proline-rich region, which is involved in its interactions with the cytoplasmic oxidase component p47phox. Phosphorylation at threonine 147 is reported to enhance NADPH oxidase activity by promoting p47phox binding. The alpha subunit has been proposed as a primary component of the microbicidal oxidase system of phagocytes. It associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. Mutations in CYBA gene are known to cause autosomal recessive chronic granulomatous disease that is characterized by the failure of activated phagocytes to generate superoxide. (Ref.: Taylor, RM., et al. (2004). J. Immunol. 173(12); 7349-7357).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG2a in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Applications
Application
Anti-Cytochrome b-245/p22phox, clone 44.1, Cat. No. MABS2192, is a mouse monoclonal antibody that detects Cytochrome b-245 light chain and is tested for use in Flow Cytometry and Western Blotting.
Key Applications
Flow Cytometry
Western Blotting
Application Notes
Western Blotting Analysis: A representative lot detected Cytochrome b-245/p22phox in Western Blotting applications (Burritt, J.B., et. al. (1995). J Biol Chem. 270(28):16974-80).
Flow Cytometry Analysis: A representative lot detected Cytochrome b-245/p22phox in Flow Cytometry applications (Burritt, J.B., et. al. (1995). J Biol Chem. 270(28):16974-80).
Biological Information
Immunogen
Partially purified human neutrophil flavocytochrome b-245 light chain.
Clone
44.1
Host
Mouse
Specificity
Clone 44.1 is a mouse monoclonal antibody that detects human cytochrome b-245. It recognizes a discontinuous epitope within 5 amino acids from the N-terminal region and 6 amino acids from the C-terminal region.
~22 kDa observed; 21.01 kDa calculated. Uncharacterized bands may be observed in some lysate(s).
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in THP-1 cell lysate.
Western Blotting Analysis: 1 µg/mL of this antibody detected Cytochrome b-245/p22phox light chain in THP-1 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Cytochrome b of human neutrophils is the central component of the microbicidal NADPH-oxidase system. However, the folding topology of this integral membrane protein remains undetermined. Two random-sequence bacteriophage peptide libraries were used to map structural features of cytochrome b by determining the epitopes of monoclonal antibodies (mAbs) 44.1 and 54.1, specific for the p22phox and gp91phox cytochrome b chains, respectively. The unique peptides of phage selected by mAb affinity purification were deduced from the phage DNA sequences. Phage selected by mAb 44.1 displayed the consensus peptide sequence GGPQVXPI, which is nearly identical to 181GGPQVNPI18 of p22phox. Phage selected by mAb 54.1 displayed the consensus sequence PKXAVDGP, which resembles 382PKIAVDGP389 of gp91phox. Western blotting demonstrated specific binding of each mAb to the respective cytochrome b subunit and selected phage peptides. In flow cytometric analysis, mAb 44.1 bound only permeabilized neutrophils, while 54.1 did not bind intact or permeabilized cells. However, mAb 54.1 immunosedimented detergent-solubilized cytochrome b in sucrose gradients. These results suggest the 181GGPQVNPI188 segment of p22phox is accessible on its intracellular surface, but the 382PKIAVDGP389 region on gp91phox is not accessible to antibody, and probably not on the protein surface.
