Recombinant Mouse A Disintegrin And Metalloproteinase With Thrombospondin Motifs 13 (ADAMTS13) Protein (hFc)

Beta LifeScience SKU/CAT #: BLC-07118P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse A Disintegrin And Metalloproteinase With Thrombospondin Motifs 13 (ADAMTS13) Protein (hFc)

Beta LifeScience SKU/CAT #: BLC-07118P
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Product Overview

Description Recombinant Mouse A Disintegrin And Metalloproteinase With Thrombospondin Motifs 13 (ADAMTS13) Protein (hFc) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q769J6
Target Symbol ADAMTS13
Species Mus musculus (Mouse)
Expression System Mammalian cell
Tag C-hFc
Expression Range 904-1137aa
Protein Length Partial
Mol. Weight 54.2 kDa
Research Area Cancer
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.
Subcellular Location Secreted.
Database References
Tissue Specificity Plasma. Expression is consistently high in liver, medium in lung and spleen, low in skeletal muscle and undetectable in heart, brain, kidney and testis.

Gene Functions References

  1. ADAMTS13-vWF axis is partially involved in the pathophysiology of kidney ischemic reperfusion injury. PMID: 27507004
  2. Adamts13 deficiency in obese mice promotes hepatic microthrombosis. PMID: 27604194
  3. results suggest that ADAMTS13 controls key steps of ischemic vascular remodeling and that recombinant ADAMTS13 is a putative therapeutic avenue for promoting stroke recovery. PMID: 28428179
  4. ADAMTS13 retards progression of diabetic nephropathy, most likely by inhibiting VWF-dependent intrarenal thrombosis. PMID: 28495930
  5. administration of ADAMTS13 5 minutes after occlusion dose-dependently dissolved these t-PA-resistant thrombi resulting in fast restoration of MCA patency and consequently reduced cerebral infarct sizes PMID: 26929275
  6. Sleeping beauty transposon-mediated gene therapy achieved sustained expression of transgene ADAMTS13 and long-term prophylaxis against congenital thrombotic thrombocytopenic purpura in Adamts13(-/-) mice. PMID: 28254814
  7. Results also suggest that Toxoplasma gondii-mediated apoptosis might play a pivotal role and a different type of role in the mechanism of neurodegeneration and neuropathology in the process of toxoplasma encephalitis. Furthermore, expression of ADAMTS-13 might give an idea of the progress and is critical for diagnosis of this disease. PMID: 26542631
  8. Letter: deficiency of ADAMTS13 results in increased formation of venous thrombosis in mice. PMID: 25855507
  9. ADAMTS13 substrate specificity PMID: 25849793
  10. Data indicate that the p.D187H mutation impairs ADAMTS13 activity and secretion and may contribute to thrombotic thrombocytopenic purpura. PMID: 25442981
  11. Data show that metalloendopeptidase ADAMTS13 does not directly promote development of adipose tissue. PMID: 25813552
  12. findings provide further evidence on the pathophysiological role for the ADAMTS13/VWF axis in atherosclerosis PMID: 24261607
  13. Carboxyl terminus of ADAMTS13 directly inhibits platelet aggregation and ultra large von Willebrand factor string formation under flow in a free-thiol-dependent manner. PMID: 24357063
  14. Three novel mutations in a homozygous state were identified in these patients: c.1308G>C, c.428T>C (p.Ile143Thr) and c.1709A>G (p.Tyr570Cys) PMID: 24115559
  15. The results indicate that the microvascular process induced by ADAMTS13 deficiency triggers complement activation on platelets and the endothelium, which may contribute to formation of thrombotic microangiopathy. PMID: 23878316
  16. model of acute myocardial infarction in ADAMTS13 gene deleted (Adamts13 -/-) mice PMID: 23051932
  17. We hypothesize that ADAMTS13 protects brain from ischemia-reperfusion injury by regulating von Willebrand factor -dependent inflammation as well as microvascular plugging PMID: 22212812
  18. Cyclophilin B activity regulated secretion and activity of ADAMTS13. PMID: 23144461
  19. Adamts13(-/-) mice developed larger myocardial infarctions than wild-type control mice. PMID: 22915644
  20. ADAMTS13 and VWF are causally involved in myocardial ischemia/reperfusion injury. PMID: 22983446
  21. We revealed the epitopes of 11 monoclonal anti-ADAMTS13 antibodies on each of the domains and clarified their association with inhibitory effects on VWF catalysis under static conditions. PMID: 22721582
  22. Provide new evidence for ADAMTS13 in reducing VWF-mediated acute cerebral inflammation following ischemic stroke. PMID: 22712744
  23. ADAMTS13 plays a critical role in modulating the development of early atherosclerosis. PMID: 22652598
  24. Prophylactic administration of 200 units/kg recombinant human ADAMTS13 protected ADAMTS13 knockout mice from developing thrombotic thrombocytopenic purpura. PMID: 22529289
  25. Gender-dependent up-regulation of ADAMTS-13 in mice with obesity and hypercholesterolemia. PMID: 22192156
  26. Findings suggest a new functional role for the antithrombotic enzyme ADAMTS13 in reducing excessive vascular inflammation and plaque formation during early atherosclerosis. PMID: 22123843
  27. Results suggest that the amino terminus of ADAMTS13, specifically the variable region of the spacer domain, is crucial for modulation of arterial thromboses under (patho)physiological conditions. PMID: 21799176
  28. Glomerular endothelial cells express and secrete ADAMTS13. PMID: 21720563
  29. in vivo imaging analysis revealed that ADAMTS13 regulates the disappearance of platelet strings on DDAVP-stimulated VECs and on the FeCl3-injured venous vascular wall through the cleavage of UL-VWF. PMID: 21494805
  30. ADAMTS13 CUB and T2-8 domains influence proteolysis of platelet-decorated VWF strings in vivo PMID: 20695979
  31. von Willebrand factor clearance does not involve proteolysis by ADAMTS-13 PMID: 20704649
  32. Shiga toxin B subunits induce thrombotic microangiopathy in Adamts13(-/-) mice. PMID: 20644116
  33. Mutation and ADAMTS13-dependent modulation of disease severity in a mouse model for von Willebrand disease type 2B. PMID: 20200350
  34. ADAMTS13 down-regulates platelet adhesion and aggregation in vivo, and ADAMTS13 deficiency can provide enhanced thrombus formation at the site of vascular lesions in mice PMID: 20047094
  35. ADAMTS13 may protect the brain from ischemia by regulating VWF-platelet interactions after reperfusion. PMID: 19965676
  36. analysis of strain-specific variants of mouse Adamts13 gene encoding von Willebrand factor-cleaving protease PMID: 15136581
  37. Identification of the liver cell-type expressing ADAMTS13 will have is important for understanding pathophysiological mechanisms regulating ADAMTS13 expression. PMID: 15806136
  38. characterization of the full-length murine ADAMTS13 PMID: 15869605
  39. REVIEW: the nature of ADAMTS13's interaction with von Willebrand factor and the pathogenesis of clinical thrombotic thrombocytopenic purpura, especially in relation to ADAMTS13 PMID: 17414218
  40. REVIEW: Accumulated clinical information on patients with ADAMTS13 deficiency and mice lacking the Adamts13 gene indicates that additional environmental or genetic susceptibility factors are required to trigger thrombotic thrombocytopenic purpura. PMID: 17414219
  41. the plasma ADAMTS13 activity levels of mouse strains segregated into a high and a low group. Low ADAMTS13 activity was detected in mice containing 2 alleles of intracisternal A-type particle (IAP) retrotransposon sequence PMID: 17426255
  42. Imbalance between the blood von Willebrand factor and ADAMTS13 levels may occur in endotoxinemia, which may partly contribute to the thrombotic state associated with endotoxinemia. PMID: 18006046
  43. the potential roles played by ADAMTS13 and VWF in TTP, endotoxemia, and normal hemostasis. PMID: 18083848
  44. a new mechanism of anthrax coagulopathy affecting the levels and functional activities of both VWF and its natural regulator ADAMTS13. This mechanism may contribute to hemorrhage and thrombosis typical in anthrax. PMID: 18263586
  45. ADAMTS13 has an important role in preventing excessive spontaneous Weibel-Palade body secretion, and in the regulation of leukocyte adhesion and extravasation during inflammation PMID: 18695007
  46. the C-terminally truncated ADAMTS13 exhibited decreased activity in the cleavage of VWF under high shear rate and accelerated thrombogenesis PMID: 19109562
  47. von Willebrand factor-cleaving protease ADAMTS13 reduces ischemic brain injury in experimental stroke. PMID: 19687510


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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