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FADS2 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application 
| IF, IHC-P, WB, FC, E |
|---|---|
| Primary Accession | O95864 |
| Other Accession | Q4R749, NP_004256.1 |
| Reactivity | Human |
| Predicted | Monkey |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 52259 Da |
| Antigen Region | 79-108 aa |
| Gene ID | 9415 |
|---|---|
| Other Names | Fatty acid desaturase 2, 11419-, Delta(6) fatty acid desaturase, D6D, Delta(6) desaturase, Delta-6 desaturase, FADS2 |
| Target/Specificity | This FADS2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 79-108 amino acids from the N-terminal region of human FADS2. |
| Dilution | IF~~1:10~50 WB~~1:1000 IHC-P~~1:10~50 FC~~1:25 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | FADS2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | FADS2 (HGNC:3575) |
|---|---|
| Function | Involved in the biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors, acting as a fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 6 of the fatty acyl chain. Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively (PubMed:12713571). Subsequently, in the biosynthetic pathway of HUFA n- 3 series, it desaturates tetracosapentaenoate (24:5n-3) to tetracosahexaenoate (24:6n-3), which is then converted to docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system function (By similarity). Desaturates hexadecanate (palmitate) to produce 6Z-hexadecenoate (sapienate), a fatty acid unique to humans and major component of human sebum, that has been implicated in the development of acne and may have potent antibacterial activity (PubMed:12713571). It can also desaturate (11E)-octadecenoate (trans- vaccenoate, the predominant trans fatty acid in human milk) at carbon 6 generating (6Z,11E)-octadecadienoate (By similarity). In addition to Delta-6 activity, this enzyme exhibits Delta-8 activity with slight biases toward n-3 fatty acyl-CoA substrates (By similarity). |
| Cellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein |
| Tissue Location | Expressed in a wide array of tissues, highest expression is found in liver followed by brain, lung, heart, and retina. A lower level is found in breast tumor when compared with normal tissues; lowest levels were found in patients with poor prognostic index. |
Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene is a member of the fatty acid desaturase (FADS) gene family. Desaturase enzymes regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members FADS1 and FADS2 at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization.
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Mathias, R.A., et al. J. Lipid Res. 51(9):2766-2774(2010)
Lu, Y., et al. Am. J. Clin. Nutr. 92(1):258-265(2010)
Zabaneh, D., et al. PLoS ONE 5 (8), E11961 (2010) :
Steer, C.D., et al. PLoS ONE 5 (7), E11570 (2010) :
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