Acidic Mammalian Chitinase (Human, Active)

  • Code # CY-E1248
  • Size 10 μg
  • Price
    $440.01
Specifications

Alternative Names

CHIA, AMCase

Background

The glycosyl hydrolase family is quite large, with over 100 families. Acidic mammalian chitinase (AMCase) and chitotriosidase-1 are enzymatically active true chitinases in a member of the glycosyl hydrolase-18 family, identified by EC 3.2.1.14. In mammals, only these two enzymes cleave N-acetyl-beta-D-glucosamine (1->4)-beta linkages in chitodextrins and chitin, the second most abundant biopolymer that can be found in the cell walls of fungi, micro-filarial sheaths of helminths, and exoskeletons of insects and crustaceans (1). Other member included in this family are chitinase-like molecules, e.g. YKL-40/Chitinase-3-like-1 and YKL-39/chitinase-3-like-2, that are thought to lack the ability to hydrolyze the chitin linkages, but retain chitin-binding activity (2, 3) and act more like connective tissue proteins, and immediate early gene products. AMCase was cloned as an acid-stable active enzyme and is highly expressed in the gastrointestinal tract, and to a lesser extent, in the lung and alveolar macrophages in both humans and mice (4, 5), with an optimum activity at pH 4–5 (6). AMCase as well as chitotriosidase-1 is 50 kDa proteins, consisting of a 39 kDa catalytic region separated from a chitin-binding domain by a hinge region (7,8). They both show considerable homology to chitinases from lower organisms. AMCase is one of the important proteins involved in Th2-mediated inflammation and has been implicated in asthma and allergic diseases by affecting the IL-13 downstream pathway (9). Inhibition of AMCase results in decreased airway inflammation and airway hyper-responsiveness in a murine asthmatic model, suggesting that the AMCase activity is a part of the mechanism of Th2 cytokine-driven inflammatory response in asthma (9).
  • Description:

    Acidic Mammalian Chitinase (Human, Active) of 10 μg.

  • Formulation:
    Recombinant human acidic mammalian chitinase is supplied frozen in a buffer containing 20 mMHEPES-KOH, pH 7.5, 1 mM DTT, 50 mM NaCl and 50% glycerol.
  • Product Type:
    Recombinant Protein
  • Research Area:
    Immunology
  • Short Description:

    Acidic Mammalian Chitinase (Human, Active).

  • Size:
    10 μg
  • Storage Temperature:
    -70°C
References
  1. Tharanathan, R. N. and Kittur, F. S: Chitin-the undisputed biomolecule of great potential. Crit. Rev. Food Sci. Nutr. 2003; 43: 61.
  2. Funkhouser JD, Aronson NN Jr: Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family. BMC Evol Biol 2007; 7: 96-111.
  3. Bussink AP, Speijer D, Aerts JM, Boot RG: Evolution of mammalian chitinase(-like) members of family 18 glycosyl hydrolases. Genetics 2007; 177: 959-970.
  4. Boot RG, Blommart EF, Swart E, Ghauharali-van der Vlugt K, Bijl N, Noe C, Place A, Aerts JM: Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem 2001; 276: 6770-6778.
  5. Boot RG, Bussink AP, Verhoek M, de Boer PA, Moorman AF, Aerts JM: Marked differences in tissue-specific expression of chitinases in mouse and man. J Histochem Cytochem 2005; 53: 1283-1292.
  6. Chou YT, Yao S, Czerwinski R, Fleming M, Krykbaev R, Xuan D, Zhou H, Brooks J, Fitz L, Strand J, Presman E, Lin L, Aulabaugh A, Huang X: Kinetic characterization of recombinant human acidic mammalian chitinase. Biochemistry 2006; 45: 4444-4454.
  7. Boot, R.G., Blommaart, E.F., Swart, E., Ghauharali-van der Vlugt, K., Bijl, N., Moe, C., Place, A. and Aerts, J.M: Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J. Biol. Chem. 2001; 276: 6770-6778.
  8. Boot, R.G., Renkema, G.H., Strijland, A., van Zonneveld, A.J. and Aerts, J.M:Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages. J. Biol. Chem. 1995; 270: 26252–26256.
  9. Zhu Z, Zheng T, Homer RJ, Kim YK, Chen NY, Cohn L, Hamid Q, Elias JA: Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science 2004; 304: 1678-1682