VEGFB Antibody
Description
Biological Role of VEGF-B and Antibody Targeting
VEGF-B binds to VEGF receptor 1 (VEGFR-1) and neuropilin-1, promoting endothelial cell proliferation and survival. Its overexpression is linked to pathological angiogenesis in cancers and retinopathies. Anti-VEGF-B antibodies inhibit these interactions, reducing abnormal blood vessel formation and improving therapeutic outcomes in combination with chemotherapy .
Preclinical Efficacy of 2H10 Antibody
A murine monoclonal antibody (2H10) targeting VEGF-B demonstrated:
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High specificity: 94.2–96.5% immunoreactivity in binding assays with VEGF-B-conjugated Sepharose .
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Stability: Retained 70–72.9% activity in human serum after 8 days at 37°C .
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Therapeutic synergy: Enhanced tumor perfusion and chemotherapy delivery in murine models by normalizing vasculature .
Table 1: Radioconjugate Performance of 2H10 Anti-VEGF-B Antibody
| Parameter | ¹²⁵I-2H10 | ¹¹¹In-2H10 |
|---|---|---|
| Immunoreactivity | 94.2% | 96.5% |
| Serum stability (8 days) | 70% | 72.9% |
| Radiochemical purity | >96% | >96% |
Comparative Antibody Validation Challenges
Studies on VEGF-A antibodies highlight variability in specificity and performance, underscoring the importance of rigorous validation for VEGF-B antibodies . For example:
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Only 4/9 tested VEGF-A antibodies reliably detected VEGF in placental and colon tissues .
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Clone-dependent differences in staining patterns (e.g., RB-9031 vs. VG1) emphasize the need for standardized validation protocols .
Clinical Implications
Anti-VEGF-B antibodies are under investigation for:
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Cancer therapy: Reducing tumor vasculature abnormalities to improve drug penetration .
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Metabolic diseases: Modulating VEGF-B’s role in fatty acid uptake and cardiac metabolism .
Challenges and Future Directions
Product Specs
Target Background
- Elevated plasma VEGF-B levels are associated with type 2 diabetes mellitus. PMID: 28523459
- Clinical studies have shown variations in circulating or tissue VEGF-B expression levels in obese individuals compared to lean individuals. PMID: 28798193
- Transgenic overexpression of vascular endothelial growth factor-B in the heart did not protect heart transplants from ischemia-reperfusion injury. PMID: 27588416
- Renal VEGF-B expression correlates with the severity of Diabetic Kidney Disease. PMID: 28190774
- Research indicates that metformin treatment reduces serum vascular endothelial growth factor B (VEGF-B) levels and improves insulin resistance. PMID: 26387747
- Frameshift mutations in the VEGFB gene are linked to stomach and colorectal cancers. PMID: 25633991
- Fluid shear stress induces the synthesis of Insulin growth factor-2 and vascular endothelial growth factor (VEGF) B and D, which in turn activate MMP-12. PMID: 25435370
- MMP9 may activate VEGF-B via the PI3K/Akt signaling pathway. PMID: 25424698
- Vascular endothelial growth factor plays a role in amyotrophic lateral sclerosis. PMID: 24987705
- Low VEGFB and VEGFD gene expression is associated with early-stage non-small cell lung cancer. PMID: 24145997
- Studies suggest that VEGF-B is an angiogenesis factor in vitro and that ERK1/2 and p38-related signaling pathways are involved in these VEGF-B activities. PMID: 24374930
- VEGF-B has potential roles in cardiac protection, energy metabolism support, and neuroprotection. [review] PMID: 24987005
- High VEGF-B levels may be correlated with the presence of hyperlipidemia and target organ damage in type 2 diabetic patients. PMID: 25001655
- High VEGFB expression is associated with bone marrow metastasis in neuroblastoma. PMID: 23553333
- VEGF-B may be an important ligand in the signaling between the tumor and preexisting blood vessels, ensuring a functional blood supply for tumor survival. PMID: 23417498
- Research shows significant associations between certain VEGF (VEGF-B) family members and overall survival and distant failure. PMID: 23728940
- Data indicate that three microRNAs (miR-484, -642, and -217) can predict chemoresistance and vasculature of serous epithelial ovarian carcinomas through regulation of the VEGFB and VEGFR2 pathways. PMID: 23697367
- Expression of VEGF-B genes in the glioma cell line U87 is significantly altered under hypoxia and ischemic conditions. PMID: 23350126
- In WT1 mutant cells, reduced VEGF(165)b is attributed to a lack of WT1-mediated transcriptional repression of the splicing-factor kinase SRPK1. PMID: 22172722
- Analysis of vascular endothelial growth factor-B binding by VEGFR-1(D2) is reported. PMID: 20501651
- TIMP3 inhibits the binding of VEGF to VEGF receptor-2 and blocks downstream signaling and angiogenesis. PMID: 12652295
- This research describes the crystal structure of human vascular endothelial growth factor-B (VEGF-B) and presents a predicted model for the interaction of VEGF-B with the second domain of its receptor, VEGFR-1. PMID: 16616187
- Basophils may play a role in angiogenesis and inflammation through the expression of various forms of VEGF-B and their receptors. PMID: 17082651
- VEGFB, and its receptor, were highly expressed in dysplastic neurons. Immunoreactivity (IR) in astroglial and balloon cells was observed for VEGFA and its receptors. Double-labeling also showed expression of VEGFA, VEGFB, and VEGFR-1 in cells of the microglia/macrophage lineage. PMID: 18317782
- VEGF-B appears to have limited angiogenic activity in the ischemic heart. PMID: 18511699
- Increased VEGFB expression is associated with hepatocellular carcinoma. PMID: 18537151
- Overexpression of vascular endothelial growth factor-B in the mouse heart alters cardiac lipid metabolism and induces myocardial hypertrophy. PMID: 18757827
- This study presents the structural features of the highly ordered interaction of the Fab fragment of the antibody (Fab-2H10) with VEGF-B. PMID: 18930733
- VEGF-B mRNA was not detected in either normal urothelium or bladder cancer. PMID: 19424629
Customer Reviews
Applications : Western Blot (WB)
Sample type: tissue
Sample dilution: 1：2000
Review: I used the CSB-PA025834LA01HU antibody for WB detection. The mouse liver tissue tested was processed according to the conventional protein extraction process without special processing. The results are as follows, not bad.
