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Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.. Additionally we are shipping TPST1 Antibodies (51) and many more products for this protein.
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Results demonstrate the importance of protein-tyrosine sulfation for proper development of the retina and suggest different phenotypes resulting from elimination of TPST-1 or -2 may reflect differential expression patterns or levels of the enzymes.
two genes identified in this analysis, PLEC1 and TPST1, reduced IL-6 (show IL6 Proteins) production by macrophages
Data show that Tpst1/Tpst2 (show TPST2 Proteins) DKO leukocytes bound less P-selectin (show SELP Proteins) than wild type leukocytes despite equivalent surface expression of Psgl-1 (show SELPLG Proteins).
These results indicate that protein-tyrosine sulfation by Tpst1/2 is essential for proper outer segment morphogenesis and synaptic function, but is not critical for overall retinal structure or synapse formation.
Tpst1 and Tpst2 (show TPST2 Proteins) are the only Tpst genes in mice, tyrosine sulfation is required for normal pulmonary function at birth, and TPST-2 (show TPST2 Proteins) is required for normal thyroid gland function.
TPST1 was significantly negatively correlated with the expression of cMet in lung cancer and may be a negative prognostic biomarker of lung cancer.
TPST1 rs3757417T>G polymorphisms are associated with colorectal cancer.
up-regulation of TPST-1 and tyrosine sulfation of CXCR4 (show CXCR4 Proteins) by LMP1 (show PDLIM7 Proteins) might be a potential mechanism contributing to nasopharyngeal carcinoma metastasis
Affinity purified salivary TPST showed a single band of 50-54 kDa and is the first report characterizing a tyrosylprotein sulfotransferase in secretory fluid from the parotid gland
results exclude TPST1 as the causative gene for Shwachman-Diamond syndrome
Shear stress-dependent downregulation of TPST1 in human endothelium involves protein kinase C
Tyrosine sulfation of CCR5 N-terminal peptide follows a discrete pattern and temporal sequence
Human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
The kinetic parameters of tyrosylprotein sulfotransferase-1 and -2, catalyzing tyrosine sulfation of CCR8 (show CCR8 Proteins) peptides, were determined using liquid chromatography electrospray ionisation mass spectrometry.
TPST1 and TPST2 (show TPST2 Proteins) provide an important posttranslational modification for vision.
Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.
tyrosylprotein sulfotransferase 1
, protein-tyrosine sulfotransferase 1-like
, tyrosylprotein sulfotransferase-1
, protein-tyrosine sulfotransferase 1
, transport and golgi organization 13 homolog A