|Application ||WB, IHC, E|
|Other Accession||NP_060488, 18482385|
|Calculated MW||Predicted: 60 kDa; Observed: 60 kDa|
|Application Notes||SLC38A4 antibody can be used for the detection of SLC38A4 by Western blot at 1 - 2 µg/mL. Antibody can also be used for immunohistochemistry starting at 2.5 µg/mL.|
|Target/Specificity||SLC38A4; SLC38A4 antibody is human and mouse reactive. SLC38A4 will not cross-react with other members of the SLC38 protein family.|
|Reconstitution & Storage||SLC38A4 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||SLC38A4 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||ATA3, NAT3, SNAT4|
|Function||Sodium-dependent amino acid transporter. Mediates electrogenic symport of neutral amino acids and sodium ions. Has a broad specificity, with a preference for Ala, followed by His, Cys, Asn, Ser, Gly, Val, Thr, Gln and Met. May mediate sodium- independent transport of cationic amino acids, such as Arg and Lys. Amino acid uptake is pH-dependent, with low transport activities at pH 6.5, intermediate at pH 7.0 and highest between pH 7.5 and 8.5.|
|Cellular Location||Cell membrane; Multi-pass membrane protein|
|Tissue Location||Detected in embryonic and adult liver, and at lower levels in adult muscle, kidney and pancreas. Detected in placenta syncytiotrophoblasts throughout gestation. Detected in fetal blood vessels.|
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Provided below are standard protocols that you may find useful for product applications.
SLC38A4 is found predominantly in liver and transports both cationic and neutral amino acids (1,2). The transport of cationic amino acids by SLC38A4 is sodium and pH independent, while the transport of neutral amino acids is sodium and pH dependent (2). Recent evidence suggests that SLC38A4 functions as a regulator of protein synthesis downstream of the hepatocyte nuclear factor 4a during liver development (3). It has also been suggested that SLC38A4 has ATPase activity and is critically involved in the maintenance of mitochondrial homeostasis and cell survival (4).
Sugawara M, Nakanishi T, Fei YJ, et al. Structure and function of ATA3, a new subtype of amino acid transport system A, primarily expressed in the liver and skeletal system. Biochim. Biophys. Acta 2000; 1509:7-13.
Hatanaka T, Huang W, Ling R, et al. Evidence for the transport of neutral as well as cationic amino acids by ATA3, a novel and liver-specific subtype of amino acid transport system A. Biochim. Biophys. Acta 2001 1510:10-7.
Kondou H, Kawai M, Tachikawa K, et al. Sodium-coupled neutral amino acid transporter 4 functions as a regulator of protein synthesis during liver development. Hepatol. Res. 2013; 43:1211-23.
Yang X, Yang J, Li L, et al. PAAT, a novel ATPase and trans-regulator of mitochondrial ABC transporters, is critically involved in the maintenance of mitochondrial homeostasis. FASEB J. 2014; 28:4821-34.
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