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The antibody against SLC27A2 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 290-573 of human FATP2 (NP_003636.2) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, IHC-P, IF/ICC, ELISA.
The antibody against SLC27A2 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 290-573 of human FATP2 (NP_003636.2) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, IHC-P, IF/ICC, ELISA.
| Cat.No | ADA-09119A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | SLC27A2 |
| Target Synonyms | VLCS; FATP2; VLACS; ACSVL1; FACVL1; hFACVL1; HsT17226; SLC27A2 | Form | Liquid |
| Species Reactivity | Human, Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.05% proclin300, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | Mouse kidney, Mouse liver, Rat kidney, Rat liver | Application | ELISA, WB, IF/ICC, IHC-P |
| Immunogen Description | Recombinant fusion protein containing a sequence corresponding to amino acids 290-573 of human FATP2 (NP_003636.2). | Target Species | Human |
|---|---|---|---|
| Uniprot ID | O14975 | Immunogen Sequence |
Uniprot Id
O14975
Target Species
Human
Target Name
SLC27A2
Target Full Name
Long-chain fatty acid transport protein 2
Target Function
Acyl CoA synthetase that activates long-chain and very long-chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl-CoA. Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid. Does not activate C24 bile acids, cholate and chenodeoxycholate. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Exhibits long-chain fatty acids (LCFA) transport activity and plays an important role in hepatic fatty acid uptake.; Exhibits both long-chain fatty acids (LCFA) transport activity and acyl CoA synthetase towards very long-chain fatty acids. Shows a preference for generating CoA derivatives of n-3 fatty acids, which are preferentially trafficked into phosphatidylinositol.; Exhibits long-chain fatty acids (LCFA) transport activity but lacks acyl CoA synthetase towards very long-chain fatty acids.
Target Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein. Peroxisome membrane; Peripheral membrane protein. Cell membrane; Multi-pass membrane protein. Microsome.
Target Protein Families
ATP-dependent AMP-binding enzyme family
Target Tissue Specificity
Expressed in liver, kidney, placenta and pancreas.
Target Research Area
Metabolism
Target Synonyms
ACSVL1; FACVL1; FATP 2; FATP-2; FATP2; Fatty acid coenzyme A ligase, very long chain 1; Fatty acid transport protein 2; Fatty-acid-coenzyme A ligase; hFACVL1; HsT17226; Long chain fatty acid CoA ligase; Long-chain-fatty-acid--CoA ligase; S27A2_HUMAN; Slc27a2; Solute carrier family 27 (fatty acid transporter), member 2; Solute carrier family 27 member 2; THCA CoA ligase; THCA-CoA ligase; Very long chain acyl CoA synthetase; Very long chain fatty acid CoA ligase; Very long chain fatty acid coenzyme A ligase 1; very long-chain 1; Very long-chain acyl-CoA synthetase; Very long-chain-fatty-acid-CoA ligase; VLACS; VLCS
Target Background
The protein encoded by this gene is an isozyme of long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme activates long-chain, branched-chain and very-long-chain fatty acids containing 22 or more carbons to their CoA derivatives. It is expressed primarily in liver and kidney, and is present in both endoplasmic reticulum and peroxisomes, but not in mitochondria. Its decreased peroxisomal enzyme activity is in part responsible for the biochemical pathology in X-linked adrenoleukodystrophy. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
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