You Searched For: DL-Lysine+monohydrate

Catalog Number: (BOSSBS-11773R-A680)

Supplier: Bioss

Description: Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane, known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through the formation of disulfide bonds and gamma-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are Ca²⁺ dependent enzymes, which catalyse the formation of isopeptide bonds by transferring an amine to a glutaminyl residue, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. TGase6 (transglutaminase 6), also known as TGM6, TGY or TGM3L, is a 706 amino acid protein that catalyses the cross-linking of proteins and the conjugation of proteins to polyamines. As a result of alternative splicing, two TGase6 isoforms exist.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11773R-A350)

Supplier: Bioss

Description: Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane, known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through the formation of disulfide bonds and gamma-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are Ca2+-dependent enzymes, which catalyze the formation of isopeptide bonds by transferring an amine to a glutaminyl residue, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. TGase6 (transglutaminase 6), also known as TGM6, TGY or TGM3L, is a 706 amino acid protein that catalyzes the cross-linking of proteins and the conjugation of proteins to polyamines. As a result of alternative splicing, two TGase6 isoforms exist.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9486R-A555)

Supplier: Bioss

Description: A crucial regulator of chromatin dynamics and DNA transcription is the covalent modification and methylation of histones. Generally, methylation of certain lysine residues on Histone H3 and Histone H4 can be associated with transcriptionally active or inactive chromatin. This regulation has profound effects on the expression of genes and is part of an epigenetic memory network that determines cell fate. JMJD7 (Jumonji domain-containing protein 7) is a member of a family of JMJC domain-containing histone demethylases that are directly involved in removing methyl residues from distinct and unique lysine residues. These actions are implicated in gene expression and the regulation of cell senescence. JMJC domain-containing histone demethylases are also likely involved in development via their ability to regulate gene expression. JMJD7 contains one JMJC domain and was originally thought to be an alternatively spliced isoform of PLA2G4B.

UOM: 1 * 100 µl

Supplier: Thermo Scientific

Description: Hydrazine hydrate 100% (∼64% w/w N₂H₄)

MSDS

Supplier: Thermo Scientific

Description: Hydrazine hydrate 55% in aqueous solution (∼35% w/w N₂H₄)

MSDS

Catalog Number: (0664-2.5KG)

Supplier: VWR Chemicals

Description: DL-Malic acid 99-100.5%, high purity

UOM: 1 * 2,5 kg

MSDS

Catalog Number: (BOSSBS-7547R-A647)

Supplier: Bioss

Description: This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-7547R-FITC)

Supplier: Bioss

Description: This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-8589R-CY7)

Supplier: Bioss

Description: Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9907R-A750)

Supplier: Bioss

Description: CPN2 is a zinc metalloprotease, and cleaves carboxy-terminal arginines and lysines from peptides found in the bloodstream such as complement anaphylatoxins, kinins, and creatine kinase MM (CK-MM). By removing only one amino acid, CPN has the ability to change peptide activity and receptor binding. It is a 280 kDa tetrameric glycoprotein that is synthesised by the liver and secreted into the plasma. It consists of 2 identical 83 kDa regulatory subunits (CPN2) and 2 identical 50 kDa catalytic subunits (CPN1). CPN2, the 83 kDa subunit, binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit. CPN is a member of a larger family of carboxypeptidases, many of which also cleave arginine and lysine. Because of the highly conserved active sites and the possible redundant functions of carboxypeptidases, it has been difficult to elucidate the role of CPN in disease processes.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-8589R-A750)

Supplier: Bioss

Description: Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localising, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilisation, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9907R-A680)

Supplier: Bioss

Description: CPN2 is a zinc metalloprotease, and cleaves carboxy-terminal arginines and lysines from peptides found in the bloodstream such as complement anaphylatoxins, kinins, and creatine kinase MM (CK-MM). By removing only one amino acid, CPN has the ability to change peptide activity and receptor binding. It is a 280 kDa tetrameric glycoprotein that is synthesised by the liver and secreted into the plasma. It consists of 2 identical 83 kDa regulatory subunits (CPN2) and 2 identical 50 kDa catalytic subunits (CPN1). CPN2, the 83 kDa subunit, binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit. CPN is a member of a larger family of carboxypeptidases, many of which also cleave arginine and lysine. Because of the highly conserved active sites and the possible redundant functions of carboxypeptidases, it has been difficult to elucidate the role of CPN in disease processes.

UOM: 1 * 100 µl

Catalog Number: (47786.)

Supplier: Merck

Description: DL-α-Tocopherol acetate

UOM: 1 * 1 items

Catalog Number: (BOSSBS-1587R-A750)

Supplier: Bioss

Description: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyses the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-8589R)

Supplier: Bioss

Description: Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-8589R-A350)

Supplier: Bioss

Description: Terminally differentiating mammalian epidermal cells acquire an insoluble, 10 to 20 nm thick protein deposit on the intracellular surface of the plasma membrane known as the cross-linked cell envelope (CE). The CE is a component of the epidermis that is generated through formation of disulfide bonds and g-glutamyl-lysine isodipeptide bonds, which are formed by the action of transglutaminases (TGases). TGases are intercellularly localizing, Ca2+-dependent enzymes that catalyze the formation of isopeptide bonds by transferring an amine on to glutaminyl residues, thereby cross-linking glutamine residues and lysine residues in substrate proteins. TGases influence numerous biological processes, including blood coagulation, epidermal differentiation, seminal fluid coagulation, fertilization, cell differentiation and apoptosis. Human keratinocyte transglutaminase (TGase1) is a membrane associated, 817 amino acid protein. Human tissue transglutaminase (TGase2) is an endothelial cell specific, 687 amino acid protein.

UOM: 1 * 100 µl