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anti-Human Sortilin 1 Antibodies:
anti-Mouse (Murine) Sortilin 1 Antibodies:
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Human Polyclonal Sortilin 1 Primary Antibody for BR, FACS - ABIN5527582
Fauchais, Lalloué, Lise, Boumediene, Preudhomme, Vidal, Jauberteau: Role of endogenous brain-derived neurotrophic factor and sortilin in B cell survival. in Journal of immunology (Baltimore, Md. : 1950) 2008
Show all 4 Pubmed References
sortilin negatively regulates TGF-beta signaling by diverting trafficking of precursor proteins to the lysosome during transit through the biosynthetic pathway
A novel role of NTS in the development of Castration-resistant prostate cancer with Neuroendocrine differentiation (NED), and a possible strategy to prevent the onset of NED by targeting the NTS signaling pathway.
The disruption of Sortilin dimerization by mutations impairs efficient interferon-alpha secretion from cells. These results suggest the functional importance of Sortilin dimerization in cytokine trafficking.
Sortilin is significantly and independently associated with the presence of lower limb peripheral arterial disease in a statin-free diabetic population and it may be a promising marker for clinically significant atherosclerosis of the lower limbs.
The rs12740374 minor allele sequence enhances SORT1 expression in hepatocytes. CRISPR-Cas9 can be used in primary human hepatocytes ex vivo and locus-humanized mice in vivo to interrogate the function of noncoding regulatory regions.
show that sortilin forms homodimers with an intermolecular disulfide bond at the cysteine 783 (Cys(783)) residue, and because Cys(783) can be palmitoylated
The common variant rs12740374 associated with Lp(a) cholesterol is a quantitative trait locus for SORT1 which is independent of LDL cholesterol.
High SORT1 expression is associated with Neuroendocrine Tumors.
SORT1 is a genetic risk factor for frontotemporal dementia.
Most rotavirus strains require the cation-independent mannose-6-phosphate receptor, sortilin-1, and cathepsins to enter cells.
regulator of EGFR intracellular trafficking that promotes receptor internalization and limits signaling, which in turn impacts tumor growth
Results provide evidence that progranulin destabilizes sortilin via ubiquitination and lysosomal degradation to override the negative modulatory functions of sortilin thereby assuring the sustainable pro-tumorigenic actions of progranulin in castration-resistant prostate cancer.
we report that sortilin also plays a role in tau prion replication and may thus represent an exciting target for therapeutic intervention in tau-related diseases.
The SNP rs17646665, located in a non-coding region of the SORT1 gene, remained significantly associated with decreased risk of Alzheimer's disease after multiple testing (pc = 0.0061). In addition, other SNPs were found to be nominally associated with risk of Alzheimer's disease, as well as altered cognitive function and the CSF biomarker Abeta42, but these associations did not survive correction for multiple testing.
Sortilin was overexpressed in thyroid cancers compared with benign thyroid tissues
Authors provide evidence that Mn-induced exit of GPP130 from the trans-Golgi network (TGN) toward lysosomes is mediated by the sorting receptor sortilin interacting with the lumenal stem domain of GPP130.
increased plasma sSortilin levels may be associated with in vivo platelet activation and could be a risk factor for atherothrombosis
The longitudinal quantification of the serum sortilin-derived propeptide concentration could assist psychiatrists in the diagnosis of antidepressant response efficacy
Both circulating SORT1 and PCSK9 levels are elevated in coronary artery disease patients.
Soluble sortilin exists in cerebrospinal fluid (CSF) in ten-fold molar excess compared to progranulin and observed a highly significant positive correlation between soluble sortilin and progranulin levels in CSF but not in plasma. The carriers of the minor allele of SNP rs646776 in SORT1 encoding sortilin displayed significantly increased soluble sortilin and reduced progranulin specifically in plasma but not in CSF.
SORT1 single nucleotide polymorphism and it's association with LDL cholesterol level and risk of coronary heart disease in Pakistani population
Findings suggest a role of Sortilin (Sort1) in energy regulation and lipid homeostasis in female mice, which may be a potential therapeutic target for obesity and cardiovascular disease.
Study shows that retrograde signaling from progranulin to sort1 counteracts synapse elimination in the developing cerebellum.
The sortilin and SorCS2 are extensively present in several distinct anatomical areas in the developing nervous system and are rarely co-expressed.
this study revealed an important role of insulin signaling in regulating adipose Sort1 protein stability, and further suggests that impaired insulin signaling may underlie reduced adipose Sort1 in obesity.
Present crystal structures that show the sortilin luminal segment (s-sortilin) undergoes a conformational change and dimerizes at low pH. The conformational change, within all three sortilin luminal domains, provides an altered surface and the dimers sterically shield a large interface while bringing the two s-sortilin C-termini into close proximity.
Altogether, sortilin defines a pathway required for optimal intracellular mycobacteria control and lung inflammation in vivo.
findings provide insights into the posttranslational regulation of cytokine production through the posttranscriptional control of sortilin expression by TLR signals.
We showed that expression levels for NTS and NTSR1 varied, that NTSR2 expression was not detectable and that NTSR3 was consistently expressed in all CRC cell lines examined.
our findings indicate that sortilin is a beneficial protein for the reduction of amyloid pathology in APP/PS1 mice by promoting APP degradation
we identify interferon-gamma (IFN-gamma) as the key inflammatory mediator controlling sortilin-1 levels
Data suggest that sortilin expression in both gastrocnemius and extensor digitorum longus muscle is down-regulated by 17-18h of fasting/food deprivation; pathological levels of high blood glucose, as in streptozotocin-induced diabetes, do not alter sortilin expression in skeletal muscle; sortilin expression is elevated during differentiation of myocyte cell line or in presence of high concentration of glucose.
Shh and Sort1 can interact at the level of the Golgi and that Sort1 directs Shh away from the pathways that promote its secretion.
By contrast, treatment with dexamethasone, which also induced insulin resistance, was without effect on sortilin expression and PE production. As a putative bioactive peptide, we have evaluated its autocrine effect by the use of spadin on 3T3-L1 adipocytes by performing glucose uptake and signalling experiments. Any effect was measured on adipocytes indicating that the use of spadin as an antidepressant would have no side
Sortilin 1 (Sort1) knockout (KO) does not affect Western diet-induced obesity nor adipose fatty acid and ceramide concentrations.
sortilin regulates cholestatic liver damage and fibrosis via effects on both aSMase activity and serum IL-6.
This study demonstrated that Mice with Sort1 deficiency display normal cognition but elevated anxiety-like behavior.
TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor.
Sortilin is highly expressed in epithelial tissues of the developing lung, nasal cavity, kidney, pancreas and salivary gland.
Sortilin mediates vascular calcification via its recruitment into extracellular vesicles.
plays a role in innate immune processes and, thus, not in autoimmune neuroinflammation.
This gene encodes a protein that is a multi-ligand type-1 receptor with similarity to the yeast carboxypeptidase Y sorting receptor Vps10 protein. The encoded protein, a trans-Golgi network (TGN) transmembrane protein, binds a number of unrelated ligands that participate in a wide range of cellular processes\; however, it lacks the typical features of a signalling receptor. In the TGN, furin mediates the activation of the mature binding form. The encoded protein consists of a large luminal domain, a single transmembrane segment and short C-terminal cytoplasmic tail. The luminal domain contains a cysteine-rich region similar to two corresponding segments in the yeast Vps10p\; the cytoplasmic tail is similar to the corresponding segment of the cation-independent mannose 6-phosphate receptor and the tail also interacts with the VHS domains of GGA (Golgi-associated, gamma-adaptin homologous, ARF-interacting) proteins.
, 100 kDa NT receptor
, glycoprotein 95
, neurotensin receptor 3
, glycoprotein 110