KDR, CD309, FLK1, VEGFR, VEGFR2
Recombinant Human VEGFR2 /KDR MS Standard Protein, C13 and N15-labeled (VEGFR2 / KDR, Heavy Labeled) Met 1 - Glu 764 (Accession # AAI31823) was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain >99% incorporation efficiency at ACROBiosystems.
VEGFR2 / KDR, Heavy Labeled is fused with polyhistidine tag at the C-terminus, and has a calculated MW of 86.2 kDa. The predicted N-terminus is Met 1. DTT-reduced Protein migrates as 100-110 kDa in SDS-PAGE due to glycosylation.
VEGFR2 / KDR, Heavy Labeled is labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
Less than 1.0 EU per μg of the VEGFR2 / KDR, Heavy Labeled by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.
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See Certificate of Analysis for details of reconstitution instruction and specific concentration.
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).
Kinase insert domain receptor (KDR) is also known as CD309, FLK1, VEGFR, VEGFR2, and is one of the subtypes of VEGFR. VEGF receptors are receptors for vascular endothelial growth factor (VEGF). There are three main subtypes of VEGFR, numbered 1, 2 and 3. The VEGF receptors have an extracellular portion consisting of 7 immunoglobulin-like domains, a single transmembrane spanning region and an intracellular portion containing a split tyrosine-kinase domain. VEGF-A binds to VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1). VEGFR-2 appears to mediate almost all of the known cellular responses to VEGF.The function of VEGFR-1 is less well defined, although it is thought to modulate VEGFR-2 signaling. Another function of VEGFR-1 may be to act as a dummy/decoy receptor, sequestering VEGF from VEGFR-2 binding (this appears to be particularly important during vasculogenesis in the embryo). In addition, VEGFR2 is able to interact with HIV-1 extracellular Tat protein upon VEGF activation, and seems to enhance angiogenesis in Kaposi's sarcoma lesions.
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