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vWF

  • Official Full Name

    von Willebrand factor

  • Overview

    The glycoprotein encoded by this gene functions as both an antihemophilic factor carrier and a platelet-vessel wall mediator in the blood coagulation system. It is crucial to the hemostasis process. Mutations in this gene or deficiencies in this protein result in von Willebrands disease. An unprocessed pseudogene has been found on chromosome 22. [provided by RefSeq, Jul 2008]
  • Synonyms

    VWF; von Willebrand factor; VWD; F8VWF; coagulation factor VIII VWF;

  • Recombinant Proteins
  • Cell & Tissue Lysates
  • Native Proteins
  • Transfected Stable Cell Lines
  • Protein Pre-coupled Magnetic Beads
  • Dog
  • Human
  • Mouse
  • Pig
  • Rat
  • Rhesus Macaque
  • Zebrafish
  • CHO
  • E.coli
  • HEK293
  • Human plasma
  • Mamanlian cells
  • Mammalian Cell
  • Sf9 Insect Cell
  • Yeast
  • C
  • His
  • DDK
  • Flag
  • His (Fc)
  • Avi
  • Myc
  • His|Myc
  • Met|His
  • N/A
  • N
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human VWF-2712H Active Recombinant Human VWF protein, Met/His-tagged E.coli Met/His
Human VWF-894H Recombinant Human VWF, His tagged CHO His Met 1-Lys 2813
Human VWF-126H Recombinant Human Von Willebrand Factor E.coli N/A
Human VWF-2713H Recombinant Human VWF, DDK-tagged Sf9 Insect Cell DDK Met-Ala2200-Lys2813
Human VWF-2714H Recombinant Human VWF, DDK-tagged Sf9 Insect Cell DDK Met-Ser764-Ser1263
Human VWF-001HCL Recombinant Human VWF cell lysate CHO N/A
Human VWF-6569H Recombinant Human VWF Protein (Ala23-Lys219), N-His tagged E.coli N-His Ala23-Lys219
Human VWF-17H Native Human von Willebrand Factor, Factor VIII Free Human plasma N/A
Human VWF-30H VWF Factor Reference standard N/A
Human VWF-2543H Recombinant Human VWF protein(1491-1900 aa), C-His-tagged E.coli C-His 1491-1900 aa
Human VWF-5435HFL Recombinant Full Length Human VWF, Flag-tagged Mamanlian cells Flag
Human VWF-369H Native Human Von Willebrand Factor Human plasma N/A
Mouse Vwf-1432M Recombinant Mouse Vwf protein, His-tagged E.coli His Asp1498~Val1665
Mouse VWF-18420M Recombinant Mouse VWF Protein, His tagged HEK293 N-His
Mouse VWF-10101M-B Recombinant Mouse VWF Protein Pre-coupled Magnetic Beads HEK293
Mouse VWF-10101M Recombinant Mouse VWF Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Mouse VWF-2643M Recombinant Mouse VWF Protein (1498-1665 aa), His-Myc-tagged Yeast His/Myc 1498-1665 aa
Mouse Vwf-3758M Recombinant Mouse Vwf protein, His&Myc-tagged E.coli His&Myc 1498-1665aa
Rat Vwf-7788R Recombinant Rat Vwf protein, His-tagged E.coli His Lys49~Asn230
Rat Vwf-7789R Recombinant Rat Vwf protein, His-tagged E.coli His Ser269~Pro367 (Accession # Q62935)
Dog VWF-4940D Recombinant Dog VWF protein, His-tagged E.coli His Arg34~Leu240
Rhesus Macaque VWF-5183R Recombinant Rhesus monkey VWF Protein, His-tagged Mammalian Cell His
Rhesus Macaque VWF-4996R-B Recombinant Rhesus Macaque VWF Protein Pre-coupled Magnetic Beads HEK293
Rhesus Macaque VWF-4996R Recombinant Rhesus Macaque VWF Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Zebrafish VWF-8353Z Recombinant Zebrafish VWF Mammalian Cell His
Pig VWF-4903P Recombinant Pig VWF protein, His-tagged E.coli His Asp1167~Val1334
  • Background
  • Quality Guarantee
  • Case Study
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • Other Resource
VWF-9.jpg

Fig1. VWF domain structure. (A) Schematic representation of VWF's domain structure, (B) dimerizing disulfide bonds between the CK domains of two VWF monomers and (C) dimeric bouquet formation. (Achim Löf, 2017)

What is VWF protein?

VWF (von Willebrand factor) gene is a protein coding gene which situated on the short arm of chromosome 12 at locus 12p13. This gene encodes a glycoprotein involved in hemostasis. The encoded preproprotein is proteolytically processed following assembly into large multimeric complexes. These complexes function in the adhesion of platelets to sites of vascular injury and the transport of various proteins in the blood. The VWF protein is consisted of 2813 amino acids and its molecular mass is approximately 309.3 kDa.

What is the function of VWF protein?

This protein is 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 it 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.

VWF Related Signaling Pathway

VWF is a glycoprotein associated with blood clotting disorders and plays a role in the clotting process. VWF binds to the GPIb-IX-V complex on platelets and promotes platelet adhesion and agglutination, thus initiating the signaling pathway for thrombosis. It can also bind to platelet membrane glycoprotein (GP) complexes and subcutaneous collagen, and this interaction mediates platelet adhesion at the site of vascular injury. It is also involved in reticulum formation and thrombosis.

VWF Related Diseases

VWF protein abnormalities can cause a variety of diseases, von Willebrand disease (VWD) is a group of hereditary bleeding disorders that can be divided into three types based on their severity and the degree of functional deficiency of VWF. When VWF function may also be affected, resulting in bleeding tendencies that can cause thrombocytopenic purpura (ITP). It can also cause von Willebrand Disease Type A. When the VWF protein is abnormal, patients may experience symptoms such as easy bruising and difficulty in hemostasis.

VWF-10.jpg

Fig2. Regulation of VWF expression & secretion and diseases. (Yaozu Xiang, 2016)

Bioapplications of VWF

In patients with von Willebrand disease, supplementation of exogenous VWF proteins or coagulation factors may be required to maintain normal clotting function. Because VWD is a genetic disorder, VWF genetic testing and counseling are important for genetic risk assessment and family planning in patients with familial VWD. Intraoperative or daily monitoring of the protein level to avoid the risk of bleeding.

Case study 1: Jirawat Khanongnoi, 2018

Snake venom-metalloproteinases (SVMPs) are the primary factors that disturb hemostasis and cause hemorrhage in the venomous snake bitten subjects. Kaouthiagin is a unique SVMP that binds and cleaves von Willebrand factor (vWF) at a specific peptide bond leading to inhibition of platelet aggregation, which enhances the hemorrhage. Kaouthiagin is a low abundant venom component of Thai cobra (Naja kaouthia); thus, most horse-derived antivenins used for cobra bite treatment do not contain adequate anti-kaouthiagin. This study aimed to produce human single-chain antibody variable fragments (HuscFvs) that bind to and interfere with kaouthiagin activity for further clinical use.

Kaouthiagin was purified from N. kaouthia-holovenom by a single-step gel-filtration chromatography. The selected phages were used to infect Escherichia coli bacteria. Soluble HuscFvs expressed by three phage-transformed-E. coli clones interfered with cobra kaouthiagin binding to human vWF. omputerized simulation indicated that HuscFv of two phage-transformed E. coli clones formed contact interface with kaouthiagin residues at or near catalytic site and effectively inhibited fibrinogenolytic activity of the kaouthiagin.

VWF-3.jpg

Fig1. Western blotting patterns of the SDS-PAGE-separated fractions 44–56 probed with 1 μg/mL of recombinant human von Willebrand factor (vWF).

VWF-4.jpg
Fig2. Results of HuscFv-mediated inhibition of von Willebrand factor (vWF) binding to kaouthiagin by Western blot analysis.

Case study 2: Yingxue Qi, 2018

Platelet glycoprotein Ibα (GPIbα) extracellular domain, which is part of the receptor complex GPIb-IX-V, plays an important role in tumor metastasis. However, the mechanism through which GPIbα participates in the metastatic process remains unclear. The researchers established a series of screening models and obtained rat anti-mouse GPIbα monoclonal antibodies (mAb) 1D12 and 2B4 that demonstrated potential value in suppressing cancer metastasis. 1D12 and 2B4 affected the von Willebrand factor (vWF)-GPIbα interaction via binding to GPIbα aa 41-50 and aa 277-290 respectively, which markedly inhibited the interaction among platelets, tumor cells, and endothelial cells in vitro, and reduced the mean number of surface nodules in the experimental and spontaneous metastasis models in vivo.

VWF-5.jpg

Fig3. The vWF binding was inhibited by 2B4 and 1D12 and detected by flow cytometry. Binding of vWF was detected with FITC-conjugated mouse vWF IgG by flow cytometry and quantitated by mean fluorescence intensity.

VWF-6.jpg
Fig4. YQ3 inhibits adhesion and cancer cell-induced platelet activation. The vWF binding was inhibited by YQ3 detected by flow cytometry.
VWF-7.jpg

Fig1. Diagram of cellular pathways activated by SARS-CoV-2 S protein and the targets for pharmacological interference. (Alicia Villacampa, 2024)

VWF-8.jpg

Fig2. Coronary ruptured site and thrombus interface. (Atsushi Yamashita, 2021)

vWF involved in several pathways and played different roles in them. We selected most pathways vWF participated on our site, such as PIK-Akt signaling pathway, Focal adhesion, ECM-receptor interaction, which may be useful for your reference. Also, other proteins which involved in the same pathway with vWF were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein
PIK-Akt signaling pathwayPRLR;IRS1;PPP2R5A;FGF11;ANGPT4;IFNA10;FGF16;PRKAA1;Pdgfa&Pdgfb
Focal adhesionCOL2A1A;CDC42;MYLPF;MLCK2;MYL2B;CAPN2B;GSK3AA;COL5A2A;RHOA
ECM-receptor interactionITGA10;SV2B;GP6;ITGA3;COL11A1A;COL5A2;THBS3;THBS2;THBS3A
Complement and coagulation cascadesSERPINA1;F11;F12;SERPINA5;PLAUR;CFH;GM5077;C1QC;Serpina1c
Platelet activationPTGS1;SRC;ROCK2;PLA2G4F;VWF;MYLK2;STIM1;MYLK3;PIK3R2

vWF has several biochemical functions, for example, chaperone binding, collagen binding, glycoprotein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by vWF itself. We selected most functions vWF had, and list some proteins which have the same functions with vWF. You can find most of the proteins on our site.

Function Related Protein
chaperone bindingVWF;BAK1;TBCE;TIMM9;DNAJA3B;DNAJB6;BIRC5;GNB5;SLC25A17
collagen bindingLACRT;CTSS;Pdgfa&Pdgfb;CCBE1;C1QTNF1;TLL1;MMP13;SMAD3;HSD17B12
glycoprotein bindingCNTN1;ITGA3;BBC3;DNAJC5;Shh;DNAJA2;SERPINA1A;BMPR1A;CD4
identical protein bindingCALHM1;LUC7L;PRPF19;CD247;PITX2;CD74;APOA1;MICU1;TRIM39
immunoglobulin bindingcgr2b;HRG;VWF
integrin bindingNpnt;DMP1;COL3A1;KDR;THBS4;ITGB1BP2;WISP3;VCAM1;COL5A1
protease bindingITGB3;CCDC71L;NDUFS7;TIMP2B;C10orf2;XBP1;TIMP3;SERPINA5;CD70
protein N-terminus bindingSTX1A;BIRC2;PEX14;PHB2;MAU2;KCNIP2;SERPINB1A;HDAC1;PPP1CC
protein bindingMTNR1B;ARNTL1B;PHF17;MAU2;MED24;PURA;DCTN4;EIF1AX;EIF4H
protein homodimerization activityGHR;ATP2A1;CD247;G6PDX;LSM1;STC2;DPYD;KIT;IDH1

vWF has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with vWF here. Most of them are supplied by our site. Hope this information will be useful for your research of vWF.

GP1BA; ADAMTS13

Research Area

Related articles

Timm, A; Hillarp, A; et al. Comparison of automated von Willebrand factor activity assays. THROMBOSIS RESEARCH 135:684-691(2015).
Tomlinson, RE; Silva, MJ; et al. HIF-1 alpha regulates bone formation after osteogenic mechanical loading. BONE 73:98-104(2015).
  • Q&As
  • Reviews

Q&As (6)

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How can treatment be used to change the level or function of the VWF protein? 09/15/2022

There is currently no treatment that directly targets the VWF protein. However, some medications can improve the patient's clotting status and reduce the risk of bleeding. For example, the use of recombinant human coagulation factor VIII. can replace the deficient factor VIII and improve coagulation function. In addition, the use of antifibrinolytic drugs can inhibit the degradation of fibrin and maintain the stability of the coagulation process.

What is the relationship between VWF protein and coagulation factor VIII? 04/28/2022

VWF protein is closely related to coagulation factor VIII. Coagulation factor VIII. is a serine protease that plays a key role in the coagulation process. VWF protein can act as a cofactor for coagulation factor VIII., accelerating the coagulation process. In addition, VWF protein can also inhibit the activity of plasminogen activators, thereby inhibiting the degradation of fibrin and maintaining the stability of the coagulation process.

How does VWF play a role in hemostasis? 10/24/2020

In the process of hemostasis, the role of VWF protein is mainly to promote platelet adhesion and aggregation. When platelets bind to VWF protein, morphological changes occur and the phospholipid surface is exposed, which interacts with other platelets or endothelial cells to form platelet thrombosis and play a hemostatic role.

Is VWF protein related to other coagulation factors? 04/21/2020

There is a complex interaction between VWF protein and other coagulation factors. For example, VWF proteins can bind to glycoprotein II.b/III.a receptors on the surface of platelets, promoting platelet adhesion and aggregation.

What is the association between genetic variation in VWF protein and disease? 03/29/2020

Genetic variations in the VWF protein can lead to coagulation disorders such as von Willebrand disease (VWD). Some variants can cause VWF protein deficiency or dysfunction, which can affect the ability of platelets to adhere and aggregate, increasing the risk of bleeding. Understanding these variants can help diagnose and classify different subtypes of VWD.

What is the function of VWF protein in blood? 02/10/2020

The main function of VWF protein in blood is to promote platelet adhesion and aggregation, thereby participating in the process of hemostasis and coagulation. In addition, VWF protein can also act as a regulator of endothelial cells and participate in the repair and remodeling of blood vessel walls.

Customer Reviews (3)

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Reviews
08/25/2022

    Strong activity, a small amount can play a role, save reagents.

    03/31/2021

      It has been used in experiments, and the results are accurate and reliable.

      02/10/2021

        No significant difference was found between different batches, and the repeatability between batches was good.

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