You Searched For: 3-Amino-9H-pyrido[3,4-b]indole


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Catalog Number: (89517-444)
Supplier: Abgent
Description: Western Blot: 1:1000


Catalog Number: (89515-462)
Supplier: Abgent
Description: Western Blot: 1:1000


Catalog Number: (10495-540)
Supplier: Bioss
Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).


Catalog Number: (10083-424)
Supplier: Proteintech
Description: Axis inhibition protein2 (AXIN2), also known as Coductin or Axil, is a multidoman scaffold protein that negatively regulate Wnt signaling. AXIN2 can directly interact with beta-catenin and GSK3B. AXIN2 has a number of phosphorylation sites, and also can undergo poly(ADP-ribosy)lation by tankyrase TNKS and TNKS2. Poly(ADP-ribosy)lated AXIN2 then get unbiquitinated by RNF146 and leads to its degradation and subsequent activation of Wnt signaling. AXIN2 is localized in the cytoplasm and its mutaion is involved in colorectal cancer. Catalgo#20540-1-AP is a rabbit polyclonal antibdy raised against a 34 amino acid N-terminal of human AXIN2.


Catalog Number: (89518-774)
Supplier: Abgent
Description: Western Blot: 1:1000


Catalog Number: (89517-454)
Supplier: Abgent
Description: Western Blot: 1:1000


Catalog Number: (89518-714)
Supplier: Abgent
Description: Western Blot: 1:100~250,


Supplier: TCI America
Description: Coumarin 504T, CAS Number: 113869-06-0, Purity: 98.0% HPLC, Molecular Formula: C22H27NO4, Molecular Weight: 369.46 g/mol, Synonyms: Ethyl 2,3,6,7-Tetrahydro-1,1,7,7-tetramethyl-11-oxo-1H,5H,11H-[1]benzopyrano[6,7,8-ij]quinolizine-10-carboxylate, Physical Form: Solid, Size: 1G

SDS

Catalog Number: (10488-694)
Supplier: Bioss
Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).


Catalog Number: (10488-688)
Supplier: Bioss
Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).


Catalog Number: (10495-528)
Supplier: Bioss
Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).


Catalog Number: (10165-226)
Supplier: Genetex
Description: Rabbit Polyclonal antibody to UBE3A (ubiquitin protein ligase E3A)


Catalog Number: (89516-760)
Supplier: Abgent
Description: Western Blot: 1:100~500,


Catalog Number: (75791-954)
Supplier: Prosci
Description: Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino acid, l-tryptophan, along the kynurenine pathway. This protein is normally expressed in the dendritic cells, macrophages, microglia, eosinophils, fibroblasts, endothelial cells, and most tumor cells. IDO activity is associated with immunosuppression and immune attenuation. Several studies showed that IDO can contribute to immune escape when expressed directly in tumor cells or when expressed in immunosuppressive antigen presenting cells such as tolerogenic dendritic cells or tumor associated macrophages. IDO also is a promising therapeutic target for the treatment of cancer, chronic viral infections, and other diseases characterized by pathological immune suppression.


Catalog Number: (10488-686)
Supplier: Bioss
Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).


Catalog Number: (10488-690)
Supplier: Bioss
Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).


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