CYBB Antibody - C-terminal region
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB |
---|---|
Primary Accession | P04839 |
Other Accession | NM_000397, NP_000388 |
Reactivity | Human, Mouse, Rat, Rabbit, Pig, Horse, Bovine, Guinea Pig, Dog |
Predicted | Human, Mouse, Rat, Rabbit, Pig, Horse, Bovine, Guinea Pig, Dog |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 62kDa |
Gene ID | 1536 |
---|---|
Alias Symbol | AMCBX2, CGD, GP91-1, GP91-PHOX, GP91PHOX, NOX2, p91-PHOX |
Other Names | Cytochrome b-245 heavy chain, 1.-.-.-, CGD91-phox, Cytochrome b(558) subunit beta, Cytochrome b558 subunit beta, Heme-binding membrane glycoprotein gp91phox, NADPH oxidase 2, Neutrophil cytochrome b 91 kDa polypeptide, Superoxide-generating NADPH oxidase heavy chain subunit, gp91-1, gp91-phox, p22 phagocyte B-cytochrome, CYBB, NOX2 |
Format | Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose. |
Reconstitution & Storage | Add 50 &mu, l of distilled water. Final Anti-CYBB antibody concentration is 1 mg/ml in PBS buffer with 2% sucrose. For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles. |
Precautions | CYBB Antibody - C-terminal region is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CYBB (HGNC:2578) |
---|---|
Synonyms | NOX2 |
Function | Catalytic subunit of the phagocyte NADPH oxidase complex that mediates the transfer of electrons from cytosolic NADPH to O2 to produce the superoxide anion (O2(-)) (PubMed:15338276, PubMed:36241643, PubMed:36413210, PubMed:38355798). In the activated complex, electrons are first transferred from NADPH to flavin adenine dinucleotide (FAD) and subsequently transferred via two heme molecules to molecular oxygen, producing superoxide through an outer-sphere reaction (Probable) (PubMed:38355798). Activation of the NADPH oxidase complex is initiated by the assembly of cytosolic subunits of the NADPH oxidase complex with the core NADPH oxidase complex to form a complex at the plasma membrane or phagosomal membrane (PubMed:19028840, PubMed:38355798). This activation process is initiated by phosphorylation dependent binding of the cytosolic NCF1/p47-phox subunit to the C-terminus of CYBA/p22-phox (By similarity). NADPH oxidase complex assembly is impaired through interaction with NRROS (By similarity). |
Cellular Location | Cell membrane; Multi-pass membrane protein. Note=As unassembled monomer may localize to the endoplasmic reticulum |
Tissue Location | Detected in neutrophils (at protein level). |

Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.
References
Royer-Pokora B.,et al.Nature 322:32-38(1986).
Jirapongsananuruk O.,et al.Clin. Immunol. 104:73-76(2002).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Dinauer M.C.,et al.Nature 327:717-720(1987).

If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.