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L3408

Sigma-Aldrich

Transforming Growth Factor-β1 Latency Associated Peptide human

≥97% (SDS-PAGE), recombinant, expressed in Sf21 cells, lyophilized powder, suitable for cell culture

Synonyme(s) :

LAP, TGF-β1

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About This Item

Numéro MDL:
Code UNSPSC :
51111800
Nomenclature NACRES :
NA.41

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in Sf21 cells

Pureté

≥97% (SDS-PAGE)

Forme

lyophilized powder

Poids mol.

protein 70 kDa

Technique(s)

cell culture | mammalian: suitable

Impuretés

endotoxin, tested

Adéquation

suitable for molecular biology

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

human ... TGFB1(7040)

Description générale

Research Area: Cell Signaling

TGF-β is released from degranulating platelets and secreted from nearly all cells in a biologically inactive complex which is unable to bind to cellular receptors and is not recognized by antibodies to TGF-β. The peptide can be activated by acidification, alkalinization, or action of chaotropic agents in vitro. The complex consists of TGF-β associated non-covalently with a protein designated as the latency associated peptide (LAP). TGF-β and LAP represent components of a pro-peptide that is cleaved in a post-golgi compartment prior to secretion. The recombinant human LAP is produced from a DNA sequence corresponding to the 278 amino acid residues of pre-pro-TGF-β1 terminating prior to the mature TGF-β1. LAP contains a Cys33 to Ser33 substitution. LAP contains 249 amino acids, generated after cleavage of a 29 amino acid residue signal peptide. LAP is a glycoslyated, disulfide linked homodimer.

Application

Latency Associated Peptide (LAP) may be used to inhibit transforming growth factor-β 1 activity in various biological systems.
Transforming Growth Factor-β1 Latency Associated Peptide human has been used to coat the cell culture inserts for cell migration assays to determine the functional effects of impeding αvβ6 endocytosis in vitro. It has also been used to coat non-tissue culture-treated 96-well plates for adhesion assays.

Actions biochimiques/physiologiques

Latency Associated Peptide (LAP) binds transforming growth factor-beta 1 (TGF-β1) to form a latent complex. The activity of TGF-β1 is primarily regulated through the activation of the latent molecule. LAP has the ability to stimulate epithelial cell migration, representing a new function for LAP in controlling monocyte trafficking and immune modulation. Following post-translational modification, TGF-β1 binds non-covalently to the LAP to establish latency. Due to its crucial function in modulating TGF-β1 activity, LAP plays a fundamental role in governing a range of TGF-β1 effects. LAP is expressed on immature dendritic cells and contributes to T cell differentiation. LAP exhibits both chemotactic and anti-inflammatory activity independently of active TGF-β1.
TGF-β1 is produced by many cell types, but is reported to be most concentrated in mammalian platelets, where it is present at approximately four times the level of TGF-β2.

Forme physique

Lyophilized from 0.2 μm filtered phosphate buffered saline containing 1.25 mg bovine serum albumin.

Remarque sur l'analyse

The biological activity is measured by its ability to inhibit TGF-β1 activity on mouse HT-2 cells.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Latency associated peptide has in vitro and in vivo immune effects independent of TGF-beta1
Ali NA, et al,
PLoS ONE, 3(4), e1914-e1914 (2008)
Loss of MMP-8 in ductal carcinoma in situ (DCIS)-associated myoepithelial cells contributes to tumour promotion through altered adhesive and proteolytic function
Sarper M, et al.
Breast Cancer Research, 1-19 (2017)
Muge Sarper et al.
Breast cancer research : BCR, 19(1), 33-33 (2017-03-24)
Normal myoepithelial cells (MECs) play an important tumour-suppressor role in the breast but display an altered phenotype in ductal carcinoma in situ (DCIS), gaining tumour-promoter functions. Matrix metalloproteinase-8 (MMP-8) is expressed by normal MECs but is lost in DCIS. This

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