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alpha2AP has a profibrotic effect probably not by the action as a plasmin (zeige PLG Antikörper) inhibitor, and the blocking of alpha2AP exerts an antifibrotic effect in humans and mice with systemic sclerosis
Alpha 2 antiplasmin is involved in the recruitment of lymphocytes in the peripheral tissues.Alpha 2 antiplasmin contributes to the maintenance of immunological functions that are related to IgE.
Plasmin (zeige PLG Antikörper)/alpha(2)-AP system played an important role in hepatic repair via clearance from the injury area.
PgtE mediated degradation of the antiprotease alpha(2)-antiplasmin (zeige Alpha2 Antiplasmin Antikörper) leads to functional inactivation of the antiprotease in infected macrophages
alpha2-antiplasmin induction inhibits E-cadherin (zeige CDH1 Antikörper) processing mediated by the plasminogen (zeige PLG Antikörper) activator/plasmin (zeige PLG Antikörper) system, leading to suppression of progression of oral squamous cell carcinoma via upregulation of cell-cell adhesion
The lack of alpha2AP attenuated TGF-beta(1 (zeige TGFB1 Antikörper)) synthesis, thereby resulting in attenuated fibrosis
2.65A X-ray crystal structure of an N-terminal truncated murine alpha(2)-antiplasmin (zeige Alpha2 Antiplasmin Antikörper).
Results show that alpha2-antiplasmin is a critical regulator for vascular remodeling by inhibiting p53 (zeige TP53 Antikörper)/p21 (zeige D4S234E Antikörper) pathway.
Data suggest that protein aggregates interact with tissue-type plasminogen activator (zeige PLAT Antikörper) and plasminogen (zeige PLG Antikörper) to efficiently generate plasmin (zeige PLG Antikörper); this aggregate-bound plasmin (zeige PLG Antikörper) is shielded from inhibition by alpha-2-antiplasmin (zeige Alpha2 Antiplasmin Antikörper) and degrades protein aggregates to release smaller, soluble but relatively hydrophobic peptide fragments; these fragments bind to and are cytotoxic to microglia (by not vascular endothelial cells).
Higher plasma concentrations of a-2-AP and PAI-1 (zeige SERPINE1 Antikörper) in patients with OSA indicated that these patients had increased prothrombotic activity. OSA increases the risk of cardiovascular complications as it enhances prothrombotic activity.
Possession of the alpha2AP 407Lys allele was negatively associated with AAA (zeige APP Antikörper), and thus changes in alpha2AP may affect aneurysm growth and development.
Two differentially expressed proteins, alpha-1-antitrypsin (SERPINA1 (zeige SERPINA1 Antikörper)) and alpha-2 antiplasmin (SERPINF2 (zeige Alpha2 Antiplasmin Antikörper)) are associated with purpura fulminans.
Data suggest serum A2AP (SERPINF2) level can serve as biomarker for diabetic retinopathy; levels of A2AP (but not fibrinogen, plasminogen (zeige PLG Antikörper), or plasminogen activator inhibitor 1 (zeige SERPINE1 Antikörper)) are up-regulated in hyperglycemic type 1 diabetes with retinopathy.
Study revealed that plasmin (zeige PLG Antikörper) was present in tumor tissue, and that it was responsible for processing progalanin to galanin (zeige GAL Antikörper)(1-20) in the extracellular environment.
Data suggest that decreased amounts of alpha2-plasmin (zeige PLG Antikörper) inhibitor in plasma vs serum ex vivo may reflect reduced factor XIII (zeige UGDH Antikörper) (FXIII) in vivo; thus, plasma vs serum alpha2-plasmin (zeige PLG Antikörper) inhibitor may be useful diagnostic marker for severe FXIII deficiency.
When the C terminus of alpha(2)-antiplasmin (zeige Alpha2 Antiplasmin Antikörper) was removed, the binding affinity for active site-blocked plasmin (zeige PLG Antikörper) remained high, suggesting additional exosite interactions between the serpin core and plasmin (zeige PLG Antikörper).
Truncation of monocyte chemoattractant protein 1 (zeige CCL2 Antikörper) by plasmin (zeige PLG Antikörper) promotes blood-brain barrier disruption.
This gene encodes a member of the serpin family of serine protease inhibitors. The protein is a major inhibitor of plasmin, which degrades fibrin and various other proteins. Consequently, the proper function of this gene has a major role in regulating the blood clotting pathway. Mutations in this gene result in alpha-2-plasmin inhibitor deficiency, which is characterized by severe hemorrhagic diathesis. Multiple transcript variants encoding different isoforms have been found for this gene.
alpha 2 antiplasmin
, alpha-2-plasmin inhibitor
, pigment epithelium derived factor
, plasmin inhibitor alpha 2
, serine (or cysteine) proteinase inhibitor, clade F, member 2
, serpin F2
, serine (or cysteine) peptidase inhibitor, clade F, member 2
, serpin peptidase inhibitor, clade F , member 2, like
, serine (or cysteine) proteinase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2
, alpha-2-PI serine protease inhibitor