目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T1891 | MMP | ||
NSC 405020 是一种 MT1-MMP 的非催化抑制剂,可特异地靶向 MT1-MMP 的 PEX 结构域,不会抑制 MT1-MMP 和 MMP-2的催化活性。 | |||
T3894 | Apoptosis Others | ||
Polyphyllin II (Chonglou Saponin II) 是重楼中重要的一种皂苷,具有止血、祛痰、抑菌、抗细胞毒和抗孕杀精作用。它通过 caspases 激活和细胞周期停滞诱导细胞凋亡。 | |||
T3S0601 | Others | ||
Buddlejasaponin IVb (Saikosaponin 1b) 是一种三萜皂苷,从Clinopodium chinense (Benth.) O. Kuntze 中分离得到,能够缩短凝血时间,具有止血作用。 | |||
T6S2315 | Apoptosis Antibacterial Pyroptosis | ||
Polyphyllin VI 是一种活性皂甙,诱导 G2/M 细胞周期停滞并引发细胞凋亡,具有抗癌活性。它通过诱导非小细胞肺癌中的 ROS/NF-κB/NLRP3/GSDMD 信号轴来诱导 caspase-1 介导的细胞焦亡。 | |||
T6S2384 | Reductase | ||
Poliumoside 是从 Brandisia hancei 的茎和叶中分离出来的咖啡酰化的苯丙烷糖苷。Poliumoside 能够抑制晚期糖基化终产物的形成和大鼠晶状体醛糖还原酶,IC50分别为 19.69 和 8.47 μM。Poliumoside 具有抗炎和抗氧化特性。 | |||
T34279 | |||
Refortan, as hydroxyethyl starch, can be used in surgery for maintaining hemostasis in patients. | |||
T28128 | |||
Naftazone is a vasoprotectant drug used for hemostasis. Naftazone is shown to accelerate human saphenous vein endothelial cell proliferation in vitro at concentrations which did not alter the hemostatic balance. | |||
T82083 | |||
Idarucizumab 是一种专门中和口服直接凝血酶抑制剂(DOAC)效用的人源化单克隆抗体片段,是首个用于逆转DOAC抗凝作用的逆转剂(reversal agent),适用于恢复正常止血功能。 | |||
T82585 | Factor Xa | ||
Denecimig (Mim8) 是活化凝血因子VIII双特异性抗体,包含抗FIXa和抗FX臂,促进FX活化,实现体外及体内止血。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPY-01075 | Von Willebrand Factor/vWF Protein, Human, Recombinant (His) | Human | CHO | ||
Von Willebrand Factor (VWF) is a multimeric glycoprotein involved in hemostasis in blood, binds receptors on the surface of platelets and in connective tissue, thereby mediating the adhesion of platelets to sites of vascular injury. From studies it appears that VWF protein uncoils under these circumstances, decelerating passing platelets. VWF protein is deficient or defective in von Willebrand disease (VWD) and is involved in a large number of other diseases, including thrombosis, thrombotic thrombocytopenic purpura, Stroke, Heyde's syndrome, possibly hemolytic-uremic syndrome and so on.
|
|||||
TMPH-00346 | Limulus clotting factor C Protein, Carcinoscorpius rotundicauda, Recombinant (His) | Carcinoscorpius rotundicauda | E. coli | ||
This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of factor B.
|
|||||
TMPK-01271 | Coagulation factor XI Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Factor XI (FXI) is the zymogen of a plasma protease (FXIa) that contributes to hemostasis by activating factor IX (FIX). In the original cascade model of coagulation, FXI is converted to FXIa by factor XIIa (FXIIa), a component, along with prekallikrein and high-molecular-weight kininogen (HK), of the plasma kallikrein-kinin system (KKS).
|
|||||
TMPK-01190 | GPVI Protein, Human, Recombinant (His) | Human | HEK293 | ||
Although platelets are best known for their role in hemostasis, they are also crucial in development, host defense, inflammation, and tissue repair. Many of these roles are regulated by the immune-like receptors glycoprotein VI (GPVI) and C-type lectin receptor 2 (CLEC-2), which signal through an immunoreceptor tyrosine-based activation motif (ITAM). GPVI is activated by collagen in the subendothelial matrix, by fibrin and fibrinogen in the thrombus, and by a remarkable number of other ligands.
|
|||||
TMPK-01044 | VEGFC Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
the lymphangiogenic factors vascular endothelial growth factor C (VEGFC) and VEGFD are cleaved by thrombin and plasmin, serine proteases generated during hemostasis and wound healing. Genetic studies reveal that platelet enhancement of lymphatic growth after wounding is dependent on the release of VEGFC, but not VEGFD, a finding consistent with high expression of VEGFC in both platelets and avian thrombocytes.
|
|||||
TMPH-02974 | Von Willebrand Factor/vWF Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma.
|
|||||
TMPK-01043 | VEGFC Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
the lymphangiogenic factors vascular endothelial growth factor C (VEGFC) and VEGFD are cleaved by thrombin and plasmin, serine proteases generated during hemostasis and wound healing. Genetic studies reveal that platelet enhancement of lymphatic growth after wounding is dependent on the release of VEGFC, but not VEGFD, a finding consistent with high expression of VEGFC in both platelets and avian thrombocytes.
|
|||||
TMPJ-00786 | ITGB1 Protein, Human, Recombinant (aa 21-728, His) | Human | Human Cells | ||
Integrin β-1 (ITGB1) belongs to the integrin β chain family. Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. ITGB1 is an integrin unit associated with very late antigen receptors, which contains one VWFA domain. It is known to conjoin with α-3 subunit to create α3β1 complex that reacts to such molecules as netrin-1 and reelin.
|
|||||
TMPK-01302 | GPVI Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Although platelets are best known for their role in hemostasis, they are also crucial in development, host defense, inflammation, and tissue repair. Many of these roles are regulated by the immune-like receptors glycoprotein VI (GPVI) and C-type lectin receptor 2 (CLEC-2), which signal through an immunoreceptor tyrosine-based activation motif (ITAM). GPVI is activated by collagen in the subendothelial matrix, by fibrin and fibrinogen in the thrombus, and by a remarkable number of other ligands.
|
|||||
TMPH-01333 | Fibrinogen beta chain Protein, Human, Recombinant (His) | Human | E. coli | ||
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
|
|||||
TMPJ-00193 | TREML1 Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
Triggering Receptor Expressed on Myeloid Cells-Like Protein 1 (TREML1) is a single-pass type I membrane protein. TREML1 precursor contains a 15 amino acid signal peptide, a 147 amino acid extracellular domain with an Ig-like V-type (immunoglobulin-like) domain, and 128 amino acid cytoplasmic domain. It can be expressed exclusively in platelets and megakaryocytes (MKs). It is a cell surface receptor that may play a role in the innate and adaptive immune response. TREML1 Sequestered in cytoplasmic vesicles in resting platelets. TREML1 be transported to the cell surface after stimulation by thrombin. Soluble fragments can be released into the serum by proteolysis. The phosphorylated TREML1 can interact with PTPN6 and PTPN11. TREML1 may participate in maintaining vascular hemostasis and regulating coagulation and inflammation at sites of injury.
|
|||||
TMPY-01484 | THSD1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Thrombospondin type-1 domain-containing protein 1, also known as transmembrane molecule with thrombospondin module, THSD1 and TMTSP, is a single-pass type I membrane protein that contains one TSP type-1 domain. THSD1 is a multi-domain, multi-functional glycoprotein synthesized by many cells. Matricellular THSD1 modulates cell adhesion and proliferation. It is involved in angiogenesis, inflammation, wound healing and cancer. In vitro, nanomolar concentrations of Thrombospondin-1 are required to alter endothelial and vascular smooth muscle cell adhesion, proliferation, motility, and survival. As a major platelet protein, for a long time it was postulated to control hemostasis via platelet aggregate stabilization. THSD1 is a potent angiogenesis inhibitor, and down-regulation of THSD1 has been suggested to alter tumor growth by modulating angiogenesis in a variety of tumor types.
|
|||||
TMPY-00121 | Vitronectin Protein, Human, Recombinant (His) | Human | HEK293 | ||
Vitronectin, also known as VTN, is a member of the pexin family. It is an abundant glycoprotein found in serum the extracellular matrix and promotes cell adhesion and spreading. Vitronectin is a secreted protein and exists in either a single chain form or a cleaved, two chain form held together by a disulfide bond. Vitronectin is a plasma glycoprotein implicated as a regulator of diverse physiological process, including blood coagulation, fibrinolysis, pericellular proteolysis, complement dependent immune responses, and cell attachment and spreading. Because of its ability to bind platelet glycoproteins and mediate platelet adhesion and aggregation at sites of vascular injury, vitronectin has become an important mediator in the pathogenesis of coronary atherosclerosis. As a multifunctional protein with a multiple binding domain, Vitronectin interacts with a variety of plasma and cell proteins. Vitronectin binds multiple ligands, including the soluble vitronectin receptor. It may be an independent predictor of adverse cardiovascular outcomes following acute stenting. Accordingly, Vitronectin is suggested to be involved in hemostasis, cell migration, as well as tumor malignancy.
|
|||||
TMPY-01861 | Vitronectin Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Vitronectin, also known as VTN, is a member of the pexin family. It is an abundant glycoprotein found in serum the extracellular matrix and promotes cell adhesion and spreading. Vitronectin is a secreted protein and exists in either a single chain form or a cleaved, two chain form held together by a disulfide bond. Vitronectin is a plasma glycoprotein implicated as a regulator of diverse physiological process, including blood coagulation, fibrinolysis, pericellular proteolysis, complement dependent immune responses, and cell attachment and spreading. Because of its ability to bind platelet glycoproteins and mediate platelet adhesion and aggregation at sites of vascular injury, vitronectin has become an important mediator in the pathogenesis of coronary atherosclerosis. As a multifunctional protein with a multiple binding domain, Vitronectin interacts with a variety of plasma and cell proteins. Vitronectin binds multiple ligands, including the soluble vitronectin receptor. It may be an independent predictor of adverse cardiovascular outcomes following acute stenting. Accordingly, Vitronectin is suggested to be involved in hemostasis, cell migration, as well as tumor malignancy.
|
|||||
TMPY-04996 | Coagulation Factor II Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Coagulation Factor II Protein (FII, F2 Protein or Prothrombin) is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. Coagulation Factor II Protein (FII, F2 Protein) also plays a role in maintaining vascular integrity during development and postnatal life. Prothrombin / Coagulation Factor II is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin / Coagulation Factor II and factor Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin. Prothrombin / Coagulation Factor II is expressed by the liver and secreted in plasma. Defects in prothrombin / Coagulation Factor II are the cause of factor II deficiency (FA2D). It is very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. Defects in Coagulation Factor II are also a cause of susceptibility to thrombosis. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation.
|
|||||
TMPY-01791 | Coagulation Factor II Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Coagulation Factor II Protein (FII, F2 Protein or Prothrombin) is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. Coagulation Factor II Protein (FII, F2 Protein) also plays a role in maintaining vascular integrity during development and postnatal life. Prothrombin / Coagulation Factor II is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin / Coagulation Factor II and factor Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin. Prothrombin / Coagulation Factor II is expressed by the liver and secreted in plasma. Defects in prothrombin / Coagulation Factor II are the cause of factor II deficiency (FA2D). It is very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. Defects in Coagulation Factor II are also a cause of susceptibility to thrombosis. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation.
|
|||||
TMPY-01840 | TLT-1/TREML1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Trem-like transcript 1 protein, also known as Triggering receptor expressed on myeloid cells-like protein 1, TREML1 and TLT-1, is a cytoplasm and single-pass type I membrane protein. TREML1 / TLT-1 is expressed exclusively in platelets and megakaryocytes (MKs) and that its expression is up-regulated dramatically upon platelet activation. It is a receptor that may play a role in the innate and adaptive immune response. TREML1 / TLT-1 contains the characteristic single V-set immunoglobulin (Ig) domain, its longer cytoplasmic tail is composed of both a proline-rich region and an immune receptor tyrosine-based inhibitory motif, the latter known to be used for interactions with protein tyrosine phosphatases. The triggering receptors expressed on myeloid cells (TREMs) have drawn considerable attention due to their ability to activate multiple cell types within the innate immune system, including neutrophils, monocyte / macrophages, and dendritic cells, via their association with DAP12. TREML1 / TLT-1 is prepackaged, along with CD62P, into both MK and platelet alpha-granules. Differences in thrombin-induced redistribution of CD62P and TREML1 indicate that TREML1 is not simply cargo of alpha-granules but may instead regulate granule construction or dispersal. TREML1 / TLT-1 does not function to inhibit members of the TREM family but instead may play a role in maintaining vascular hemostasis and regulating coagulation and inflammation at sites of injury.
|