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Merck

T7154

Sigma-Aldrich

Tyr-Ile-Gly-Ser-Arg

≥97% (HPLC)

Synonym(e):

Laminin Fragment 929-933

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About This Item

Empirische Formel (Hill-System):
C26H42N8O8
CAS-Nummer:
Molekulargewicht:
594.66
MDL-Nummer:
UNSPSC-Code:
12352209
PubChem Substanz-ID:
NACRES:
NA.32

Biologische Quelle

synthetic (organic)

Qualitätsniveau

Assay

≥97% (HPLC)

Form

powder

Methode(n)

cell culture | mammalian: suitable

Löslichkeit

H2O: soluble 1 mg/mL, clear, colorless

Lagertemp.

−20°C

SMILES String

CC[C@H](C)[C@H](NC(=O)[C@@H](N)Cc1ccc(O)cc1)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O

InChI

1S/C26H42N8O8/c1-3-14(2)21(34-22(38)17(27)11-15-6-8-16(36)9-7-15)24(40)31-12-20(37)32-19(13-35)23(39)33-18(25(41)42)5-4-10-30-26(28)29/h6-9,14,17-19,21,35-36H,3-5,10-13,27H2,1-2H3,(H,31,40)(H,32,37)(H,33,39)(H,34,38)(H,41,42)(H4,28,29,30)/t14-,17-,18-,19-,21-/m0/s1

InChIKey

MWOGMBZGFFZBMK-LJZWMIMPSA-N

Amino Acid Sequence

Tyr-Ile-Gly-Ser-Arg

Anwendung

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. Wirkung

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.
Tyr-Ile-Gly-Ser-Arg is a fragment of domain III of the laminin B1 chain . It is a major receptor binding site in laminin. It competes with laminin for the cell surface receptor. It is an inhibitor of tumor growth and metastasis.

Angaben zur Herstellung

Tyr-Ile-Gly-Ser-Arg dissolves in water at 1 mg/ml to yield a clear, colorless solution.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Kunden haben sich ebenfalls angesehen

Amer F Alhaj Saleh et al.
Biopolymers, 89(1), 62-71 (2007-09-29)
Cell penetrating peptide based gene carriers are notably known for low level of gene transfer. To remedy this, as laminin receptor (LR) has been previously linked to tumor metastasis, the LR-binding domain (YIGSR) as well as a scrambled sequence (SGIYR)
T Gloe et al.
The Journal of biological chemistry, 274(23), 15996-16002 (1999-05-29)
It has been suggested that the mechanical forces acting on endothelial cells may be sensed in part by cell-matrix connections. We therefore studied the role of different matrix proteins, in particular laminin I, on a shear stress-dependent endothelial response, namely
Praveen K Dubey et al.
Drug delivery, 17(7), 541-551 (2010-06-22)
YIGSR peptide anchored pegylated nanospheres (YIGSR-SN) loaded with 5-fluorouracil (5-FU) were investigated for selective and preferential presentation of carrier contents at angiogenic endothelial cells over-expressing laminin receptors on and around tumor tissue and thus for assessing their targetability. Pegylated nanosphere
Angelo Bella et al.
Journal of medicinal chemistry, 52(24), 7966-7969 (2009-12-03)
Conformationally constrained mimetics of the laminin cell-adhesion site, YIGSR, are described. The site is the natural antagonist of the integrin-associated laminin receptor 1 (LAMR1) known to mediate metastatic tumor adhesion. The attachment of selected metastatic cell lines toward the constrained
Bart G J Dekkers et al.
Respiratory research, 11, 170-170 (2010-12-07)
Fibroproliferative airway remodelling, including increased airway smooth muscle (ASM) mass and contractility, contributes to airway hyperresponsiveness in asthma. In vitro studies have shown that maturation of ASM cells to a (hyper)contractile phenotype is dependent on laminin, which can be inhibited

Artikel

Conjugated polymers offer charge transport between inorganic, electrically conducting metals and organic, proton-conducting biological systems.

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