SCPA (C-Term) anticorps

Détails pour le produit réf. ABIN967004, Fournisseur: Connectez-vous pour afficher
Antigène
Épitope
C-Term
Reactivité
Staphylococcus aureus (S. aureus)
Hôte
Lapin
Clonalité
Polyclonal
Application
Immunohistochemistry (IHC)
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Immunogène Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of Bacteria: Staphylococcus aureus scpA (Staphylococcal cysteine proteinaseA)
Antigène
Sujet The scpA (Staphylococcal cysteine proteinaseA) is able to degrade elastin. scpA (Staphylococcal cysteine proteinaseA) has a broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate. Prematurely activated/folded staphopain A is inhibited by staphostatin A (scpB), which is probably required to protect staphylococcal cytoplasmic proteins from degradation by scpA. In the cytoplasm, prematurely activated/folded scpA forms a stable non-covalent complex with scpB. Cleavage leads to the activation of scpA probably by an auto-catalytic manner. The catalytic maturation of scpA appears to reside outside the cascade of activation started by the metalloprotease aureolysin (aur) scpA (Staphylococcal cysteine proteinaseA) belongs to the peptidase C47 family.
Synonyms: sspP, sspB2, Staphopain A
Restrictions For Research Use only
Produit citée dans: Golonka, Filipek, Sabat, Sinczak, Potempa: "Genetic characterization of staphopain genes in Staphylococcus aureus." dans: Biological chemistry, Vol. 385, Issue 11, pp. 1059-67, 2004 (PubMed).

Dubin, Krajewski, Popowicz, Stec-Niemczyk, Bochtler, Potempa, Dubin, Holak: "A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus." dans: Biochemistry, Vol. 42, Issue 46, pp. 13449-56, 2003 (PubMed).

Potempa, Dubin, Korzus, Travis: "Degradation of elastin by a cysteine proteinase from Staphylococcus aureus." dans: The Journal of biological chemistry, Vol. 263, Issue 6, pp. 2664-7, 1988 (PubMed).

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