2147
None
IF(IHC-P)
anticorps
Unmodified
Polyclonal
499nm/519nm
Alexa Fluor
1ug per 1ul
Human, Mouse, Rat
ALEXA FLUOR® 488
IF(IHC-P)(1:50-200)
Polyclonal antibody
Thrombin heavy chain
Purified by Protein A.
Conjugated Primary Antibodies
Rabbit (Oryctolagus cuniculus)
Anti-Thrombin heavy chain PAb ALEXA FLUOR 488
This is a highly specific antibody against Thrombin heavy chain.
Thrombin heavy chain Polyclonal Antibody, ALEXA FLUOR 488 Conjugated
Due to limited amount of testing and knowledge, not every possible cross-reactivity is known.
This antibody was obtained by immunization of the host with KLH conjugated synthetic peptide derived from human Thrombin heavy chain
Store this antibody in aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Keep refrigerated at 2 to 8 degrees Celcius for up to one year.
coagulation factor II; prothrombin; F2; Cf-2; Cf2; FII; F 2; coagulation factor II thrombin; Coagulation factor II; Coagulation factor II precursor; F2; Factor II; Factor-II; Prothrombin; prothrombin B-chain; PT; serine protease; THRB; THRB_HUMAN; Thrombin; Thrombin heavy chain.
For facs or microscopy Alexa 1 conjugate.Alexa Fluor 488 has the same range to that of fluorescein isothiocyanate (FITC), yet the Anti-Thrombin heavy chain has a very high photo stability. As a result of this photo stability, it has turned into an antibody for fluorescent microscopy and FACS FLOW cytometry. It is distinguished in the FL1 of a FACS-Calibur or FACScan. Also Alexa Fluor 488 is pH stable.If you buy Antibodies supplied by Bioss Primary Conjugated Antibodies. ALEXA FLUOR they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.
Thrombin is the final protease in the blood coagulation cascade and serves both pro- and anticoagulant functions through the cleavage of several targets. The ability of thrombin to specifically recognize a wide range of substrates derives from interactions which occur outside of the active site of thrombin. Thrombin possesses two anion binding exosites which mediate many of its interactions with cofactors and substrates, and although many structures of thrombin have been solved, few such interactions have been described in molecular detail. Glycosaminoglycan binding to exosite II of thrombin plays a major role in switching off the procoagulant functions of thrombin by mediating its irreversible inhibition by circulating serpins and by its binding to the endothelial cell surface receptor thrombomodulin.