Volociximab Biosimilar, Anti-human Integrin α5β1 Monoclonal Antibody
The cheapest research grade volociximab biosimilar (anti-human integrin α5β1 monoclonal antibody, mAb) for ELISA, neutralization, in vivo functional assays such as bioanalytical PK and ADA assays, and those in vitro and in vivo assays for studying biological pathways affected by volociximab. The research grade volociximab biosimilar protein is for research use only.
Synonyms: integrin α5β1, integrin alpha 5 beta 1, fibronectin receptor, ITGA5, CD49e, ITGB1, CD29
产品参数
| 货号 | C065P |
|---|---|
| 产品名称 | Volociximab Biosimilar, Anti-human Integrin α5β1 Monoclonal Antibody |
| 供货商名称 | Syd Labs, Inc. |
| 品牌名 | Syd Labs |
| 同种型 | Human IgG4 kappa. |
| 来源 | The anti-human integrin α5β1 monoclonal antibody volociximab biosimilar was produced in the volociximab biosimilar CHO stable cell line. |
| 特异性 | The in vivo grade volociximab biosimilar specifically binds to the human integrin α5β1. |
| 抗体形式 | 0.2 uM filtered solution, pH 6.0, no stabilizers or preservatives. |
| 内毒素 | < 0.1 EU per 1 ug of the protein by the LAL method. |
| 纯度 | >95% by SDS-PAGE under reducing conditions and HPLC. |
| 运输 | The research grade volociximab biosimilar is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below. |
| 稳定性与存储 | Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70°C as supplied. 1 month from date of receipt, 2 to 8°C as supplied. |
| 产品咨询 | Syd Labs在国内只通过代理商销售其产品，不做直销。终端用户咨询价格请联系Syd Labs中国代理商。 关于Syd Labs产品如果有任何技术或其它问题，欢迎随时联系Syd Labs国内市场推广合作伙伴：武汉多找找科技有限公司，企业微信：duozhaozhao2024 联系电话：18162581039（龙经理） |
文献
C065P: Volociximab Biosimilar (Research Grade), Anti-human Integrin α5β1 Monoclonal Antibody
Recombinant Humanized IgG4 Monoclonal Antibody.
Background
Volociximab Biosimilar uses the same protein sequences as the therapeutic antibody volociximab.
Volociximab is a high-affinity IgG4 chimeric (82% human, 18% murine) monoclonal antibody that specifically binds to α5β1 integrin. Integrins are a superfamily of widely expressed transmembrane glycoprotein receptors for extracellular matrix ligands, such as fibronectin, vitronectin, laminin, collagens, and other plasma membrane proteins, and function in the regulation of a broad variety of cellular processes, including embryogenesis, inflammation, bone metabolism, apoptosis, cell proliferation, angiogenesis, and tumor metastasis.
Integrins exist as noncovalent heterodimers comprising α and β subunits. Receptor diversity, function, and versatility in ligand binding is determined by the specific pairing of α and β subunits. The cytoplasmic tail of the β subunit links to the actin cytoskeleton and components of the focal adhesion plaque. The interaction with the focal adhesion plaque can lead to signaling, through different pathways, to influence cell survival, growth, and motility. Consequently, all of these protein associations allow cells to sense and respond to their extracellular environment.
Endothelial cell expression of the α5β1 integrin and the ligand fibronectin are both up-regulated during tumor angiogenesis. The sites of the α5β1 integrin increase in expression and are more accessible in the vasculature during angiogenesis and tumor growth, which is in contrast to normal tissue vasculature. Disruption of α5β1 integrin binding to fibronectin results in the inhibition of angiogenesis and the induction of apoptosis of activated endothelial cells. In preclinical models, selective antagonists targeted to α5β1 integrin inhibit tumor growth.
Relevant preclinical models for the mechanism of action and antitumor activity evaluation were selected based on the cross-reactivity of volociximab to the nonhuman α5β1 homologues. Volociximab and its parent mouse antibody, IIA1, do not cross-react with murine α5β1 integrin, but do cross-react and block the chicken and cynomolgus monkey target protein. Volociximab inhibited human umbilical vein endothelial cells from forming tube-like vessel structures in a three-dimensional fibrin matrix in vitro and was independent of the growth factor stimulus. These data suggest that the α5β1 signaling pathways are downstream of growth factor stimulation. Moreover, volociximab inhibited growth factor–stimulated human neonatal foreskin vascular growth when grafted into severe combined immunodeficient mice in vivo. In addition, volociximab inhibited vessel formation and human tumor xenograft growth in the chicken chorioallantoic membrane model in ovo. Finally, in a preclinical model of choroidal neovascularization in cynomolgus monkeys, volociximab was a potent inhibitor of angiogenesis.