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The protein encoded by CD93 is a cell-surface glycoprotein and type I membrane protein that was originally identified as a myeloid cell-specific marker. Additionally we are shipping CD93 Antibodies (103) and CD93 Kits (24) and many more products for this protein.
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The expression of cd93 was observed in pancreatic islets, and leaky vessels were apparent in cd93-deficient pancreases. We further demonstrated that stress-induced release of sCD93 is impaired by hyperglycemia. Study propose CD93 as an important component in glucometabolic regulation.
soluble EGF (show EGF Proteins)-like domain containing CD93 protein is a novel angiogenic factor (show VEGFA Proteins) acting on the endothelium
[review] CD93 regulates inflammation as demonstrated in a murine model of cerebral ischemia reperfusion-induced injury and peritonitis; recent data suggests that a soluble form of CD93 regulates the inflammatory function of monocytes/ macrophages.
these data suggest that cell-associated CD93 regulates leukocyte recruitment and complement activation during murine peritonitis.
we speculate that CD93-neuroprotection is mediated via suppression of the neuroinflammatory response through downregulation of CCL21 (show CCL21 Proteins).
Cd93 may be an autoimmune susceptibility gene residing within the Idd13 locus, which plays a role in regulating absolute numbers of CD4 (show CD4 Proteins)(+) NKT (show CTSL1 Proteins) cells.
Data demonstrate that inflammation triggers release of sCD93 in vivo, identify the inflammatory macrophage as a source of sCD93, and provide insight into the mechanism by which CD93 contributes to engulfment of apoptotic cells.
Impaired uptake of apoptotic cells in C1qRp-deficient mice indicates that the C1qRp receptor may contribute to the removal of dying cells in vivo.
CD93-deficient mice were unable to maintain antibody secretion and bone-marrow plasma-cell numbers, demonstrating that CD93 is important for the maintenance of plasma cells in bone marrow niches.
These data suggest that AA4.1 is a cell surface marker that can identify the earliest lymphohematopoietic progenitors in mouse development.
These findings identify novel protein interactions involving CLEC14A (show CLEC14A Proteins), CD93 and CD248 (show CD248 Proteins) with MMRN2 (show MMRN2 Proteins) as targetable components of vessel formation
CD93 and Other Plasma Cell Survival Factor Genes Associated with Measles-Specific Antibody Response after Vaccination
Soluble expression of disulfide-bonded C-type lectin like domain of human CD93 in the cytoplasm of Escherichia coli. The recombinant protein could alter LPS pro-inflammatory activity on THP1 cells.
Vascular CD93 expression is elevated in nasopharyngeal carcinoma and is correlated with T classification, N classification, distant metastasis, clinical stage and poor prognosis (all P < 0.05). In addition, overexpression of CD93 promoted angiogenesis in vitro.
both transmembrane and soluble CD93 are overexpressed in patients with neovascular Age-Related Macular Degeneration.
Elevated serum sCD93 levels reflected exacerbated status of allergic diseases, including CSU [chronic spontaneous urticaria ], AR[allergic rhinitis], and asthma. ICS (show DNAI1 Proteins) [inhaled corticosteroid] use significantly diminished serum sCD93 levels in steroid-naive patients with BA[Bronchial asthma]. This result may suggest sCD93 in serum as a therapeutic marker for allergic inflammation.
Data show that CD93 antigen proved to be phosphorylated on tyrosine 628 and 644 following cell adhesion on laminin through dystroglycan.
CD93 expression identifies a predominantly cycling, non-quiescent leukemia-initiating cell population in MLL (show MLL Proteins)-rearranged AML (show RUNX1 Proteins), providing opportunities for selective targeting and eradication of LSCs.
The T/T genotype of SNP rs2749817 of CD93 is associated with disseminated cancer.
CD93 is a key regulator of glioma angiogenesis and vascular function, acting via cytoskeletal rearrangements required for cell-cell and cell-matrix adhesion.
The protein encoded by this gene is a cell-surface glycoprotein and type I membrane protein that was originally identified as a myeloid cell-specific marker. The encoded protein was once thought to be a receptor for C1q, but now is thought to instead be involved in intercellular adhesion and in the clearance of apoptotic cells. The intracellular cytoplasmic tail of this protein has been found to interact with moesin, a protein known to play a role in linking transmembrane proteins to the cytoskeleton and in the remodelling of the cytoskeleton.
, cell surface antigen AA4
, complement component 1 q subcomponent receptor 1
, complement component 1, q subcomponent, receptor 1
, complement component C1q receptor
, lymphocyte antigen 68
, C1q receptor 1
, CD93 antigen
, matrix-remodeling-associated protein 4
, matrix-remodelling associated 4