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>   首页   >   产品   >   一抗   >   癌症   >   Cytochrome P450 4A11/22 Antibody   

Cytochrome P450 4A11/22 Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
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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, IP
Primary Accession Q02928
Reactivity Human
Host Rabbit
Clonality Polyclonal
Calculated MW 59348 Da
Additional Information
Gene ID 1579
Other Names Cytochrome P450 4A11, 20-hydroxyeicosatetraenoic acid synthase, 20-HETE synthase, CYP4AII, CYPIVA11, Cytochrome P-450HK-omega, Cytochrome P450HL-omega, Fatty acid omega-hydroxylase, Lauric acid omega-hydroxylase, CYP4A11, CYP4A2
Target/Specificity KLH-conjugated synthetic peptide encompassing a sequence within the center region of human Cytochrome P450 4A11/22. The exact sequence is proprietary.
Dilution WB~~1:1000
IP~~N/A
Format 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50%
StorageStore at -20 °C.Stable for 12 months from date of receipt
Protein Information
Name CYP4A11 {ECO:0000303|PubMed:8274222, ECO:0000312|HGNC:HGNC:2642}
Function A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins) (PubMed:10553002, PubMed:10660572, PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:10553002, PubMed:10660572, PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids, the catalytic efficiency decreasing in the following order: dodecanoic > tetradecanoic > (9Z)-octadecenoic > (9Z,12Z)- octadecadienoic > hexadecanoic acid (PubMed:10553002, PubMed:10660572). Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver (PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (PubMed:10620324, PubMed:10660572, PubMed:15611369). Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency (PubMed:7679927). May contribute to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acid, thereby initiating chain shortening (PubMed:18182499). Omega-hydroxylates (9R,10S)-epoxy-octadecanoate stereoisomer (PubMed:15145985). Plays a minor role in omega-oxidation of long-chain 3-hydroxy fatty acids (PubMed:18065749). Has little activity toward prostaglandins A1 and E1 (PubMed:7679927).
Cellular Location Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein
Tissue Location Expressed in liver (PubMed:7679927). Expressed in S2 and S3 segments of proximal tubules in cortex and outer medulla of kidney (PubMed:10660572, PubMed:7679927).
Research Areas

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

BACKGROUND

Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate, myristate and palmitate. Has little activity toward prostaglandins A1 and E1. Oxidizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE).

REFERENCES

Palmer C.N.A.,et al.Biochim. Biophys. Acta 1172:161-166(1993).
Kawashima H.,et al.J. Biochem. 116:74-80(1994).
Imaoka S.,et al.DNA Cell Biol. 12:893-899(1993).
Bellamine A.,et al.Arch. Biochem. Biophys. 409:221-227(2003).
Gregory S.G.,et al.Nature 441:315-321(2006).

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