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PHYH Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O14832 |
|---|---|
| Other Accession | Q9UJ83 |
| Clone Names | 90909094 |
| Gene ID | 5264 |
|---|---|
| Other Names | Phytanoyl-CoA dioxygenase, peroxisomal, Phytanic acid oxidase, Phytanoyl-CoA alpha-hydroxylase, PhyH, PHYH, PAHX |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8711a was selected from the N-term region of human PHYH. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | PHYH |
|---|---|
| Synonyms | PAHX |
| Function | Catalyzes the 2-hydroxylation of not only racemic phytanoyl- CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (PubMed:9326939, PubMed:10744784, PubMed:12031666, PubMed:12923223). Does not hydroxylate long and very long straight chain acyl-CoAs or 2- methyl- and 4-methyl-branched acyl-CoAs (PubMed:10744784, PubMed:12923223). |
| Cellular Location | Peroxisome. |
| Tissue Location | Expressed in liver, kidney, and T-cells, but not in spleen, brain, heart, lung and skeletal muscle |
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Provided below are standard protocols that you may find useful for product applications.
Background
PHYH2 catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.
References
Foulon,V., et.al., J. Biol. Chem. 280 (11), 9802-9812 (2005)Kikuchi,M., et.al., J. Biol. Chem. 279 (1), 421-428 (2004)
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