|Application ||WB, E|
|Other Accession||NP_861441, 222418631|
|Calculated MW||Predicted: 53 kDa |
Observed: 52 kDa
|Application Notes||SLC36A2 antibody can be used for detection of SLC36A2 by Western blot at 1 - 2 µg/ml.|
|Target/Specificity||SLC36A2; SLC36A2 antibody is human specific. SLC36A2 is predicted to not cross-react with other members of the SLC36 protein family.|
|Reconstitution & Storage||SLC36A2 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||SLC36A2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in a pH-dependent electrogenic neuronal transport and sequestration of small amino acids. Transports glycine and proline. Inhibited by sarcosine (By similarity).|
|Cellular Location||Cell membrane; Multi-pass membrane protein. Cytoplasm|
|Tissue Location||Abundantly expressed in kidney and muscle. Expressed in the S1 segment of the proximal tubule close to the glomerulus.|
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Provided below are standard protocols that you may find useful for product applications.
SLC36A2 is a pH-dependent proton-coupled amino acid transporter that belongs to the amino acid auxin permease 1 protein family. The encoded protein primarily transports small amino acids such as glycine, alanine and proline (1,2). Both SLC36A2 and its paralog SLC36A1 are expressed in neurons, but SLC36A2 localizes to the endoplasmic reticulum and recycling endosome, while SLC36A1 is expressed in the lysosome (2). SLC36A2 is thought to contribute to neuronal transport and sequestration of amino acids such as glycine, alanine, and proline (2). Mutations in this gene are associated with iminoglycinuria and hyperglycinuria (3).
Boll M, Foltz M, Rubio-Aliaga I, et al. Functional characterization of two novel mammalian electrogenic proton-dependent amino acid cotransporters. J. Biol. Chem. 2002; 277:22966-73.
Rubio-Aliaga I, Boll M, Vogt Weisenhorn DM, et al. The proton/amino acid cotransporter PAT2 is expressed in neurons with a different subcellular localization than its paralog PAT1. J. Biol. Chem. 2004; 279:2754-60.
Broer S, Bailey CG, Kowalczuk S, et al. Iminoglycinuria and hyperglycinuria are discrete human phenotypes resulting from complex mutations in proline and glycine transporters. J. Clin. Invest. 2008; 118:3881-92.
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