Home Biosimilar Antibodies Angiogenesis VEGFR null Ramucirumab (anti-VEGFR2) For research use only.
Not for use in humans.

Ramucirumab (anti-VEGFR2)

Synonyms: IMC-1121B, LY3009806, IMC-1121

Ramucirumab is a monoclonal antibody of the IgG1 class that binds to VEGF-R2 and prevents its activation. The IC50 value for blocking KDR binding to VEGF is 0.8 nM for ramucirumab, MW: 143.6 KD.

Ramucirumab (anti-VEGFR2)

Click to purchase the isotype control of Ramucirumab (anti-VEGFR2)

Selleck's Ramucirumab (anti-VEGFR2) has been cited by 3 publications

Purity & Quality Control

Batch: A200301 Purity: 99.4% Protein concentration: 5mg/ml Endotoxin Level: ≤1 EU/mg
99.4

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1. "+" indicates inhibitory effect. Increased inhibition is marked by a higher "+" designation. 2. "✔" indicates inhibitory effect, but without specific value.

Biological Activity

Description Ramucirumab is a monoclonal antibody of the IgG1 class that binds to VEGF-R2 and prevents its activation. The IC50 value for blocking KDR binding to VEGF is 0.8 nM for ramucirumab, MW: 143.6 KD.
Targets
KDR/VEGF interaction [5]
0.8 nM
In Vitro
In vitro

Ramucirumab is direct inhibitor of VEGF-R2, where it binds to the extracellular VEGF-binding domain with high degree of specificity and affinity, at picomolar dose range. It thus prevents the binding of the VEGF ligand to the VEGF-R2 receptor. Ramucirumab has potential advantages over bevacizumab as it is selective for VEGF-R2, whereas bevacizumab by targeting VEGF-A affects VEGF-R1, -R2, and the noncatalytic coreceptors neuropilin-1and -2[1]. Ramucirumab prevents the binding of VEGFR ligands: VEGF-A, VEGF-C, and VEGF-D to its receptors. Thus, ramucirumab inhibits the angiogenesis pathways involved in the development and progression of gastric cancer[2]. ramucirumab demonstrates inhibition of VEGF-stimulated VEGFR-2 activation, proliferation of human endothelial cells, VEGF migration of human leukemia cells, and VEGF induced phosphorylation of VEGFR-2 in human umbilical vein and porcine aortic endothelial cells overexpressing VEGFR-2[3]. Preclinical in vitro data revealed that ramucirumab has a high affinity for VEGFR-2, showing a half-maximal effective concentration (EC50) of 0.15 nM, 8- to 9-fold higher than its natural ligand VEGFA. Ramucirumab binds VEGFR-2 in domain 3 near the N-terminus, both as a soluble protein and as a cell-surface receptor, with a IC50 of 1-2 nM[4].
Cell Research:

The anti-KDR antibodies were added to the microwells of a 96-well plate coated with KDR(Ig1-7) (full-length KDR ECD), KDR(Ig1-3) (variant that contains only the first three N-terminal Ig domains of KDR ECD), or KDR(Ig1) (variant that contains only the first N-terminal Ig domain of KDR ECD) and incubated at room temperature for 1 h. The plate was washed and then incubated with a mouse anti-human Fc antibody-HRP conjugate for additional 1 h, after which the plate was developed as described above. Antibody binding to the two Ig deletion variants are shown as relative (as percentages) to their binding to the full-length KDR ECD.
In Vivo
In vivo In preclinical studies, ramucirumab concentrations of >20 μg/mL were associated with anticancer activity[1]. And ramucirumab potently inhibited VEGF binding to VEGFR-2 with a binding affinity constant of ramucirumab to VEGFR-2 of 5 × 10-11 M. Pharmacokinetic evaluation has demonstrated a nonlinear pharmacokinetic, with incremental doses of this agent being associated with a decrease in clearance. Ramucirumab has a half-life of 200-300 h[3]. Preclinical studies were also to be conducted in mice, but interspecies receptor differences made ramucirumab inactive in preclinical mouse models[4].

Product Details

CAS No. 947687-13-0
Isotype human IgG1
Formulation PBS buffer, pH 7.2
Storage
(From the date of receipt)		 Store the undiluted solution at 4°C in the dark to avoid freeze-thaw cycles

Comparison of Clones for

*Literature analysis of various clone (for this target) products available on the market shows that Selleck's selected clones are more frequently applied. (data until September 2024)

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