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- xy11504-RP02
- 2025年07月08日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
常温，避光
- 克隆性：
单克隆
- 抗体名：
Carboxypeptidase B2 / CPB2抗体
Antibody Type : Rabbit Polyclonal Antibody ( Antibody Purification Platform )
抗体宿主 : Rabbit IgG
缓冲液 : 0.2 μm filtered solution in PBS, 5% trehalose may be added in some batches. Please read the hardcopy of COA or contact our customer service to confirm the formulation.
制备方法 : Produced in rabbits immunized with purified, recombinant Human Carboxypeptidase B2 / CPB2 (rh Carboxypeptidase B2 / CPB2; Catalog#11504-H08H; NP_001863.2; Met1-Val423). Carboxypeptidase B2 / CPB2 specific IgG was purified by Human Carboxypeptidase B2 / CPB2 affinity chromatography.
Carboxypeptidase B2 / CPB2抗体 Background
Carboxypeptidase B2, also known as Carboxypeptidase U, Thrombin-activable fibrinolysis inhibitor, Plasma carboxypeptidase B, CPB2, is a secreted protein which belongs to the peptidase M14 family. Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). CPB2 is activated by thrombin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen. When it is activated by proteolysis at residue Arg92 by the thrombin / thrombomodulin complex. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. CPB2 exhibits carboxypeptidase activity and activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.
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文献和实验Preparation of Carboxypeptidase Y and Its Properties
analysis. The enzyme is quite different from the pancreatic carboxypeptidases A and B in many aspects. Carboxypeptidase Y is an acidic glycoprotein without metals. Since carboxypeptidase Y was found in 1967, its physical and chemical properties
Binding of Duck Carboxypeptidase D to Duck Hepatitis B Virus
The initial step in viral infection is binding of the particle to a receptor on the host-cell surface. The specificity of this process is the outcome of an evolutionary adaptation of the pathogen to its host. Receptor recognition frequently
Carboxypeptidase Y (EC 3.4.16.1)
sequence data. These are: carboxypeptidase A (EC 3.4.17-l) from bovine pancreas (1 ), carboxypeptidase B (EC 3.4.17.2) from porcine pancreas (1 ), carboxypeptidase C (EC 3.4.12.1) from orange leaves (2 ), and carboxypeptidase Y (EC 3.4.16.1) from yeast
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