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ChemicalBook--->CAS DataBase List--->110590-64-2

110590-64-2

110590-64-2 Structure

110590-64-2 Structure
IdentificationBack Directory
[Name]

TYR-ILE-GLY-SER-ARG
[CAS]

110590-64-2
[Synonyms]

YIGSR
LAMININ FRAGMENT
Laminin (929-933)
TYR-ILE-GLY-SER-ARG
LAMININ PENTAPEPTIDE
LAMININ FRAGMENT 929-933
H-TYR-ILE-GLY-SER-ARG-OH
TYR-ILE-GLY-SER-ARG USP/EP/BP
Tyr-Ile-Gly-Ser-Arg >=97% (HPLC)
TYR-ILE-GLY-SER-ARG-NH2: YIGSR-NH2
LAMININ B1 CHAIN PENTAPEPTIDE FRAGMENT
tyrosyl-isoleucyl-glycyl-seryl-arginine
Laminin beta-1 Chain (929-933) (human, mouse)
Tyrosinyl-isoleucinyl-glycinyl-serinyl-arginine
L-Arginine, L-tyrosyl-L-isoleucylglycyl-L-seryl-
Laminin β-1 Chain (929-933) (human, mouse), YIGSR
LaMinin b-1 Chain (929-933) (huMan, Mouse), YIGSR
Laminin β-1 Chain (929-933) (human, mouse), YIGSR
Laminin β-1 Chain (929-933) (human, mouse) Tyr-Ile-Gly-Ser-Arg
L-Arginine, N2-(N-(N-(N-L-tyrosyl-L-isoleucyl)glycyl)-L-seryl)-
[Molecular Formula]

C26H42N8O8
[MDL Number]

MFCD00076472
[MOL File]

110590-64-2.mol
[Molecular Weight]

594.66
Chemical PropertiesBack Directory
[Melting point ]

126-129 °C
[density ]

1.44±0.1 g/cm3(Predicted)
[storage temp. ]

-20°C
[solubility ]

H2O: soluble1mg/mL, clear, colorless
[form ]

Solid
[pka]

3.23±0.10(Predicted)
[color ]

White to off-white
[biological source]

synthetic (organic)
[Water Solubility ]

H2O: soluble 1mg/mL, clear, colorless
Safety DataBack Directory
[WGK Germany ]

3
Hazard InformationBack Directory
[Uses]

Tyr-Ile-Gly-Ser-Arg (YIGSR) can be used at the interface between the conjugated polymer and the tissue for the engineering of tissue interface. The product can also be used to study the role of integrins β1, α6, and α3 in promoting type II epithelial differentiation during lung maturation in the fetus.
[Biochem/physiol Actions]

Tyr-Ile-Gly-Ser-Arg (YIGSR) is a pentapeptide of the protein laminin that reduces the lung colony formation in mice administered with melanoma cells as well as can block the invasiveness of the cells in vitro. It inhibits the increased expression of endothelial nitric-oxide synthase in primary porcine aortic endothelial cells.
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