Recombinant Human TGF-alpha Protein, >98%(SDS-PAGE), high purity

Features and benefits
  • Expression System: E. coli
  • Accession #: P01135
  • Protein Tag: C-His
  • Endotoxin Concentration: <0.1 EU/μg
Item Number
rp152259
Grouped product items
SKUSizeAvailabilityPrice Qty
rp152259-10μg
10μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$49.90
rp152259-20μg
20μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$66.90
rp152259-100μg
100μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$210.90
rp152259-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$1,806.90

Animal Free, >98%(SDS-PAGE), Active, E.coli, His, 40-89aa

Basic Description

Product NameRecombinant Human TGF-alpha Protein, >98%(SDS-PAGE), high purity
Synonymsprotransforming growth factor alpha; TFGA; TGFA; TGFalpha; TGF-alpha; transforming growth factor, alpha; transforming growth factor-alpha
GradeAnimal Free, Azide Free, Carrier Free
Product Description

Transforming growth factor alpha (TGF-α) is a protein that in humans is encoded by the TGFA gene. TGF-alpha is a member of the EGF family of cytokines that are synthesized as transmembrane precursors and are characterized by the presence of one or several EGF structural units in their extracellular domain. Expression of TGF-alpha is widespread in tumors and transformed cells. TGF-alpha is also expressed in normal tissues during embryogenesis and in adult tissues, including pituitary, brain, keratinocytes, and macrophages.

Function

TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.


Specifications & PurityAnimal Free, Carrier Free, Azide Free, ≥98%(SDS-PAGE)
Purity>98%(SDS-PAGE)
Endotoxin Concentration<0.1 EU/μg
Expression SystemE. coli
SpeciesHuman
Amino Acids40-89 aa
SequenceVVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA
Protein TagC-His
N-terminal SequenceMet
Accession #P01135
Predicted molecular weight6.49 kDa
SDS-PAGE8.4 kDa, under reducing conditions; 8.4 kDa, under non-reducing conditions.

Images

Recombinant Human TGF-alpha Protein (rp152259) - SDS-PAGE
4 μg/lane of Recombinant TGF-alpha was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 8.4 kDa.

Product Specifications

FormLyophilized
ReconstitutionIt is recommended to reconstitute the lyophilized protein in sterile H2O to a concentration not less than 100 μg/mL and incubate the stock solution for at least 20 min to ensure sufficient re-dissolved. In some experiments, it recommends to add 10 mM HCl
Storage TempStore at -20°C
Shipped InIce chest + Ice pads
Stability And StorageShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle. This product is an active protein and may elicit a biological response in vivo, handle with caution.

Certificates

Certificate of Analysis(COA)

Enter Lot Number to search for COA:

Find and download the COA for your product by matching the lot number on the packaging.

2 results found

Lot NumberCertificate TypeDateItem
ZJ23F0800924Certificate of AnalysisAug 30, 2023 rp152259
ZJ23F0800925Certificate of AnalysisAug 30, 2023 rp152259

Related Documents

References

1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K et al..  (2004)  Complete sequencing and characterization of 21,243 full-length human cDNAs..  Nat Genet,  36  (1): (40-5).  [PMID:14702039]
2. Bean, M F MF and Carr, S A SA..  (1992)  Characterization of disulfide bond position in proteins and sequence analysis of cystine-bridged peptides by tandem mass spectrometry..  Analytical biochemistry,      [PMID:1632509]
3. Harvey, T S TS, Wilkinson, A J AJ, Tappin, M J MJ, Cooke, R M RM and Campbell, I D ID..  (1991)  The solution structure of human transforming growth factor alpha..  European journal of biochemistry,    (15):   [PMID:2050136]
4. Kline, T P TP and 5 more authors..  (1990)  Solution structures of human transforming growth factor alpha derived from 1H NMR data..  Biochemistry,    (28):   [PMID:2261437]
5. Jakowlew, S B SB, Kondaiah, P P, Dillard, P J PJ, Sporn, M B MB and Roberts, A B AB..  (1988)  A novel low molecular weight ribonucleic acid (RNA) related to transforming growth factor alpha messenger RNA..  Molecular endocrinology (Baltimore, Md.),      [PMID:2464748]
6. Jakobovits, E B EB, Schlokat, U U, Vannice, J L JL, Derynck, R R and Levinson, A D AD..  (1988)  The human transforming growth factor alpha promoter directs transcription initiation from a single site in the absence of a TATA sequence..  Molecular and cellular biology,      [PMID:2907605]
7. Derynck, R R, Roberts, A B AB, Winkler, M E ME, Chen, E Y EY and Goeddel, D V DV..  (1984)  Human transforming growth factor-alpha: precursor structure and expression in E. coli..  Cell,      [PMID:6088071]
8. Qian, J F JF, Feingold, J J, Stoll, C C and May, E E..  (1993)  Transforming growth factor-alpha: characterization of the BamHI, RsaI, and TaqI polymorphic regions..  American journal of human genetics,      [PMID:8100397]
9. Qian, J F JF, Lazar-Wesley, E E, Breugnot, C C and May, E E..  (1993)  Human transforming growth factor alpha: sequence analysis of the 4.5-kb and 1.6-kb mRNA species..  Gene,    (15):   [PMID:8224876]
10. Moy, F J FJ and 5 more authors..  (1993)  Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints..  Biochemistry,    (27):   [PMID:8338831]
11. Shum, L L, Turck, C W CW and Derynck, R R..  (1996)  Cysteines 153 and 154 of transmembrane transforming growth factor-alpha are palmitoylated and mediate cytoplasmic protein association..  The Journal of biological chemistry,    (8):   [PMID:8910478]
12. Collin, G B GB, Marshall, J D JD, Naggert, J K JK and Nishina, P M PM..  (1999)  TGFA: exon-intron structure and evaluation as a candidate gene for Alström syndrome..  Clinical genetics,      [PMID:10066034]
13. Fernández-Larrea, J J, Merlos-Suárez, A A, Ureña, J M JM, Baselga, J J and Arribas, J J..  (1999)  A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface..  Molecular cell,      [PMID:10230395]
14. Xu, X X, Liao, J J, Creek, K E KE and Pirisi, L L..  (1999)  Human keratinocytes and tumor-derived cell lines express alternatively spliced forms of transforming growth factor-alpha mRNA, encoding precursors lacking carboxyl-terminal valine residues..  Oncogene,    (30):   [PMID:10523832]
15. Machida, J J and 5 more authors..  (1999)  Transforming growth factor-alpha (TGFA): genomic structure, boundary sequences, and mutation analysis in nonsyndromic cleft lip/palate and cleft palate only..  Genomics,    (1):   [PMID:10552925]
16. Hillier, Ladeana W LW and 121 more authors..  (2005)  Generation and annotation of the DNA sequences of human chromosomes 2 and 4..  Nature,    (7):   [PMID:15815621]
17. Castro, Carolina Perez CP, Piscopo, Denise D, Nakagawa, Takatoshi T and Derynck, Rik R..  (2007)  Cornichon regulates transport and secretion of TGFalpha-related proteins in metazoan cells..  Journal of cell science,    (15):   [PMID:17607000]
18. Ding, Wei W and 6 more authors..  (2008)  EGF receptor-independent action of TGF-alpha protects Naked2 from AO7-mediated ubiquitylation and proteasomal degradation..  Proceedings of the National Academy of Sciences of the United States of America,    (9):   [PMID:18757723]

Solution Calculators