VEGF165 Protein, Human (HEK293, C-His)

VEGF165 Protein is a subtype of Vascular Endothelial Growth Factor A (VEGF-A). VEGF-A is a key member of the VEGF family of cytokines that can promote neovascularization and increase vascular permeability. VEGF165 Protein, Human (HEK293, C-His) is the recombinant human-derived VEGF165 protein, expressed by HEK293 , with C-10*His labeled tag. The total length of VEGF165 Protein, Human (HEK293, C-His) is 165 a.a., with molecular weight of 20-23 kDa.

VEGF165 is a subtype of Vascular Endothelial Growth Factor A (VEGF-A). VEGF-A is a key member of the VEGF family of cytokines, along with VEGF-B, -C, -D, and PGF. VEGF-A participates in angiogenesis, vasculogenesis, and endothelial cell growth, inducing endothelial cell proliferation, promoting cell migration, inhibiting cell apoptosis, and inducing vascular permeability. VEGF-A binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. VEGF-A also binds to NRP1 initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. VEGF165 may be secreted by tumour cells, binds with high affinity to VEGFR-1 and VEGFR-2 receptors^{[1][2][3][4][5][6][7][8]}.

Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. The ED₅₀ this effect is 2.859-2.929 ng/ml, corresponding to a specific activity is ≤3.41×10⁵ units/mg.

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  Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. The ED₅₀ for this effect is 2.929 ng/mL, corresponding to a specific activity is 3.41×10⁵ units/mg.

Human

HEK293

C-10*His

P15692-4 (A27-R191)

7422  [NCBI]

Partial

APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR

Approximately 20-23 kDa, based on SDS-PAGE under reducing conditions.

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  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 300 mM NaCl, pH 7.4.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Vempati P, et al. Extracellular regulation of VEGF: isoforms, proteolysis, and vascular patterning. Cytokine Growth Factor Rev. 2014 Feb;25(1):1-19.  [Content Brief]

  [2]. Murphy JF, et al. Vascular endothelial growth factor induces cyclooxygenase-dependent proliferation of endothelial cells via the VEGF-2 receptor. FASEB J. 2001 Jul;15(9):1667-9.  [Content Brief]

  [3]. Dixelius J, et al. Minimal active domain and mechanism of action of the angiogenesis inhibitor histidine-rich glycoprotein. Cancer Res. 2006 Feb 15;66(4):2089-97.  [Content Brief]

  [4]. Glorioso N, et al. Association of ATP1A1 and dear single-nucleotide polymorphism haplotypes with essential hypertension: sex-specific and haplotype-specific effects. Circ Res. 2007 May 25;100(10):1522-9.  [Content Brief]

  [5]. Khayati F, et al. EMMPRIN/CD147 is a novel coreceptor of VEGFR-2 mediating its activation by VEGF. Oncotarget. 2015;6(12):9766-80.  [Content Brief]

  [6]. Ferrara N, et al. Molecular and biological properties of the vascular endothelial growth factor family of proteins[J]. Endocrine reviews, 1992, 13(1): 18-32.

  [7]. Ferrara N, et al. Molecular and biological properties of the vascular endothelial growth factor family of proteins. Endocr Rev. 1992 Feb;13(1):18-32.  [Content Brief]

  [8]. Terman BI, et al. Identification of the KDR tyrosine kinase as a receptor for vascular endothelial cell growth factor. Biochem Biophys Res Commun. 1992 Sep 30;187(3):1579-86.  [Content Brief]