|Application ||WB, E|
|Other Accession||Q9EPI0, Q9EPL0, NP_071450.2|
|Calculated MW||96767 Da|
|Antigen Region||29-58 aa|
|Other Names||Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2|
|Target/Specificity||This XYLT2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 29-58 amino acids from the N-terminal region of human XYLT2.|
|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||XYLT2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Probably catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes (By similarity). Its enzyme activity has not been demonstrated.|
|Cellular Location||Endoplasmic reticulum membrane; Single-pass type II membrane protein Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Widely expressed. Expressed at higher level in kidney and pancreas.|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene is an isoform of xylosyltransferase, which belongs to a family of glycosyltransferases. This enzyme transfers xylose from UDP-xylose to specific serine residues of the core protein and initiates the biosynthesis of glycosaminoglycan chains in proteoglycans including chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate. The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis.
Condac, E., et al. Glycobiology 19(8):829-833(2009)
Casanova, J.C., et al. Biochem. Biophys. Res. Commun. 383(1):4-10(2009)
Ponighaus, C., et al. Am. J. Hypertens. 22(4):432-436(2009)
Ambrosius, M., et al. Clin. Biochem. 42 (1-2), 1-4 (2009) :
Hendig, D., et al. Clin. Chim. Acta 398 (1-2), 90-94 (2008) :
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