NCF4 Antibody | 18-497

NCF4 Antibody | 18-497 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Mouse, Rat

Homology: N/A

Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 1-190 of human NCF4 (NP_038202.2) .

Research Area: Cancer, Cell Cycle, Signal Transduction

Tested Application: WB, IHC, IF

Application: WB: 1:500 - 1:2000
IHC: 1:50 - 1:200
IF: 1:50 - 1:200

Specificiy: N/A

Positive Control 1: HL-60

Positive Control 2: Jurkat

Positive Control 3: Mouse liver

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: Observed: 42kDa

Validation: N/A

Isoform: N/A

Purification: Affinity purification

Clonality: Polyclonal

Clone: N/A

Isotype: IgG

Conjugate: Unconjugated

Physical State: Liquid

Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Concentration: N/A

Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.

Alternate Name: NCF4, MGC3810, NCF, P40PHOX, SH3PXD4

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: The protein encoded by this gene is a cytosolic regulatory component of the superoxide-producing phagocyte NADPH-oxidase, a multicomponent enzyme system important for host defense. This protein is preferentially expressed in cells of myeloid lineage. It interacts primarily with neutrophil cytosolic factor 2 (NCF2/p67-phox) to form a complex with neutrophil cytosolic factor 1 (NCF1/p47-phox) , which further interacts with the small G protein RAC1 and translocates to the membrane upon cell stimulation. This complex then activates flavocytochrome b, the membrane-integrated catalytic core of the enzyme system. The PX domain of this protein can bind phospholipid products of the PI (3) kinase, which suggests its role in PI (3) kinase-mediated signaling events. The phosphorylation of this protein was found to negatively regulate the enzyme activity. Alternatively spliced transcript variants encoding distinct isoforms have been observed.