SRP0348
Flt1 active human
recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE)
别名:
VEGFR1, fms-related tyrosine kinase 1 (vascular endothelial growth factor/vascular permeability factor receptor)
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关于此项目
NACRES:
NA.32
UNSPSC Code:
12352200
Form:
aqueous solution
Assay:
≥70% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in baculovirus infected Sf9 cells
Mol wt:
67.5 kDa
biological source
human
recombinant
expressed in baculovirus infected Sf9 cells
assay
≥70% (SDS-PAGE)
form
aqueous solution
mol wt
67.5 kDa
packaging
pkg of 10 μg
technique(s)
activity assay: suitable, inhibition assay: suitable
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... FLT1(2321)
General description
Human Flt1 ( GenBank Accession No. AF063657), amino acids 783-end with N-terminal His-tag, MW=67.5 kDa, expressed in a Baculovirus infected Sf9 cell expression system.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Other Notes
One unit is defined as the amount of enzyme that will transfer 1 nmol phosphate to the tyrosine substrate per minute at pH 7.4 and 30°C.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
存储类别
6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
M Shibuya
The international journal of biochemistry & cell biology, 33(4), 409-420 (2001-04-20)
Vascular endothelial growth factor receptor-1 (VEGFR-1/Flt-1) is structurally a typical tyrosine kinase receptor of about 180 kDa, and carries seven Ig-like domains in the extracellular region and a tyrosine kinase domain with a long kinase insert. Recent studies have revealed
N Rahimi et al.
The Journal of biological chemistry, 275(22), 16986-16992 (2000-04-05)
Vascular endothelial growth factor (VEGF) provokes angiogenesis in vivo and stimulates growth and differentiation of endothelial cells in vitro. Although VEGF receptor-1 (VEGFR-1) and VEGFR-2 are known to be high affinity receptors for VEGF, it is not clear which of
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