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VPS26A belongs to a group of vacuolar protein sorting (VPS) genes. Additionally we are shipping Vacuolar Protein Sorting 26 Homolog A (S. Pombe) Antibodies (66) and and many more products for this protein.
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We investigated the modification of air pollution and diabetes association by a genetic risk score covering 63 T2D genes. Five single variants near GRB14 (show GRB14 Proteins), UBE2E2 (show UBE2E2 Proteins), PTPRD (show PTPRD Proteins), VPS26A and KCNQ1 (show KCNQ1 Proteins) showed nominally significant interactions with PM10 (P<0.05). Our results suggest that genetic risk for T2D may modify susceptibility to air pollution through alterations in insulin (show INS Proteins) sensitivity.
The retromer complex is a highly conserved membrane trafficking assembly composed of three proteins - Vps26, Vps29 (show VPS29 Proteins) and Vps35 (show vps35 Proteins), which are impaired in neurodegenerative diseases. (Review)
X-ray crystallographic analysis of a 4-component complex comprising the VPS26 & VPS35 (show vps35 Proteins) subunits of retromer, sorting nexin SNX3 (show SNX3 Proteins), & recycling signal from the divalent cation transporter DMT1 (show DMRT1 Proteins)-II; analysis identifies a binding site for canonical recycling signals at the interface between VPS26 & SNX3 (show SNX3 Proteins); shows cooperative interactions among the VPS subunits, SNX3 (show SNX3 Proteins) & cargo that couple signal-recognition to membrane recruitment.
Mutagenesis studies coupled with coimmunoprecipitations revealed that retromer-mediated trafficking requires the Env cytoplasmic tail that we show binds directly to retromer components Vps35 and Vps26.
provides molecular insights into the essential role of Vps26 and Vps35 (show vps35 Proteins) in Rab7 (show RAB7B Proteins)-mediated recruitment of the core retromer complex
This study demonstrated that Genetic variability of VPS26A in parkinsonism.
Mutations in VPS26A are not a frequent cause of Parkinson's disease.
VPS26A binding increases the affinity of the SNX27 PDZ domain for PDZ- binding motifs by an order of magnitude, revealing cooperativity in cargo selection.
Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function
Colocalization of Vps26 paralogues with different endosomally located Rab (show HRB Proteins) proteins shows prolonged association of Vps26B (show VPS26B Proteins)-retromer with maturing endosomes relative to Vps26A-retromer.
Vps26 is implicated in regulating Vps35p membrane association, therefore Vps26 plays a role in cargo recognition of the cytoplasmic coat retromer complex.
These results revealed that the retromer complex could be formed from different Vps26 isoforms in a tissue-specific manner.
This gene belongs to a group of vacuolar protein sorting (VPS) genes. The encoded protein is a component of a large multimeric complex, termed the retromer complex, involved in retrograde transport of proteins from endosomes to the trans-Golgi network. The close structural similarity between the yeast and human proteins that make up this complex suggests a similarity in function. Expression studies in yeast and mammalian cells indicate that this protein interacts directly with VPS35, which serves as the core of the retromer complex. Alternative splicing results in multiple transcript variants encoding different isoforms.
vacuolar protein sorting-associated protein 26A
, vesicle protein sorting 26A
, H beta 58
, h58 protein
, vacuole protein sorting 26
, vacuolar protein sorting 26 A
, vacuolar protein sorting 26 homolog A (S. pombe)
, vacuolar protein sorting-associated protein 26A-like
, vacuolar protein sorting 26
, vacuolar protein sorting homolog26
, Zea mouse H58 homolog1
, vacuolar protein sorting-associated protein 26A-A
, vesicle protein sorting 26A-A
, vacuolar protein sorting 26 homolog A
, Vesicle protein sorting 26A