Catalogue Number | PRO-607 |
Synonyms | Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Defibrase, Reptilase, Batroxobin. |
Introduction | Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
Batroxobin is a single chain glycopeptide with a molecular mass of 43kDa on SDS-PAGE gel and its pI-6.6. Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin. |
Description | The Batroxobin Recombinant Protein, produced in yeast, is a single, glycosilated polypeptide chain containing 231 amino acids and having an Mw of approximately 28-33 kDa. |
Source | Pichia Pastoris. |
Physical Appearance | Sterile Filtered white lyophilized powder. |
Formulation | The Batroxobin protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM sodium acetate buffer, pH 7.4. |
Solubility | It is recommended to reconstitute the lyophilized Batroxobin in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. |
Stability | Batroxobin although stable at room temperature for 3 weeks, should be stored below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below
-18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles. |
Purity | Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE. |
Biological Activity | Batroxobin’s biological activity was found to be of no less than 500KU/mg. (Klobusitzky Unit). |
Amino Acid Sequence | VIGGDECDIN EHPFLAFMYY SPRYFCGMTL INQEWVLTAA HCNRRFMRIH LGKHAGSVAN YDEVVRYPKE KFICPNKKKN VITDKDIMLI RLDRPVKNSE HIAPLSLPSN PPSVGSVCRI MGWGAITTSE DTYPDVPHCA NINLFNNTVC REAYNGLPAK TLCAGVLQGG IDTCGGDSGG PLICNGQFQG ILSWGSDPCA
EPRKPAFYTK VFDYLPWIQS IIAGNKTATC P. |
References | Title:Impaired clot retraction in factor XIII A subunit-deficient mice Supplemental materials for: Kasahara et al
Publication:Published online before print December 8, 2009, doi: 10.1182/blood-2009-06-227645 Blood |