目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T75585 | |||
Naja Mossambica Venom (Mozambique Spitting Cobra Venom) 是一种蛇毒,可从 Naja Mossambica 获得。Naja Pallida Venom 对Candida 物种具有抗真菌活性。Naja Mossambica Venom 提取物 (如磷脂酶 A2) 可抑制钠钾 ATP 酶活性。 | |||
T80487 | GABA Receptor | ||
MmTx2 toxin作为一种GABAA受体调节剂,具有提升GABAA受体对激动剂反应敏感性的作用。该毒素来源于珊瑚蛇的毒液,并在神经系统相关疾病(例如癫痫、精神分裂症及慢性疼痛)的研究中发挥重要用途。 | |||
T75589 | |||
Bitis Cornuta Venom (Many-horned Adder Venom) 是从 Bitis Cornuta 提取的蛇毒,含有sPLA2毒素,该毒素具有通过抑制凝血酶原复合物以发挥抗凝活性的能力,并能促使凝血酶原转化为凝血酶,引发凝块形成。 | |||
T36295 | |||
Echistatin TFA, the smallest active RGD protein belonging to the family of disintegrins that are derived from snake venoms, is a potent inhibitor of platelet aggregation. Echistatin is a potent inhibitor of bone resorption in culture. Echistatin is a potent antagonist of αIIbβ3, αvβ3 and α5β1[1][2][3][4]. [1]. J Musial, et al. Inhibition of platelet adhesion to surfaces of extracorporeal circuits by disintegrins. RGD-containing peptides from viper venoms. Circulation. 1990 Jul;82(1):261-73.[2]. M Sato, et al. Echistatin is a potent inhibitor of bone resorption in culture. J Cell Biol. 1990 Oct;111(4):1713-23.[3]. C C Kumar, et al. Biochemical characterization of the binding of echistatin to integrin alphavbeta3 receptor. J Pharmacol Exp Ther. 1997 Nov;283(2):843-53.[4]. I Wierzbicka-Patynowski, et al. Structural requirements of echistatin for the recognition of alpha(v)beta(3) and alpha(5)beta(1) integrins. J Biol Chem. 1999 Dec 31;274(53):37809-14. | |||
T37832 | |||
CAY10761 is an inhibitor of ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1; IC50s = 467 and 429 μM for the human and snake venom enzymes, respectively).1,2 It also inhibits mushroom tyrosinase (Ki = 1.9 μM) and urease from jack bean, P. mirabilis, and B. pasteurii (IC50s = 0.093, <0.125, and 0.089 mM, respectively, at pH 8.2).3,4 |1. Khan, K.M., Fatima, N., Rasheed, M., et al. 1,3,4-Oxadiazole-2(3H)-thione and its analogues: A new class of non-competitive nucleotide pyrophosphatases/phosphodiesterases 1 inhibitors. Bioorg. Med. Chem. 17(22), 7816-7822 (2009).|2. Onyedibe, K.I., Wang, M., and Sintim, H.O. ENPP1, an old enzyme with new functions, and small molecule inhibitors - A STING in the tale of ENPP1. Molecules 24(22), E4192 (2019).|3. Ghani, U., and Ullah, N. New potent inhibitors of tyrosinase: Novel clues to binding of 1,3,4-thiadiazole-2(3H)-thiones, 1,3,4-oxadiazole-2(3H)-thiones, 4-amino-1,2,4-triazole-5(4H)-thiones, and substituted hydrazides to the dicopper active site. Bioorg. Med. Chem. 18(11), 4042-4048 (2010).|4. Amtul, Z., Rasheed, M., Choudhary, M.I., et al. Kinetics of novel competitive inhibitors of urease enzymes by a focused library of oxadiazoles/thiadiazoles and triazoles. Biochem. Biophys. Res. Commun. 319(3), 1053-1063 (2004). |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPY-00586 | CLEC-2 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
CLEC1B, also known as CLEC2, is a C-type lectin-like receptor expressed in myeloid cells and NK cells. Natural killer (NK) cells express multiple calcium-dependent (C-type) lectin-like receptors, such as CD94 and NKG2D, that interact with major histocompatibility complex class I molecules and either inhibit or activate cytotoxicity and cytokine secretion. CLEC2 acts as a receptor for the platelet-aggregating snake venom protein rhodocytin. Rhodocytin binding leads to tyrosine phosphorylation and this promotes the binding of spleen tyrosine kinase (Syk) and initiation of downstream tyrosine phosphorylation events and activation of PLC-gamma-2. CLEC2 contains 1 C-type lectin domain and is expressed preferentially in the liver. It acts as an attachment factor for human immunodeficiency virus type 1 (HIV-1) and facilitates its capture by platelets.
|
|||||
TMPH-00215 | SVTLE Protein, Bothrops jararaca, Recombinant (His & Myc) | Bothrops jararaca | E. coli | ||
Thrombin-like snake venom serine protease that clots fibrinogen by releasing fibrinopeptide A from the alpha chain of fibrinogen (FGA), induces platelet aggregation through its interaction with GPIb (GP1BA/GP1BB), and activates factor VIII (F8).
|
|||||
TMPH-00768 | SVTLE Protein, Gloydius ussuriensis, Recombinant (His & Myc) | Gloydius ussuriensis | E. coli | ||
Thrombin-like snake venom serine protease. Has a coagulant activity. Acts on alpha-chains of fibrinogen (FGA) generating fibrinopeptide A.
|
|||||
TMPH-00038 | Thrombin-like enzyme contortrixobin Protein, Agkistrodon contortrix, Recombinant (His & Myc) | Agkistrodon contortrix | E. coli | ||
Thrombin-like snake venom serine protease that cleaves beta chain of fibrinogen (FGB), releasing fibrinopeptide B. Has a coagulant activity activating blood coagulation factors V (F5) and XIII (F13A1).
|
|||||
TMPY-03877 | ADAM8/CD156a Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
ADAM8, also known as CD156, is a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. ADAM8 is possiblely involved in extravasation of leukocytes As a metalloprotease, ADAM8 also may be involved in cell adhesion during neurodegeneration, and it is thought to be a target for allergic respiratory diseases, including asthma.
|
|||||
TMPY-05532 | ADAM8/CD156a Protein, Human, Recombinant (His) | Human | HEK293 | ||
ADAM8, also known as CD156, is a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. ADAM8 is possiblely involved in extravasation of leukocytes As a metalloprotease, ADAM8 also may be involved in cell adhesion during neurodegeneration, and it is thought to be a target for allergic respiratory diseases, including asthma.
|
|||||
TMPY-02162 | Phospholipase A2 IIE/PLA2G2E Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Group IIE secretory phospholipase A2, also known as GIIE sPLA2, sPLA2-IIE, Phosphatidylcholine 2-acylhydrolase 2E and PLA2G2E is a secreted protein that belongs to the phospholipase A2 family. Mammalian secretory phospholipase A2s (sPLA2s) form a family of structurally related enzymes that are involved in a variety of physiological and pathological processes via the release of arachidonic acid from membrane phospholipids or the binding to specific membrane receptors. Phospholipases A2 / PLA2 are enzymes that release fatty acids from the second carbon group of glycerol. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Phospholipases A2 / PLA2 are commonly found in mammalian tissues as well as insect and snake venom. Venom from both snakes and insects is largely composed of melittin, which is a stimulant of Phospholipases A2 / PLA2. Due to the increased presence and activity of Phospholipases A2 / PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site. PLA2G2E catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids.
|
|||||
TMPY-02181 | PLA2G12B Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Group XIIB secretory phospholipase A2-like protein, also known as Group XIII secretory phospholipase A2-like protein, GXIII sPLA2-like, sPLA2-GXIIB, GXIIB, PLA2G13 and PLA2G12B, is a secreted protein that belongs to the phospholipase A2 family. PLA2G12B / PLA2G13 is strongly expressed in liver, small intestine and kidney. Mammalian secretory phospholipase A2s ( sPLA2s ) form a family of structurally related enzymes that are involved in a variety of physiological and pathological processes via the release of arachidonic acid from membrane phospholipids or the binding to specific membrane receptors. Phospholipases A2 / PLA2 are enzymes that release fatty acids from the second carbon group of glycerol. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Phospholipases A2 / PLA2 are commonly found in mammalian tissues as well as insect and snake venom. Venom from both snakes and insects is largely composed of melittin, which is a stimulant of Phospholipases A2 / PLA2. Due to the increased presence and activity of Phospholipases A2 / PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site.
|
|||||
TMPH-00214 | SVMP Protein, Bothrops atrox, Recombinant (His & Myc) | Bothrops atrox | E. coli | ||
Snake venom zinc metalloproteinase that acts on fibrinogen, fibrin, fibronectin (FN1), type I collagen, type IV collagen, integrin alpha-7/beta-1 (ITGA7/ITGB1) and integrin alpha-1/beta-1 (ITGA1/ITGB1). Binds to fibronectin (FN1), fibrinogen and, weakly, to type I collagen and laminin. Cleaves Xaa-Leu bonds. Inhibits ADP- and collagen-induced platelet aggregation both in the presence (IC(50)=1.4 uM for collagen) and in the absence (IC(50)=2.2 uM for collagen) of cofactors. Has hemorrhagic activity.
|
|||||
TMPH-03163 | SVTLE Protein, Protobothrops flavoviridis, Recombinant (His & Myc) | Protobothrops flavoviridis | E. coli | ||
Thrombin-like snake venom serine protease that clots fibrinogen (FGA) by releasing fibrinopeptide A. According to PubMed:8585090, only cleaves rabbit fibrinogen, whereas no specificity is described in PubMed:3910643 (tests done on bovine fibrinogen). Also acts as a C3 convertase that independently cleaves human C3 and kick-starts the complement cascade. Also increases urokinase-type plasminogen activator (PLAU) and plasminogen activator inhibitor (SERPINE1) in cultured bovine pulmonary artery endothelial cells. Dose-dependently inhibits collagen-induced platelet aggregation.
|
|||||
TMPY-02357 | CLEC-2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CLEC1B, also known as CLEC2, is a C-type lectin-like receptor expressed in myeloid cells and NK cells. Natural killer (NK) cells express multiple calcium-dependent (C-type) lectin-like receptors, such as CD94 and NKG2D, that interact with major histocompatibility complex class I molecules and either inhibit or activate cytotoxicity and cytokine secretion. CLEC2 acts as a receptor for the platelet-aggregating snake venom protein rhodocytin. Rhodocytin binding leads to tyrosine phosphorylation and this promotes the binding of spleen tyrosine kinase (Syk) and initiation of downstream tyrosine phosphorylation events and activation of PLC-gamma-2. CLEC2 contains 1 C-type lectin domain and is expressed preferentially in the liver. It acts as an attachment factor for human immunodeficiency virus type 1 (HIV-1) and facilitates its capture by platelets.
|
|||||
TMPH-00324 | SVTLE Protein, Calloselasma rhodostoma, Recombinant (His) | Calloselasma rhodostoma | Yeast | ||
Thrombin-like snake venom serine protease that acts as an anticoagulant. It cleaves fibrinogen (FGA) to split off the A-fibrinopeptides (A, AY and AP), but not the B-fibrinopeptide. The resulting fibrin polymers are imperfectly formed and much smaller in size (1 to 2 um long) than the fibrin polymers produced by the action of thrombin. These ancrod-induced microthrombi are friable, unstable, urea-soluble and have significantly degraded alpha chains. They do not cross-link to form thrombi. They are markedly susceptible to digestion by plasmin and are rapidly removed from circulation by either reticuloendothelial phagocytosis or normal fibrinolysis, or both. Anticoagulation through the removal of fibrinogen from the blood is rapid, occurring within hours following its administration. It does not activate plasminogen and does not degrade preformed, fully cross-linked thrombin fibrin. It also reduces the level of plasminogen activator inhibitor (PAI) and may stimulate the release of tissue plasminogen activator (PLAT) from the endothelium. The profibrinolytic effect of these 2 actions appears to be limited to local microthrombus degradation.
|