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Merck

H8791

Sigma-Aldrich

Transforming Growth Factor-β3 human

HumanKine®, 95% (SDS-PAGE), recombinant, expressed in HEK 293 cells, lyophilized powder, suitable for cell culture

Sinónimos:

TGF-β3

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.77

product name

Transforming Growth Factor-β3 human, TGF-β3, recombinant, expressed in HEK 293 cells, HumanKine®, suitable for cell culture

biological source

human

Quality Level

recombinant

expressed in HEK 293 cells

assay

≥95% (SDS-PAGE)

form

lyophilized powder

potency

≤1.0 ng/mL EC50

quality

endotoxin tested

mol wt

dimer 25 kDa (non-glycosylated)

packaging

pkg of 5 μg

manufacturer/tradename

HumanZyme

storage condition

avoid repeated freeze/thaw cycles

technique(s)

cell culture | mammalian: suitable

impurities

≤1 EU/μg

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... TGFB3(7043)

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General description

TGF-β3 (transforming growth factor-β3) belongs to the TGF β superfamily. The TGFβ3 gene is mapped to human chromosome 14q24.3

Biochem/physiol Actions

TGF-β3 (transforming growth factor-β3) regulates lymphocyte proliferation, apoptosis, hematopoiesis and embryogenesis to maintain immune homeostasis. TGF-β plays an important role in cell growth, differentiation, and survival. TGF-β3 specifically promotes chondrogenic differentiation.TGF-β3 is a strong growth inhibitor for normal and transformed epithelial, lymphoid, fibroblast, and keratinocyte cells. TGF-2 inhibits antitumor action of NK (natural killer) cells, T-cells, macrophages, monocytes and neutrophils. TGF-β3 is a tumor suppressor 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-β isoforms is known to participate in wound healing and tissue fibrosis. TGF-β3 is crucial for tissue restoration and scarless tissue repair. Mutation in the TGFβ3 gene is associated with development of non-syndromic cleft palate only (NS CPO), a rare congenital disease.
TGF-β3 is less prevalent in natural expression than either TGF-β1 or TGF-β2, but it is the most abundant mRNA expressed in chick embryos. It is also expressed in human umbilical cord, in a variety of mesenchymal cells of human and rodent origin, and in several human carcinoma cells.

Physical form

Lyophilized from a 0.2 μm filtered solution of 50 mM NaOAc pH 4.5

Preparation Note

HumanKine TGF-β3 is expressed in human HEK 293 cells as a mature, disulfide linked, non- glycosylated homodimer with a predicted molecular mass of 25 kDa.
This product is lyophilized from a solution of 50mM NaOAc, pH 3.7.

Analysis Note

The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2).

Legal Information

HumanKine is a registered trademark of Proteintech Group, Inc. and Humanzyme, Inc

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Visite la Librería de documentos

Hongbin Fan et al.
Journal of biomedical materials research. Part A, 95(4), 982-992 (2010-09-28)
Although most in vitro studies indicate that transforming growth factor β3 (TGF-β3) immobilized scaffold is suitable for cartilage tissue engineering, in vivo studies of implanting immobilized scaffold for chondral defect repair are still lacking. This study is to evaluate the
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)
Adipose tissue fibrosis in human cancer cachexia: the role of TGFβ pathway.
Alves MJ, et al.
BMC Cancer, 17(1) (2017)
Transforming growth factor β (TGF-β) and inflammation in cancer
Bierie B, et al.
Cytokine & Growth Factor Reviews, 21(1), 49?59-49?59 (2010)
TGFβ3 / SfaN1 gene variant and the risk factor of nonsyndromic cleft palate only among Indonesian patients.
Nasroen SL, et al.
Cellular and Molecular Biology, 63(2), 88-91 (2017)

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