Shop Now Contact

Recombinant Human VEGF-165 Protein

Cat # Size Price Quantity
63100120 µg$295
631002100 µg$610
631003500 ug$1450

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile 20mM Tris, 150mM NaCl, pH 8.0
Expression HostHEK293
Target NameVEGFA165, VEGFA, MVCD1, VEGF, Vascular permeability factor (VPF)
SpeciesHuman
accession numberP15692-4
SourcesA DNA sequence encoding the human / cynomolgus VEGF165 isoform (P15692-4) (Met1-Arg191) was expressed. Human and Cynomolgus VEGF165 sequences are identical.
Molecular WeightThe recombinant human / cynomolgus VEGF165 consists of 165 amino acids and predicts a molecular mass of 19.2 KDa. It migrates as an approximately 22 kDa and 24 kDa band in SDS-PAGE under reducing conditions.
Affinity TagNone
Purity≥ 95 % as determined by SDS-PAGE. ≥ 95 % as determined by SEC-HPLC.
Regulatory StatusRUO
Endotoxin level<0.01EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Background Information

Human vascular endothelial growth factor 165 (VEGF-165) is a major pro-angiogenic isoform of VEGF-A that plays a central role in blood vessel formation, vascular permeability, and endothelial cell survival. It is particularly important in both physiological processes such as wound healing and embryonic vascular development, and in pathological angiogenesis associated with disease. VEGF-165 is the most abundant and biologically active splice variant of VEGF-A, distinguished by its intermediate size and strong heparin-binding capacity, which influences its distribution in extracellular matrices.


Structurally, VEGF-165 is a disulfide-linked homodimer composed of two identical subunits, each contributing to receptor binding and dimer stabilization. The protein contains distinct domains, including a receptor-binding domain and a heparin-binding domain encoded by the inclusion of exon 7 in its splice form. This structural feature enhances its interaction with extracellular matrix components and co-receptors. VEGF-165 primarily binds to VEGF receptor tyrosine kinases VEGFR-1 (FLT1) and VEGFR-2 (KDR), with VEGFR-2 being the dominant mediator of angiogenic signaling. It can also interact with co-receptors such as neuropilins (NRP1/NRP2), which enhance signaling potency.


VEGF-165 does not have multiple classical ligands; rather, it functions as a ligand itself within the VEGF-A family isoforms. Dysregulation of VEGF-165 expression is strongly implicated in cancer, diabetic retinopathy, age-related macular degeneration, and other disorders characterized by abnormal vascular growth or permeability. Therapeutically, VEGF-165 is a major target of anti-angiogenic strategies, including monoclonal antibodies, receptor decoys, and small-molecule inhibitors. Conversely, controlled delivery of VEGF-165 has been investigated for promoting therapeutic angiogenesis in ischemic heart disease and peripheral vascular disease.

Data Sheets

Recombinant Human VEGF-165 Protein TDS

Frequently Asked Questions

What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.
What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.
How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.
Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.
Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

Have a product or application question? Consult our FAQs or contact us.