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Results for "

Carboxypeptidase C

" in MedChemExpress (MCE) Product Catalog:

10

Inhibitors & Agonists

3

Peptides

4

Recombinant Proteins

3

Isotope-Labeled Compounds

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Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-P2746
    Carboxypeptidase B, Porcine pancreas

    EC 3.4.2.2

    		 Endogenous Metabolite Metabolic Disease
    Carboxypeptidase B, Porcine pancreas (EC 3.4.2.2) is a peptide exonuclease that can specifically degrade peptide chains. Carboxypeptidase B is progressively degraded from the C-terminal to release free amino acids. Carboxypeptidase B hydrolyzes only peptide bonds with basic amino acids (such as arginine and lysine) as C-terminal residues .
    Carboxypeptidase B, Porcine pancreas
  • HY-W704574
    Mergetpa

    		Carboxypeptidase Bradykinin Receptor Interleukin Related Cardiovascular Disease Metabolic Disease
    Mergetpa is a reversible Arg-carboxypeptidase inhibitor with high affinity. Mergetpa reduces B1R. Mergetpa blocks the overexpression of IL-1β protein and mRNA in glucose-fed rats. Mergetpa significantly increases the expression of IL-1β protein in the renal cortex. Mergetpa is used to block the conversion of kinins and B2 receptor antagonists into metabolites lacking the C-terminal arginine. Mergetpa inhibits the time-dependent enhancement of the response of isolated rabbit aorta to bradykinin. Mergetpa preserves the chemotactic activity of full-length SDF-1α on cells. Mergetpa reverses hyperglycemia, excessive weight gain, elevated levels of oxidative stress markers and overexpression of inflammatory markers in glucose-fed rats .
    Mergetpa
  • HY-114118S1
    Semaglutide-d8 tetraTFA

    		Isotope-Labeled Compounds GLP Receptor Insulin Receptor α-synuclein Apoptosis p38 MAPK Autophagy Bcl-2 Family Neurological Disease Metabolic Disease Cancer
    Semaglutide-d8 tetraTFA is the deuterium labeled Semaglutide (HY-114118). Semaglutide is a long-acting, selective, competitive GLP-1R agonist that can penetrate the blood-brain barrier. After activating GLP-1R, Semaglutide promotes insulin secretion, inhibits gastric emptying and appetite, and at the same time enhances autophagy, inhibits oxidative stress and apoptosis. Semaglutide also regulates mitochondrial function and lipid metabolism (such as reducing de novo lipogenesis in the liver). Semaglutide has activities such as lowering blood sugar, reducing weight, neuroprotection (such as improving motor function in Parkinson's disease models, reducing α-synuclein aggregation) and improving hepatic steatosis. Semaglutide can be used for the study of neurodegenerative diseases and liver diseases such as type 2 diabetes, obesity, Parkinson's disease, metabolic associated fatty liver disease (MASLD), and cancer .
    Semaglutide-d8 tetraTFA
  • HY-114118S
    Semaglutide-d8

    		Isotope-Labeled Compounds GLP Receptor Insulin Receptor α-synuclein Apoptosis p38 MAPK Autophagy Bcl-2 Family Neurological Disease Metabolic Disease Cancer
    Semaglutide-d8 is the deuterium labeled Semaglutide (HY-114118). Semaglutide is a long-acting, selective, competitive GLP-1R agonist that can penetrate the blood-brain barrier. After activating GLP-1R, Semaglutide promotes insulin secretion, inhibits gastric emptying and appetite, and at the same time enhances autophagy, inhibits oxidative stress and apoptosis. Semaglutide also regulates mitochondrial function and lipid metabolism (such as reducing de novo lipogenesis in the liver). Semaglutide has activities such as lowering blood sugar, reducing weight, neuroprotection (such as improving motor function in Parkinson's disease models, reducing α-synuclein aggregation) and improving hepatic steatosis. Semaglutide can be used for the study of neurodegenerative diseases and liver diseases such as type 2 diabetes, obesity, Parkinson's disease, metabolic associated fatty liver disease (MASLD), and cancer .
    Semaglutide-d8
  • HY-E70201
    Carboxypeptidase B (MS grade)

    EC 3.4.2.2 (MS grade)

    		 Endogenous Metabolite Others
    Carboxypeptidase B (MS grade) is a peptide exonuclease that can specifically degrade peptide chains. Carboxypeptidase B (MS grade) is progressively degraded from the C-terminal to release free amino acids. Carboxypeptidase B (MS grade) hydrolyzes only peptide bonds with basic amino acids (such as arginine and lysine) as C-terminal residues .
    Carboxypeptidase B (MS grade)
  • HY-P2980
    Carboxypeptidase A, Bovine pancreas

    EC 3.4.2.1

    		 Endogenous Metabolite Others
    Carboxypeptidase A, Bovine pancreas (EC 3.4.2.1) is a zinc-containing metalloprotease, is often used in biochemical studies. Carboxypeptidase A catalyzes the hydrolysis of the peptide bonds that are adjacent to the C-terminal end of a polypeptide chain. Carboxypeptidase A is a prototypical enzyme for metalloproteases that plays important roles in biological systems .
    Carboxypeptidase A, Bovine pancreas
  • HY-P2981
    Carboxypeptidase C

    Carboxypeptidase Y; EC 3.4.16.1

    		 Carboxypeptidase Others
    Carboxypeptidase C is a carboxypeptidase, is often used in biochemical studies. Carboxypeptidase C removes COOH-terminal lysine, arginine, and proline, as well as all other neutral, aliphatic, aromatic, and the acidic protein amino acids of a peptide chain .
    Carboxypeptidase C
  • HY-176313S
    Carboxypeptidase B2, Arg-13C6,15N4, Lys-13C6,15N2

    		Isotope-Labeled Compounds Cardiovascular Disease
    Carboxypeptidase B2, Arg- 13C6, 15N4, Lys- 13C6, 15N2 is the 13C-labeled and 15N-labeled Carboxypeptidase B2.
    Carboxypeptidase B2, Arg-13C6,15N4, Lys-13C6,15N2
  • HY-P2746A
    Carboxypeptidase-B rat

    		Carboxypeptidase Others
    Carboxypeptidase-B rat (EC 3.4.17.2) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. Carboxypeptidase-B rat (EC 3.4.17.2) may be used for sequence analysis by successive cleavage of C-terminal basic amino acids.
    Carboxypeptidase-B rat
  • HY-E70958
    Carboxypeptidase G, Pseudomonas sp.

    		Carboxypeptidase Metabolic Disease
    Carboxypeptidase G, Pseudomonas sp. (EC 3.4.17.11) is a lysosomal thiol-dependent protease that stepwise cleaves γ-glutamylpteroyl polyγ-glutamic acid to generate pteroyl-α-glutamic acid (folic acid) and free glutamic acid. Carboxypeptidase G is highly specific for the γ-glutamyl bond but not for the C-terminal amino acid of the leaving group. Carboxypeptidase G can be activated by Zn 2+ ions.
    Carboxypeptidase G, Pseudomonas sp.

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