Recombinant human VEGFC protein (ab155739)
Key features and details
- Expression system: HEK 293 cells
- Purity: > 95% SDS-PAGE
- Endotoxin level: < 1.000 Eu/µg
- Active: Yes
- Tags: His tag C-Terminus
- Suitable for: Functional Studies, SDS-PAGE
Description
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Product name
Recombinant human VEGFC protein
See all VEGFC proteins and peptides -
Biological activity
Immobilized Human VEGF R3, Fc Tag at 5 μg/mL (100 μL/well) can bind Human VEGF-C, His Tag with a linear range of 2-20 ng/mL.
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Purity
> 95 % SDS-PAGE.
Purified by Immobilized metal affinity chromatography. -
Endotoxin level
< 1.000 Eu/µg -
Expression system
HEK 293 cells -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
TEETIKFAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGVATNTFF KPPCVSVYRCGGCCNSEGLQCMNTSTSYLSKTLFEITVPLSQGPKPVTIS FANHTSCRCMSKLDVYRQVHSIIRR -
Predicted molecular weight
15 kDa including tags -
Amino acids
103 to 227 -
Tags
His tag C-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab155739 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Functional Studies
SDS-PAGE
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Form
Lyophilized -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
pH: 7.40
Constituents: 95% PBS, 5% Trehalose
Normally Mannitol or Trehalose are added as protectants before lyophilisation.This product is an active protein and may elicit a biological response in vivo, handle with caution.
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ReconstitutionReconstitute with sterile deionized water to a concentration of 250 µg/ml.
General Info
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Alternative names
- Flt 4L
- Flt4 ligand
- FLT4 ligand DHM
see all -
Function
Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors. -
Tissue specificity
Spleen, lymph node, thymus, appendix, bone marrow, heart, placenta, ovary, skeletal muscle, prostate, testis, colon and small intestine and fetal liver, lung and kidney, but not in peripheral blood lymphocyte. -
Sequence similarities
Belongs to the PDGF/VEGF growth factor family. -
Post-translational
modificationsUndergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGF-C first form an antiparallel homodimer linked by disulfide bonds. Before secretion, a cleavage occurs between Arg-227 and Ser-228 producing an heterotetramer. The next extracellular step of the processing removes the N-terminal propeptide. Finally the mature VEGF-C is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions. -
Cellular localization
Secreted. - Information by UniProt
Images
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Functional Studies - Recombinant human VEGFC protein (ab155739)Immobilized Human VEGF-C, His Tag at 2 µg/mL (100 µL/well) can bind Biotinylated Human VEGF R1, His,Avitag with a linear range of 0.02-0.625 µg/mL.
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Functional Studies - Recombinant human VEGFC protein (ab155739)Immobilized Human VEGF R3, Fc Tag at 5 µg/mL (100 µL/well) can bind Human VEGF-C, His Tag with a linear range of 2-20 ng/mL. -
SDS-PAGE - Recombinant human VEGFC protein (ab155739)SDS-PAGE analysis of reduced ab155739 stained overnight with Coomassie Blue.
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab155739 has not yet been referenced specifically in any publications.
