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>   首页   >   产品   >   一抗   >   癌症   >   Rabbit Anti-NOX2/gp91phox Polyclonal Antibody   

Rabbit Anti-NOX2/gp91phox Polyclonal Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Rabbit Anti-NOX2/gp91phox Polyclonal Antibody AP52079
    Mouse spleen lysates probed with NOX2/gp91phox Polyclonal Antibody, unconjugated (AP52079) at 1:300 overnight at 4°C followed by a conjugated secondary antibody at 1:10000 for 60 minutes at 37°C.
  • 14 - Rabbit Anti-NOX2/gp91phox Polyclonal Antibody AP52079
    Formalin-fixed and paraffin embedded rat pancreas labeled with Anti NOX2/gp91phox Polyclonal Antibody, Unconjugated (AP52079) at 1:200 followed by conjugation to the secondary antibody and DAB staining
  • 14 - Rabbit Anti-NOX2/gp91phox Polyclonal Antibody AP52079
    Formalin-fixed and paraffin embedded rat brain labeled with Rabbit Anti-NOX2/gp91phox Polyclonal Antibody, Unconjugated (AP52079) at 1:200 followed by conjugation to the secondary antibody and DAB staining
  • 14 - Rabbit Anti-NOX2/gp91phox Polyclonal Antibody AP52079
    Formalin-fixed and paraffin embedded rat brain labeled with Rabbit Anti-NOX2/gp91phox Polyclonal Antibody, Unconjugated (AP52079) at 1:200 followed by conjugation to the secondary antibody Goat Anti-Rabbit IgG, Cy3 conjugated used at 1:200 dilution for 40 minutes at 37°C.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, IHC-F, IF, E
Primary Accession P04839
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW 65336 Da
Physical State Liquid
Immunogen KLH conjugated synthetic peptide derived from human NOX2
Epitope Specificity 501-570/570
Isotype IgG
Purity affinity purified by Protein A
Buffer 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
SUBCELLULAR LOCATION Membrane.
SIMILARITY Contains 1 FAD-binding FR-type domain. Contains 1 ferric oxidoreductase domain.
Post-translational modifications Glycosylated.
DISEASE Defects in CYBB are a cause of chronic granulomatous disease X-linked (XCGD) [MIM:306400]. Chronic granulomatous disease is a genetically heterogeneous disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections.
Important Note This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
Background Descriptions NOX2/gp91phox is a 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. It 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. Defects in CYBB are a cause of X-linked chronic granulomatous disease (X-CGD). X-CGD is characterized by the failure of activated phagocytes to generate superoxide. Patients suffer from life-threatening bacterial/fungal infections.
Additional Information
Gene ID 1536
Other Names CGD; NOX2; IMD34; AMCBX2; GP91-1; GP91PHOX; p91-PHOX; GP91-PHOX; Cytochrome b-245 heavy chain; 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; p22 phagocyte B-cytochrome; CYBB
Dilution WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500,ELISA=1:5000-10000
Format0.01M TBS(pH7.4) with 1% BSA, 0.09% (W/V) sodium azide and 50% Glyce
StorageStore at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Protein Information
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).
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

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).

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