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anti-Rat (Rattus) TCIRG1 Antibodies:
anti-Mouse (Murine) TCIRG1 Antibodies:
anti-Human TCIRG1 Antibodies:
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Human Monoclonal TCIRG1 Primary Antibody for ELISA, WB - ABIN564479
Schulz, Dave, Stehberger, Chau, Wagner: Differential localization of vacuolar H+-ATPases containing a1, a2, a3, or a4 (ATP6V0A1-4) subunit isoforms along the nephron. in Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 2007
Show all 3 Pubmed References
Human Monoclonal TCIRG1 Primary Antibody for ELISA, WB - ABIN523715
Thudium, Moscatelli, Flores, Thomsen, Brüel, Gudmann, Hauge, Karsdal, Richter, Henriksen: A comparison of osteoclast-rich and osteoclast-poor osteopetrosis in adult mice sheds light on the role of the osteoclast in coupling bone resorption and bone formation. in Calcified tissue international 2014
Human Polyclonal TCIRG1 Primary Antibody for ICC, IF - ABIN4358111
Bronckers, Lyaruu, Bervoets, Medina, DenBesten, Richter, Everts: Murine ameloblasts are immunonegative for Tcirg1, the v-H-ATPase subunit essential for the osteoclast plasma proton pump. in Bone 2012
Here we show mice homozygous for R740S (R740S/R740S) of the Vacuolar-type H(+)-ATPases have more severe osteopetrosis (show CSF1 Antibodies) and die by postnatal day 14
Luteolin can be effective in reducing bone resorption and that this effect of luteolin may be through disruption of osteoclast V-ATPase a3-d2 interaction.
increased lysosomal pH in V ATPase a3 mutant mice osteoclasts leads to decreased NFATc1 (show NFATC1 Antibodies) signaling and nuclear translocation, resulting in a cell autonomous impairment of osteoclastogenesis in vitro.
These results demonstrate that adeno (show ADORA2A Antibodies)-associated virus-mediated Atp6i/TIRC7 knockdown in periapical tissues can inhibit endodontic disease development, bone resorption, and inflammation.
The N termini of a-subunit isoforms are involved in signaling between vacuolar H+-ATPase (show ATP6V1B2 Antibodies) (V-ATPase (show DNAH8 Antibodies)) and cytohesin-2 (show CYTH2 Antibodies)
we report for the first time on biological effects mediated by a peptide corresponding to the C-terminus of Tirc7 protein, which interfere with monocytic differentiation pathways.
Tcirg1, which is essential for osteoclasts to pump protons into the bone, is not appreciably expressed in maturation stage mouse ameloblasts.
ocular phenotype of mice deficient in Tcirg1 function
V-ATPase (show ATP6V1H Antibodies) localization and activity in kidney cells via direct PKA-dependent phosphorylation of the A subunit at Ser-175
RANKL (show TNFSF11 Antibodies) treatment releases the negative regulation of PARP-1 (show PARP1 Antibodies) on Tcirg1 gene expression during osteoclastogenesis
TIRC7 is involved in inflammation in multiple sclerosis and anti-TIRC7 mAb can prevent immune activation via selective inhibition of Th1 (show TH1L Antibodies)- and Th17-associated cytokine expression.
Since a3 subunit of V-ATPase (show ATP6V1H Antibodies) complex plays a crucial role in bone resorption process, structurally abnormal a3 subunit might have adversely affected bone resorption process, leading to infantile osteopetrosis (show CSF1 Antibodies) in Pakistani family.
TCIRG1 may be involved in endolysosomal transport-a process known to be important to development of early onset AD.
TCIRG1 gene mutation in a Chinese family is associated with infantile malignant osteopetrosis (show CSF1 Antibodies).
Nine rare missense variants at evolutionarily conserved sites in TCIRG1 are associated with lower absolute neutrophil count.
an intronic region in TCIRG1 that seems to be particularly prone to splicing mutations, allowing the production of a small amount of protein sufficient to reduce the severity of the phenotype usually associated with TCIRG1 defects.
TIRC7 might be involved in the pathogenesis of aplastic anemia.
An A to T transversion in the fourth base of the intron 2 donor splice site (c.117+4A-->T) in TCIRG1 in the Ashkenazi Jewish (AJ) population was found to be responsible for osteopetrosis (show CSF1 Antibodies).
TIRC7 might be associated with the pathogenesis of ITP (show ITPA Antibodies), and TIRC7 levels could be used as an indicator to evaluate patients' response to HD-DXM treatment.
Increased expression of TIRC7 in plasma was associated with the severity of acute graft-versus-host disease.
Through alternate splicing, this gene encodes two proteins with similarity to subunits of the vacuolar ATPase (V-ATPase) but the encoded proteins seem to have different functions. V-ATPase is a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, and receptor-mediated endocytosis. V-ATPase is comprised of a cytosolic V1 domain and a transmembrane V0 domain. Mutations in this gene are associated with infantile malignant osteopetrosis.
ATPase, H+ transporting, lysosomal V0 protein a
, T cell immune response cDNA7 protein
, T-cell, immune regulator 1, ATPase, H+ transporting, lysosomal V0 protein A3
, T-cell, immune regulator 1, ATPase, H+ transporting, lysosomal V0 protein a
, V-type proton ATPase 116 kDa subunit a
, V-type proton ATPase 116 kDa subunit a isoform 3
, osteoclastic proton pump
, v-ATPase 116-kDa
, v-H+ATPase subunit a3
, ATPase, H+ transporting, lysosomal I
, T-cell, immune regulator 1
, V-ATPase a3
, ATPase, H+ transporting, 116kD
, OC-116 kDa
, T-cell immune response cDNA 7
, V-ATPase 116-kDa
, osteoclastic proton pump 116 kDa subunit
, specific 116-kDa vacuolar proton pump subunit
, vacuolar proton translocating ATPase 116 kDa subunit A