Human Gamma Thrombin

Description

Human Gamma Thrombin

Human Gamma Thrombin is a proteolytically modified form of alpha-thrombin, characterized by a truncated structure that retains selective enzymatic activity while exhibiting altered substrate specificity. With a molecular weight of approximately 12 kDa, this highly purified preparation is supplied as a lyophilized powder and is ideal for use in coagulation studies, platelet activation assays, and receptor signaling research.

Gamma thrombin is generated through limited proteolysis and differs functionally from alpha-thrombin in its ability to cleave specific substrates and modulate immune responses. It has been studied for its interactions with glycoprotein V, antithrombin III, and thrombomodulin, as well as its role in cytokine regulation and platelet aggregation. This product is stable at 20C and should be reconstituted in sterile buffer for optimal performance. All solutions are prepared using Type I ultrapure water and filtered through 0.22 m membranes to ensure consistency and reproducibility.

Key benefits:

• Highly purified gamma thrombin for biochemical and immunological assays
• Validated molecular weight (12 kDa) and lyophilized format
• Supports research in coagulation, inflammation, and receptor biology
• Ideal for substrate specificity and proteolytic activity studies
• Stable at 20C; filtered and formulated with ultrapure water

Indication for Use:
This product is for Research Use Only (RUO). It is not intended for human or animal use, diagnostic procedures, or therapeutic applications.

References:

• Davie EW, Kulman JD. An overview of the structure and function of thrombin Semin Thromb Hemost. 2006 Apr;32 Suppl 1:3-15.
• Jandrot-Perrus M, Guillin MC, Nurden AT. Human gamma-thrombin: lack of correlation between a platelet functional response and glycoprotein V hydrolysis Thromb Haemost. 1987 Oct 28;58(3):915-20.
• Naldini A, Morena E, Filippi I, Pucci A, Bucci M, Cirino G, Carraro F. Thrombin inhibits IFN-gamma production in human peripheral blood mononuclear cells by promoting a Th2 profile J Interferon Cytokine Res. 2006 Nov;26(11):793-9.
• Brower MS, Walz DA, Garry KE, Fenton JW 2nd. Human neutrophil elastase alters human alpha_thrombin function: limited proteolysis near the gamma-cleavage site results in decreased fibrinogen clotting and platelet-stimulatory activity Blood. 1987 Mar;69(3):813-9.
• Bezeaud A, Denninger MH, Guillin MC. Interaction of human alpha_thrombin and gamma_thrombin with antithrombin III, protein C and thrombomodulin Eur J Biochem. 1985 Dec 16;153(3):491-6.
• Rydel TJ, Yin M, Padmanabhan KP, Blankenship DT, Cardin AD, Correa PE, Fenton JW 2nd, Tulinsky A. Crystallographic structure of human gamma_thrombin J Biol Chem. 1994 Sep 2;269(35):22000-6.
• Soslau G, Prest PJ, Class R, Jost M, Mathews L. Inhibition of gamma_thrombin-induced human platelet aggregation by histone H1subtypes and H1.3 fragments Platelets. 2009 Aug;20(5):349-56.
• Witting JI, Miller TM, Fenton JW 2nd. Human alpha- and gamma_thrombin specificity with tripeptide p-nitroanalide substrates under physiologically relevant conditions Thromb Res. 1987 May 15;46(4):567-74.
• Bishop PD, Lewis KB, Schultz J, Walker KM. Comparison of recombinant human_ thrombin_ and plasma-derived human alpha_thrombin Semin Thromb Hemost. 2006 Apr;32 Suppl 1:86-97.
• Huntington JA. Thrombin plasticity Biochim Biophys Acta. 2012 Jan;1824(1):246-52.