TGFA Protein (AA 40-89)
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- Target See all TGFA Proteins
- TGFA (Transforming Growth Factor, alpha (TGFA))
- Protein Type
- Recombinant
- Biological Activity
- Active
- Protein Characteristics
- AA 40-89
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Application
- Western Blotting (WB), Immunofluorescence (IF)
- Purity
- >98 % , as determined by Coomassie stained SDS-PAGE and HPLC analysis.
- Endotoxin Level
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Less than 0.1 ng per μg of protein.
- Top Product
- Discover our top product TGFA Protein
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Comment
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Biological activity: The expected ED50 is ≤ 0.2 ng/ml, corresponding to a specific activity of ≥ 5 x 106 units/mg, as determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells.
- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/mL. Do not vortex. It is recommended to further dilute in a buffer, such as 5 % Trehalose, and store working aliquots at -20 °C to -80 °C.
- Buffer
- Lyophilized, carrier-free.
- Handling Advice
- Avoid repeated freeze/thaw cycles.
- Storage
- -20 °C
- Storage Comment
- Unopened vial can be stored at -20°C or -70°C.
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- Target
- TGFA (Transforming Growth Factor, alpha (TGFA))
- Alternative Name
- TGF-alpha (TGFA Products)
- Synonyms
- TFGA Protein, LOC100009482 Protein, TGF alpha Protein, TGFA Protein, wa-1 Protein, wa1 Protein, RATTGFAA Protein, TGFAA Protein, NV15606 Protein, si:ch211-10e8.7 Protein, transforming growth factor alpha Protein, transforming growth factor alpha L homeolog Protein, transforming growth factor-alpha Protein, transforming growth factor, alpha Protein, TGFA Protein, TGF-A Protein, Tgfa Protein, tgfa.L Protein, LOC100121300 Protein, LOC100009150 Protein, tgfa Protein
- Background
- TGF-α was initially identified in the culture medium of several transformed cell lines. TGF-α is structurally and functionally related to the epidermal growth factor and belongs to the EGF subfamily that also includes amphiregulin (AR), heparin binding EGF-like growth factor (HB-EGF), betacellulin (BTC), epiregulin (EPR), and epigen (EPG). TGF-α is derived from a transmembrane precursor (20-22 kD), pro-TGFα undergoes several posttranslational modifications that include N- and O-linked glycosylation and palmitoylation. The pro-TGFα includes a glycosylated N-terminal domain, a TGF-α region with the EGF-like motif, a linker sequence that joins the ectodomain to the transmembrane domain, and an intracellular portion. TGF-α is proteolytically released from the membrane by tumor necrosis factor-α converting enzyme (TACE/ADAM-17). TGF-α is cleaved at the N- and C-terminus of the EGF motif, the proteolytic cleavage at the C-terminus is required to release the soluble form. The N-terminal cleavage of pro-TGF α occurs at the cell surface by TACE-independent activity. TGF-α plays a key role regulating follicle development and tumorigenesis. TGF-α and its receptor are highly expressed in papillary thyroid carcinoma. Also, TGF-α polymorphism has been associated with oral birth defects.
- Molecular Weight
- The 55 amino acid recombinant protein has a predicted Molecular mass of 5.5 kDa. The predicted N-terminal amino acid is Val.
- Pathways
- NF-kappaB Signaling, RTK Signaling, EGFR Signaling Pathway
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