TGFB3 Protein (AA 301-412)

Catalog No. ABIN2666748

Recombinant TGFB3 protein expressed in CHO Cells.

Quick Overview for TGFB3 Protein (AA 301-412) (ABIN2666748)

Target: TGFB3 (Transforming Growth Factor, beta 3 (TGFB3))

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: CHO Cells

Application: Flow Cytometry (FACS)

Purity: > 98 % , as determined by Coomassie stained SDS-PAGE.

Product Details

Protein Characteristics: AA 301-412

Sterility: 0.22 μm filtered

Endotoxin Level:

Less than 0.01 ng per μg cytokine as determined by the LAL method.

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

Biological activity: TGF-β3 inhibits the proliferation of mouse HT-2 cells induced by IL-4. The ED50 is from 0.10 to 0.4 ng/ml, corresponding to a specific activity of 2.5-10 x 106 units/mg.

Restrictions: For Research Use only

Handling

Format: Liquid

Reconstitution: For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 μg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 1 % BSA or HAS or 10 % FBS. After dilution, the cytokine can be stored between 2 °C and 8 °C for one month or from -20 °C to -70 °C for up to 3 months.

Buffer: 0.22 μm filtered protein solution is in 25 % Acetonitrile, 0.1 % TFA (trifluoroacetic acid).

Handling Advice: Avoid repeated freeze/thaw cycles.

Storage: -20 °C

Storage Comment: Unopened vial can be stored between 2°C and 8°C for three months, at -20°C for six months, or at -70°C for one year.

Target Details

Target: TGFB3 (Transforming Growth Factor, beta 3 (TGFB3))

Alternative Name: TGF-Beta3

Background: Human TGF-β3 precursor consists of two disulfide-linked identical subunits with 412 amino acids each. The carboxy-terminal (112 residues) of TGF-β3 represents the biologically active form of this protein, this portion of TGF-β 3 exhibits 86/112 and 89/112 identical residues compared with TGF-β1 and TGF-β2, respectively. TGF-β3 precursor is cleaved by furin, and localized in the residue 300 of the trans-Golgi network. Furin processes the TGF-β3 precursor at the carboxyl side of the consensus sequence RKKR which precedes the NH2-terminal Ala 301 residue of the mature TGF-β3. The TGF-β3 precursor includes (in the N-terminal portion) the latency-associated peptide (LAP dimer) and (in the C-terminal) the 25 kD portion that constitutes the mature TGF-β3. The LAP dimer and the TGF-β3 mature protein remain non-covalently associated after furin cleavage, and this complex does not bind to the TFG-β receptor. In addition, the TGF-β3 latent complex is joined covalently through LAP to LTBP. The TGF-β1 active form requires dissociation from LAP. Some activators can release TGF-β1 from LAP, such as thrombospondin-1, reactive oxygen species, and the integrins avb6 and avb8, and these activators might release TGF-β3 through similar mechanism. TGF-β3 induces biomechanical remodeling in avian embryonic atrioventricular valves. Also, gene delivery of a mutant TGF-β3 reduces re-epithelialization density and fibroblast/myofibroblast transdifferentiation within the wound area, both mechanisms are indicative of reduced scar tissue formation. In fact, recombinant TGF-β3 has been used in clinical trials as prophylactic treatment of human scars.

Molecular Weight: The 112 amino acid recombinant protein has a predicted molecular mass of approximately 12.7 kDa. The DTT-reduced protein migrates at approximately 14 kDa and non-reduced protein migrates at 28-30 kDa by SDS-PAGE. The N-terminal amino acid is Alanine.

Pathways: Cell-Cell Junction Organization, Production of Molecular Mediator of Immune Response, Protein targeting to Nucleus