Reactivity | HuSpecies Glossary |
Applications | IHC, mIF |
Clone | 1072103 |
Clonality | Monoclonal |
Host | Mouse |
Conjugate | Unconjugated |
Immunogen | E. coli-derived recombinant human VWF Asp1498-Val1665 Accession # P04275 |
Specificity | Detects recombinant human VWF in Direct ELISA. |
Source | N/A |
Isotype | IgG2b |
Clonality | Monoclonal |
Host | Mouse |
Purity Statement | Protein A or G purified from hybridoma culture supernatant |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution Instructions | Reconstitute lyophilized material at 0.2mg/ml in sterile PBS. For liquid material, refer to CoA for concentration. |
von Willebrand Factor (vWF) is a large, multimeric glycoprotein made by endothelial cells and megakaryocytes. The pre-pro-vWF protein contains 2813 amino acids (aa), which consists of 22 aa signal peptide, 741 aa propeptide, and mature vWF monomer of 2050 aa (1-4). The pro-vWF undergoes dimerization in the endoplasmic reticulum (ER) through C-terminal “cysteine-knot” (CK) domain. The pro-vWF dimmers are transported to Golgi and form multimers by forming disulfide bond in amino-terminal region of the mature form. The proteolytic processing of pro-region also occurs in Golgi. The matured vWF is stored in Weibel-Pallade bodies in endothelial cells and granules in megakaryocytes and platelets. The unusually-large vWF (ulvWF) multimers released from cells are very efficient in binding to platelets to form thrombus. The population of these highly active ulvWF multimers is controlled by a specific protease, ADAMTS13, which cleaves between residues Tyr1605 and Met1606 in the A2 domain of vWF. In the plasma, vWF appears as a series of large and intermediate multimers with molecular masses from several thousand to 500 kDa. vWF also performs hemostatic functions (3-5). In a high shear-stressed environment, vWF undergoes conformational change to expose a binding site for glycoprotein Ib alpha . As a result, vWF facilitates aggregation of platelets. In addition to platelet binding, vWF binds coagulation factor VIII to increase the lifetime of FVIII in plasma. The purified rhvWF-A2 contains the A2 domain of vWF.
Secondary Antibodies |
Isotype Controls |
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