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Salmon thrombin （三文鱼凝血酶/鲑鱼凝血酶）
Catalog Number
SEA-135
Description
Plasma protein from the blood of farmed S. salar
Product Background
Background:
- Fibrin gels made from salmon proteins have demonstrated remarkable properties in neuron survival and growth.
- Salmon fibrin gels represent the optimal matrix for neuronal cell cultural
- Salmon fibrin gels have also properties superior to mammalian gels in an in vitro angiogenesis model. The salmon gels were 60-188% more efficient than human fibrin gels supporting growth of human endothetlial cells. These results indicate that salmon fibrin may be attractive alternate ECM for support of microvascular network formation.
- Salmon fibrinogen and thrombin can be used at room temperature
- Soft salmon fibrin gels have been shown to promote selection and growth of tumorigenic cells
Research Targets:
- Regenerative Medicine
- Spinal Cord Injury
- Neural cell regrowth
- Pain & CNS Investigators
- Stem Cell Research
- Cancer stem cell research
Benefits:
- Superior Performance- demonstrated superiority to Matrigel as an extracellular matrix for neuronal cell growth.
- Safety from mammalian pathogens
- Easy of rehydration & improved thermal properties.
For more information on Salmon fibrinogen and thrombin:
Sieminski and Gooch. 2004. J Biomater Sci Polym. Ed 15(2):237-42
Ju, et al. Biomaterials. 2007 April; 28 (12): 2097-2108
Liu J, et al. Nat Mater. 2012 Jul 1;11(8):734-41. doi: 10.1038/nmat3361.
Information Sheet
Application Note
Category
Miscellaneous Proteins
Formulation
Dialyzed in 200 mM Tris, 3 mM CaCl2, 0.15M NaCl, pH 7.2-7.5.
Reconstitution
Rehydrate with H2O at room temperature or below. Remove the amount to be used that day, and hold on ice. Salmon thrombin retains greater than 80% activity after 24 hours on ice. Aliquot remaining thrombin and freeze at <-60°C
Storage
Freezer (<-10°C). Avoid freeze-thaw cycles
Purity
Affinity chromatography on immobilized heparin, SDS-PAGE
Sourced from salmon shown by certified tests to be negative for fish viruses. Activity tested by spectrophometric analysis of peptide hydrolysis (Chromozyme), and compared to human standard.
Filtered to 0.2 u
Activity
≥ 1000 Units/ mg protein
References
US Patent #6,007,811 and 6,861,225. Michaud et al, 2002. Thrombosis Research 107:245-54
Sieminski and Gooch. 2004. J Biomater Sci Polym. Ed 15(2):237-42
Ju, et al. Biomaterials. 2007 April; 28 (12): 2097-2108
Salmon fibrin treatment of spinal cord injury promotes functional recovery and density of serotonergic innervation
Liu J, et al. Nat Mater. 2012 Jul 1;11(8):734-41. doi: 10.1038/nmat3361.
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