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The protein encoded by TPST2 catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. Additionally we are shipping TPST2 Antibodies (61) and TPST2 Kits (1) and many more products for this protein.
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cerebral abnormalities in grt/grt Tpst2 gene defect mice are characterized by cortical hypoplasia at the frontooccipital axis with immature pyramidal neurons and insufficient development of callosal fibers
Findings indicate that low body weight and salivary gland hypofunction in Tpst2-/- mice is due solely to primary hypothyroidism.
Results demonstrate the importance of protein-tyrosine sulfation for proper development of the retina and suggest different phenotypes resulting from elimination of TPST-1 (show TPST1 Proteins) or -2 may reflect differential expression patterns or levels of the enzymes.
Data show that Tpst1 (show TPST1 Proteins)/Tpst2 DKO leukocytes bound less P-selectin (show SELP Proteins) than wild type leukocytes despite equivalent surface expression of Psgl-1 (show SELPLG Proteins).
Lack of tyrosylprotein sulfotransferase-2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm.
These results indicate that protein-tyrosine sulfation by Tpst1 (show TPST1 Proteins)/2 is essential for proper outer segment morphogenesis and synaptic function, but is not critical for overall retinal structure or synapse formation.
demonstrated that the Tpst2 transgene rescues the mutant phenotypes both in vitro and in vivo
Considering that Tpst2 is the responsible gene of grt mice, mutation of which is associated with a poor function of TSH receptor (show TSHR Proteins), the findings raise the possibility of involvement of factors including Tpst2 in the insulin (show INS Proteins) hyposecretion in grt mice.
results demonstrate conclusively that TPST-1 (show TPST1 Proteins) and TPST-2 have distinct biological roels in vivo and document for the first time the critical importance of protein-tyrosine O-sulfation in male fertility
The growth-retarded (grt) mutation leads to a loss of TPST2 activity, and TPST2 isoform has a high degree of substrate preference for TSH receptor (TSHR (show TSHR Proteins)).
Using a quantum mechanics protocol of alanine scanning, the study identified unequivocally the role of the amino acids involved in the TPST-2 catalytic mechanism.
the first crystal structure of the human tyrosylprotein sulfotransferase isoform 2 complexed with a substrate peptide (C4P5Y3) derived from complement C4 and 3'-phosphoadenosine-5'-phosphate at 1.9 A resolution, is reported.
Shear stress-dependent upregulation of TPST2 in human endothelium is mediated by a tyrosine kinase (show TXK Proteins)-dependent pathway
Tyrosine sulfation of CCR5 N-terminal peptide follows a discrete pattern and temporal sequence
The kinetic parameters of tyrosylprotein sulfotransferase-1 (show TPST1 Proteins) and -2, catalyzing tyrosine sulfation of CCR8 (show CCR8 Proteins) peptides, were determined using liquid chromatography electrospray ionisation mass spectrometry.
The protein encoded by this gene catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The encoded protein is a type II integral membrane protein found in the Golgi body. Two transcript variants encoding the same protein have been found for this gene.
protein-tyrosine sulfotransferase 2
, tyrosylprotein sulfotransferase 2
, tyrosylprotein sulfotransferase-2
, transport and golgi organization 13 homolog B
, tyrosylprotein phosphotransferase 2