T5300

Sigma-Aldrich

Transforming Growth Factor-β2 from porcine platelets

powder, suitable for cell culture

Synonym(s):
TGF-β2
MDL number:
NACRES:
NA.77
Pricing and availability is not currently available.

Quality Level

biological source

Porcine (Platelets)

assay

≥97% (SDS-PAGE and N-terminal analysis)

form

powder

potency

0.05-0.5 ng/mL ED50/EC50

mol wt

protein 25 kDa

packaging

pkg of 1 μg

storage condition

avoid repeated freeze/thaw cycles

application(s)

cell culture | mammalian: suitable

impurities

endotoxin, tested

UniProt accession no.

storage temp.

−20°C

Gene Information

pig ... TGFB2(397084)

General description

TGF-β2 (transforming growth factor-β2) belongs to the TGF-β superfamily and the gene is mapped to pig (Sus scrofa) chromosome 10p16.

Biochem/physiol Actions

TGF-β2 is responsible for maintaining immune homeostasis. TGF-β2 promotes cellular growth, differentiation and survival. TGF-β2 controls lymphocyte proliferation, apoptosis, hematopoiesis, and embryogenesis. TGF-β2 is a tumor suppress or in the early stages of carcinogenesis, but in the later stages acts as a tumor promoter by inducing epithelial-mesenchymal transition and stimulating angiogenesis. TGF-β2 prevents NK (natural killer) cells growth as well as B and T cell proliferation. TGF-β2 also greatly inhibits the growth of both normal and transformed epithelial. The growth of lymphoid, fibroblast and keratinocyte cells are also known to be hinder by TGF-β2. TGF-β2 controls intestinal homeostasis by functioning in synergy with the bacterial lipopolysaccharide and thereby maintain interleukin-8.
TGF-β2, like TGF-β1, is produced by many cell types and reported to be most concentrated in mammalian platelets.

TGF-β2 belongs to the TGF-β superfamily. TGF-β2 is important for immune homeostasis by balancing lymphocyte proliferation, apoptosis, hematopoiesis, and embryogenesis. TGF-β2 is crucial in cell growth, differentiation, and survival. TGF-β2 is a strong growth inhibitor for normal and transformed epithelial, lymphoid, fibroblast, and keratinocyte cells. TGF-β2 is a tumor suppress or in the early stages of carcinogenesis, but in the later stages acts as a tumor promoter by inducing epithelial-mesenchymal transition and stimulating angiogenesis. TGF-β2 inhibits NK cells growth as well as B and T cell proliferation.
TGF-β2, like TGF-β1, is produced by many cell types and reported to be most concentrated in mammalian platelets.

Physical form

Lyophilized from a 0.2 μm filtered solution in 25% acetonitrile and 0.1% trifluoroacetic acid containing 0.05 mg bovine serum albumin.

Analysis Note

The biological activity of porcine TGF-β2 was tested in culture by measuring its ability to inhibit thymidine incorporation in the IL-4 dependent mouse T-helper cell line HT-2. The EC50 is defined as the effective concentration of growth factor that elicits 50% inhibition of cell growth in a cell based bioassay.
The biological activity is measured by its ability to inhibit the IL-4-dependent proliferation of mouse HT-2 cells.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
Transforming growth factor-? induces epithelial to mesenchymal transition and suppresses the proliferation and transdifferentiation of cultured human pancreatic duct cells.
Hong OK, Shin JA, Lee HJ, Jeon SY
Journal of Cellular Biochemistry (2010)
Mapping of the porcine urate oxidase and transforming growth factor β 2 genes by fluorescence in situ hybridization.
Rettenberger G, et al.
Chromosome Research, 4(2), 147-150 (1996)
Transforming growth factor-2 and endotoxin interact to regulate homeostasis via interleukin-8 levels in the immature intestine
Nguyen DN, et al.
American Journal of Physiology: Gastrointestinal and Liver Physiology, 307, G689- G699 (2014)
Curcumin suppresses doxorubicin-induced epithelial?mesenchymal transition via the inhibition of TGF-β and PI3K/AKT signaling pathways in triple-negative breast cancer cells.
Chen WC, et al.
Journal of Agricultural and Food Chemistry, 61(48), 11817-11824 (2013)
Tsang, M., et al.
Lymphokine Research, 9, 607-607 (1990)

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