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TMEM165 encodes a predicted transmembrane protein with a perinuclear Golgi-like distribution in fibroblasts. Additionally we are shipping and many more products for this protein.
Showing 10 out of 17 products:
Human Polyclonal TMEM165 Primary Antibody for ICC, IF - ABIN4360614
Foulquier, Amyere, Jaeken, Zeevaert, Schollen, Race, Bammens, Morelle, Rosnoblet, Legrand, Demaegd, Buist, Cheillan, Guffon, Morsomme, Annaert, Freeze, Van Schaftingen, Vikkula, Matthijs: TMEM165 deficiency causes a congenital disorder of glycosylation. in American journal of human genetics 2012
Decreased expression of several markers of cartilage and bone development suggests that Tmem165 deficiency alters both chondrocyte and osteoblast differentiation.
This manuscript is a review of the current state of knowledge on TMEM165 deficiencies in Congenital Disorders of Glycosylation as well as new data on function of TMEM165 and some speculative models on TMEM165/Golgi functions are discussed.
Study not only provides novel insights into the molecular causes of glycosylation defects observed in TMEM165-deficient cells but also suggests that TMEM165 is a key determinant for the regulation of Golgi Mn(2+) homeostasis.
Antisense oligonucleotide-mediated pseudoexon skipping used in a Golgi-resident protein, a promising treatment option for a specific TMEM165-congenital disorders of glycosylation.
Congenital Disorders of Glycosylation disease-causing mutations of TMEM165 changes subcellular localization of the protein.
Defects in TMEM165 affect both Ca2 (show CA2 Antibodies)+ and pH homeostasis.
we identified TMEM165 (also named TPARL) as a gene involved in congenital disorders of glycosylation (CDG).
The timing, magnitude of TMEM165 expression and its Golgi location supports a role for this Golgi Ca2 (show CA2 Antibodies)+/H+ antiporter as a contributor to mammary Golgi calcium transport needs, in addition to the better-characterized roles of SPCA1 (show ATP2C1 Antibodies) and 2.
This gene encodes a predicted transmembrane protein with a perinuclear Golgi-like distribution in fibroblasts. Mutations in this gene are associated with the autosomal recessive disorder congenital disorder of glycosylation, type IIk. Knockdown of this gene's expression causes decreased sialylation in HEK cells and suggests this gene plays a role in terminal Golgi glycosylation. Alternative splicing results in multiple transcript variants.
TPA regulated locus
, transmembrane protein 165
, transmembrane protein PT27
, transmembrane protein TPARL
, TPA-regulated locus protein
, transmembrane protein 164
, transmembrane protein PFT27