Recombinant Mouse Von Willebrand Factor (VWF) Protein (His&Myc)

Name: Recombinant Mouse Von Willebrand Factor (VWF) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-02573P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Von Willebrand Factor (VWF) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q8CIZ8
Target Symbol	VWF
Synonyms	Vwfvon Willebrand factor; vWF) [Cleaved into: von Willebrand antigen 2; von Willebrand antigen II)]
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	DVVFVLEGSDEVGEANFNKSKEFVEEVIQRMDVSPDATRISVLQYSYTVTMEYAFNGAQSKEEVLRHVREIRYQGGNRTNTGQALQYLSEHSFSPSQGDRVEAPNLVYMVTGNPASDEIKRLPGDIQVVPIGVGPHANMQELERISRPIAPIFIRDFETLPREAPDLV
Expression Range	1498-1665aa
Protein Length	Partial
Mol. Weight	23.9 kDa
Research Area	Cardiovascular
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	Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma.
Subcellular Location	Secreted. Secreted, extracellular space, extracellular matrix.
Database References	KEGG: mmu:22371 STRING: 10090.ENSMUSP00000001995 UniGene: Mm.22339
Tissue Specificity	Plasma. Expressed in liver.

Gene Functions References

is synthesized in megakaryocytes and endothelial cells (ECs) and has two main roles: to carry and protect coagulation factor VIII (FVIII) from degradation by forming VWF-FVIII complex; and to mediate platelet adhesion and aggregation at sites of vascular injury. PMID: 29392565
this study shows that Von Willebrand factor protects against acute CCl4-induced hepatotoxicity through phospho-p38 MAPK signaling pathway inhibition PMID: 28868583
the ADAMTS13-vWF axis is partially involved in the pathophysiology of kidney ischemic reperfusion injury. PMID: 27507004
Type 2N von Willebrand disease variants were associated with decreased VWF secretion and impaired factor VIII binding/stability. PMID: 28581694
identify a critical role for VWF in cerebral inflammation and blood-brain barrier damage after intracerebral haemorrhage PMID: 27782211
Refrigeration-induced binding of VWF to platelets facilitates their rapid clearance by inducing GPIbalpha-mediated signaling. PMID: 29097365
BLOC-2 subunit HPS6 deficiency affects the tubulation and secretion of von Willebrand factor from mouse endothelial cells PMID: 27889498
A novel single-domain antibody against von Willebrand factor A1 domain that interferes with VWF-platelet interactions in vivo. By using this sdAb, show that the A1 domain is pertinent to the participation of VWF in the inflammatory response. PMID: 28642239
These experiments delineate an unexpected pathway in which microbiota-triggered TLR2 signaling alters the synthesis of proadhesive VWF by the liver endothelium and favors platelet integrin-dependent thrombus growth. PMID: 28572286
ADAMTS13 controls vascular remodeling by modifying VWF reactivity during stroke recovery. PMID: 28428179
these novel findings support the hypothesis that conformation of the VWF A domains plays a critical role in modulating macrophage-mediated clearance of VWF in vivo. PMID: 27554083
results revealed localized vascular expression of FVIII and von Willebrand factor and identified lymphatic endothelial cell as a major cellular source of FVIII in extrahepatic tissues. PMID: 27207787
Endothelial cell derivedVWF is the major determinant that mediates VWF-dependent ischemic stroke by promoting postischemic thrombo-inflammation. PMID: 27444201
VWF deficiency reduces the progression of liver fibrosis, suggesting a mechanistic role of elevated plasma VWF levels in cirrhosis PMID: 28527913
von Willebrand factor exerts beneficial effects in a mouse sepsis model via recruitment of neutrophils to inflammatory sites. PMID: 26494840
Staphylococcus lugdunensis binds directly to von Willebrand factor, which proved to be vital for withstanding shear forces and for its adhesion to the vessel wall and cardiac valves. PMID: 26743845
Clinical experimental cerebral malaria progression was delayed, and overall survival was significantly prolonged in VWF(-/-) mice compared with WT controls. PMID: 26511133
in stable compensated heart failure mice, disruptions in endothelial vWF expression and extrusion may reduce the incidence of endocardial thrombosis PMID: 26565707
VWF is expressed in a mosaic pattern in the capillaries of many vascular beds and in the aorta. Hearts of VWF-null mice demonstrate an abnormal endothelial phenotype as well as cardiac dysfunction. PMID: 26744078
SNAP23 Regulates Endothelial Exocytosis of von Willebrand Factor PMID: 26266817
Both platelet-VWF and plasma-VWF are required for optimal platelet-derived FVIII gene therapy for hemophilia A in the presence of inhibitors. PMID: 25955153
a genetic link between EGLN1 and VWF in a constitution specific manner which could modulate thrombosis/bleeding susceptibility and outcomes of hypoxia, is reported. PMID: 26047609
novel findings demonstrate a specific and critical role for the R1205 residue in modulating macrophage-mediated clearance of VWF in vivo PMID: 25690668
Clearance differences between blood group O and non-blood group O individuals may therefore be related to the blood group status of the individual rather than the ABH antigen loading on VWF itself. PMID: 25650553
Certain VWD-type 2B mutations relieve the need for shear stress to induce LRP1 binding. Enhanced LRP1 binding coincides with a reduced survival of VWF/p.R1306Q and VWF/p.V1316M PMID: 25728415
These data suggest that whereas platelet-derived VWF does not play a crucial role in hemostasis and arterial thrombosis, it aggravates thrombo-inflammatory diseases such as stroke via a GPIb-dependent mechanism. PMID: 26209660
Platelet-endothelial interactions occur in early atherosclerosis. These interactions are in part caused by endothelial von Willebrand factor large multimers, which can be reversed with exogenous ADAMTS13. PMID: 26156014
Data suggest that targeting platelet receptor glycoprotein Ibalpha (GPIbalpha)-von Willebrand factor VWF-A1 binding interface may offer a therapeutic approach to reducing platelet-driven thrombosis. PMID: 25293780
Absence of vWF increases hematopoiesis in long-term bone marrow cultures and has a protective effect in irradiated lungs. PMID: 24982209
VWF-binding protein contributes to vascular adhesion of S aureus through 2 independent mechanisms: shear-mediated binding to VWF and activation of prothrombin to form S aureus-fibrin-platelet aggregates. PMID: 24951431
a delayed and markedly reduced thrombogenic response was still evident in VWF(-/-), GPVI, and alpha2beta1 blocked animals, suggesting that alternative primary hemostatic mechanisms can partially rescue the bleeding phenotype associated with these defects. PMID: 25051961
a fragment containing only approximately 20% of the VWF sequence is sufficient to support FVIII stability in vivo PMID: 24850761
Expression of VWF/p.S1494C-p.A1534C in mice triggers an acute onset of thrombotic thrombocytopenic purpura. PMID: 24713928
Following endothelial damage, platelet cross-linking during closure of the vessel lumen is mediated by GPIbalpha-VWF interactions. PMID: 24553181
The results indicate that elevation of extracellular sodium within the physiological range raises vWF sufficiently to increase coagulability and risk of thrombosis. PMID: 24733925
Galpha12 may play an important role in promoting membrane trafficking and exocytosis for basal and thrombin-induced vWF secretion, in a process involving SNAP, Galpha12/13 and Galphaq/11 PMID: 24081657
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
VWF represents a promising target for the treatment of cutaneous inflammation, e.g., leukocytoclastic vasculitis. PMID: 23812299
VWF has a role in leukocyte recruitment with chromatin decondensation by PAD4, which increases myocardial ischemia/reperfusion injury in mice PMID: 24200682
Platelet aggregation, secretion, and spreading were diminished due to inhibition of integrin alphaIIbbeta3 in platelets from mice expressing a vWD-type 2B-associated vWF (vWF/p.V1316M). PMID: 24270421
a new function for VWF in vivo as regulator of bloodstream thrombopoiesis PMID: 23737952
VWF type 2B binds to platelets, which is a signal for clearance by macrophages, possibly contributing to thrombocytopenia PMID: 23945153
VWF deficiency confers partial preservation of blood brain barrier integrity after hypoxia/reoxygenation and seizures. PMID: 23825365
Compared with wild-type mice (n=6), we found less bacteria in postcapillary (60+/-6 versus 32+/-5 bacteria) and collecting venules (48+/-5 versus 18+/-4 bacteria; P<0.05) of VWF knockout mice (n=5). PMID: 23720451
Hypoxia is associated with a phenotypic shift which target regulation of VWD in lung endothelial cells. PMID: 23580145
These findings implicate a role for intronic splicing in mediating lineage-specific expression of vWF in the endothelium. PMID: 23529929
ADAMTS13 and VWF are causally involved in myocardial ischemia/reperfusion injury. PMID: 22983446
Provide new evidence for ADAMTS13 in reducing VWF-mediated acute cerebral inflammation following ischemic stroke. PMID: 22712744
Endothelial cell (EC) VWF is sufficient to support hemostasis in VWF-/- mice, and VWF produced in megakaryocytes/platelets can also contribute to hemostasis in the absence of EC-derived VWF. PMID: 22642380
study showed O-glycosylations are dispensable for normal VWF multimerization and biosynthesis; it appears that some O-glycosylation sites, particularly the T1255 and T1256 residues, are involved in maintenance of VWF plasma levels and are essential for normal haemostasis PMID: 22616016

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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.