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Human SERPINB2 Protein expressed in Wheat germ - ABIN1319612
Chung, Jorgensen, Tonry, Kashanchi, Bailey, Popov: Secreted Bacillus anthracis proteases target the host fibrinolytic system. in FEMS immunology and medical microbiology 2011
PAI-2 likely plays a key role in cardiovascular disease through multiple pathophysiologic processes including racial dependency, platelet clot (show TXNDC17 Proteins) initiation and propagation, oxidative stress, inflammation effects on HDL (show HSD11B1 Proteins) metabolism and coagulation
This study is the first to associate enhancer RNAs with SERPINB2 and is the first demonstration of acquisition of NELF binding by enhancer RNAs on chromatin.
This study establishes a novel role for SerpinB2 in the stromal compartment in pancreatic ductal adenocarcinoma invasion through regulation of stromal remodelling
The variant of PAI-2 gene was associated with coronary artery disease and recurrent coronary event risk in Chinese Han population, in Xinjiang.
SerpinB2 plays an important role in proteostas
a total of 500 ESCC cases and 500 matched controls in a Southwest China population were evaluated for six SNPs in the exons of three Serpin genes (SerpinB5 (show SERPINB5 Proteins), SerpinB2, and SerpinE1 (show SERPINE1 Proteins)).
PAI-2 was up-regulated in tensioned keloid fibroblasts and normal fibroblasts, but more so in keloid cells. Knockdown of PAI2 reduced cell proliferation in fibroblasts under tension.
Soluble guanylate cyclase activators might alleviate or reverse vascular remodeling in pulmonary hypertension through the up-regulation of PAI-2.
We found no association between allele frequency and risk of multiples sclerosis for any single nucleotide polymorphism investigated for serpinb2
A role for SERPINB2 in patients with head and neck squamous cell carcinoma.
The efficient and rapid formation of uPA:PAI-2 complexes was thus shown to be associated with specific and rapid internalisation of PAI-2, which could be localised within endosomes and lysosomes
Data suggest that the function of keratinocyte SerpinB2 is protection of the stratum corneum from proteolysis via inhibition of urokinase, thereby maintaining the integrity and barrier function of the stratum corneum, particularly during times of skin inflammation
PAI-2 is a novel regulator of venous thrombus resolution, which modulates several pathways involving both inflammatory and uPA (show PLAU Proteins) activity mechanisms, distinct from PAI-1 (show SERPINE1 Proteins)
SerpinB2 has previously been implicated as a mediator of DMBA/TPA (show PLAT Proteins)-induced skin carcinogenesis
The presence of SerpinB2 on the surface of MPs provides a physiological mechanism whereby cancer cell SerpinB2 can reach the extracellular milieu and access urokinase plasminogen (show PLG Proteins) activator (uPA (show PLAU Proteins)).
Brain metastatic cells from lung cancer and breast cancer express high levels of anti-plasminogen (show PLG Proteins) activator (PA) serpins, including neuroserpin (show SERPINI1 Proteins) and serpin B2, to prevent plasmin (show PLG Proteins) generation and its metastasis-suppressive effects.
C/EBP-beta mediates both constitutive and LPS-induced serpinB2 mRNA expression in mouse embryonic fibroblasts and inflammatory primary macrophages.
Depletion PAI-2 resulted in NLRP3- and ASC-dependent caspase-1 activation and IL-1beta secretion in macrophages upon Toll-like receptor 2 (TLR2) and TLR4 engagement.
SerpinB2 can be induced by lentiviral infection in vivo.
Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell- derived PAI-1.
, placental plasminogen activator inhibitor
, plasminogen activator inhibitor 2
, plasminogen activator inhibitor, type II (arginine-serpin)
, serine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 2
, serpin B2
, urokinase inhibitor
, serine proteinase inhibitor, clade B, member 2
, plasminogen activator inhibitor type 2
, plasminogen activator inhibitor, type 2 (arginine-serpin)
, serpin peptidase inhibitor, clade B (ovalbumin), member 2
, plasminogen activator inhibitor 2, macrophage
, plasminogen activator inhibitor, type II
, serine (or cysteine) proteinase inhibitor, clade B, member 2
, plasminogen activator inhibitor 2 type A
, serine (or cysteine) peptidase inhibitor, clade B, member 2
, plasminogen activator inhibitor-2
, serine/cysteine proteinase inhibitor, clade B (ovalbumin), member 2