Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Purification
This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogen
This HtrA3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 112-144 amino acids from the N-terminal region of human HtrA3.
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Expiry Date
6 months
Narkiewicz, Klasa-Mazurkiewicz, Zurawa-Janicka, Skorko-Glonek, Emerich, Lipinska: "Changes in mRNA and protein levels of human HtrA1, HtrA2 and HtrA3 in ovarian cancer." in: Clinical biochemistry, Vol. 41, Issue 7-8, pp. 561-9, (2008) (PubMed).
Grau, Baldi, Bussani, Tian, Stefanescu, Przybylski, Richards, Jones, Shridhar, Clausen, Ehrmann: "Implications of the serine protease HtrA1 in amyloid precursor protein processing." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, Issue 17, pp. 6021-6, (2005) (PubMed).
Nie, Hampton, Li, Findlay, Salamonsen et al.: "Identification and cloning of two isoforms of human high-temperature requirement factor A3 (HtrA3), characterization of its genomic structure and comparison of its tissue distribution with HtrA1 and ..." in: The Biochemical journal, Vol. 371, Issue Pt 1, pp. 39-48, (2003) (PubMed).
Insulin-like growth factors (IGFs) stimulate the proliferation and differentiation of a vast number of cell types. The action of the growth factors is mediated and controlled by a complex system of components, including several proteases that cleave the IGF-Binding Proteins. HtrA1 is a 480 aa protein that contains an N-terminus homologous to MAC25 (IGFBP7) with a conserved Kazal-type serine protease inhibitor motif, as well as a C-terminal PDZ domain. Semiquantitative RT-PCR and immunoblot analyses showed an approximately 7-fold increase of PRSS11 in osteoarthritis cartilage compared with controls. HTRA2 is released from mitochondria and inhibits the function of XIAP by direct binding in a way similar to SMAC. Moreover, when overexpressed extramitochondrially, HTRA2 induced atypical cell death, which was neither accompanied by a significant increase in caspase activity nor inhibited by caspase inhibitors, including XIAP. A catalytically inactive mutant of HTRA2, however, did not induce cell death. Suzuki et al. (2001) concluded that HTRA2 is a SMAC-like inhibitor of IAP (inhibitor of apoptosis proteins) activity with a serine protease-dependent cell death-inducing activity.