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T7154

Sigma-Aldrich

Tyr-Ile-Gly-Ser-Arg

≥97% (HPLC)

Synonyme(s) :

Laminin Fragment 929-933

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About This Item

Formule empirique (notation de Hill):
C26H42N8O8
Numéro CAS:
110590-64-2
Poids moléculaire :
594.66
Numéro MDL:
MFCD00076472
Code UNSPSC :
12352209
ID de substance PubChem :
24900419
Nomenclature NACRES :
NA.32
Le tarif et la disponibilité ne sont pas disponibles actuellement.

Source biologique

synthetic (organic)

Niveau de qualité

200

Essai

≥97% (HPLC)

Forme

powder

Technique(s)

cell culture | mammalian: suitable

Solubilité

H2O: soluble 1 mg/mL, clear, colorless

Température de stockage

−20°C

Chaîne SMILES 

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

Clé InChI

MWOGMBZGFFZBMK-LJZWMIMPSA-N

Amino Acid Sequence

Tyr-Ile-Gly-Ser-Arg

Application

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.[1]

Actions biochimiques/physiologiques

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.[2] It inhibits the increased expression of endothelial nitric-oxide synthase in primary porcine aortic endothelial cells.[3]
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.

Notes préparatoires

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

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Certificats d'analyse (COA)

Lot/Batch Number
0000261358
0000261358
SLCN4078
SLCL5444
SLCK3748

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Sigma-Aldrich

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Arg-Gly-Asp ≥97% (TLC)

Sigma-Aldrich

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Arg-Gly-Asp

Presenting multiple adhesion ligands on hydrogels for control of PC12 phenotype.
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Journal of controlled release : official journal of the Controlled Release Society, 152 Suppl 1, e219-e220 (2011-12-27)
Yamato Kikkawa et al.
Cell adhesion & migration, 7(1), 150-256 (2012-12-25)
Laminin-111 is a large trimeric basement membrane glycoprotein with many active sites. In particular, four peptides active in tumor malignancy studies have been identified in laminin-111 using a systematic peptide screening method followed by various assays. Two of the peptides
Rajeev K Sinha et al.
Journal of the American Society for Mass Spectrometry, 22(9), 1645-1650 (2011-09-29)
Charge-directed fragmentation has been shown to be the prevalent dissociation step for protonated peptides under the low-energy activation (eV) regime. Thus, the determination of the ion structure and, in particular, the characterization of the protonation site(s) of peptides and their
Jong Hyuk Yoon et al.
Biochemical and biophysical research communications, 428(3), 416-421 (2012-11-01)
The dermal ECM is synthesized from fibroblasts and is primarily compromised of fibrillar collagen and elastic fibers, which support the mechanical strength and resiliency of skin, respectively. Laminin, a major glycoprotein located in the basement membrane, promotes cell adhesion, cell
T Michigami et al.
Clinical & experimental metastasis, 16(7), 645-654 (1999-02-05)
B-cell lymphoma frequently shows simultaneous dissemination to multiple organs. It also occasionally involves bone and causes osteolytic lesions. To study the mechanisms responsible for this capacity of lymphoma cells to grow in different tissue microenvironments and search for effective therapeutic
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