Recombinant Human IGF-1 Protein, >95% SDS-PAGE, high purity

Features and benefits
  • Expression System: Pichia pastoris
  • Accession #: P05019
  • Protein Tag: No tag
  • Bioactivity: Measured in a cell proliferation assay using MCF7 breast cancer cell line. The ED₅₀ for this effect is typically <4.6 ng/mL.
  • Endotoxin Concentration: <0.2 EU/μg
Item Number
rp147252
Grouped product items
SKUSizeAvailabilityPrice Qty
rp147252-100μg
100μg
In stock
$79.90
rp147252-1mg
1mg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$239.90
rp147252-500μg
500μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$179.90

Animal Free, ≥95% (SDS-PAGE), Active, E.coli, No tag, 49-188 aa

Basic Description

Product NameRecombinant Human IGF-1 Protein, >95% SDS-PAGE, high purity
SynonymsIBP1; IGF1; IGF-1; IGF1A; IGFI; IGF-I; IGF-IA; IGF-IB; insulin-like growth factor 1 (somatomedin C); insulin-like growth factor 1; insulin-like growth factor I; insulin-like growth factor IA; insulin-like growth factor IB; Mechano growth factor; MGF; Soma
GradeActiBioPure™, Animal Free, Bioactive, Carrier Free, High Performance
Product Description

The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake.

Specifications & PurityAnimal Free, Carrier Free, Bioactive, ActiBioPure™, High performance, ≥95%(SDS-PAGE)
Purity>95% SDS-PAGE
BioactivityMeasured in a cell proliferation assay using MCF7 breast cancer cell line. The ED₅₀ for this effect is typically <4.6 ng/mL.
Endotoxin Concentration<0.2 EU/μg
Expression SystemPichia pastoris
SpeciesHuman
Amino Acids49-118 aa
SequenceGP ETLCGAELVD ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSA
Protein TagNo tag
N-terminal SequenceGly
Protein LengthFull length protein
Accession #P05019
SourceRecombinant
Predicted molecular weight7.7 kDa
SDS-PAGE8.5 kDa, under reducing conditions; 8.5 kDa, under non-reducing conditions.

Images

Recombinant Human IGF-1 Protein (rp147252)-Protein Bioactivity
Measured in a cell proliferation assay using MCF7 breast cancer cell line. The ED₅₀ for this effect is typically <4.6ng/mL.

Recombinant Human IGF-1 Protein (rp147252)-SDS-PAGE
5μg/lane of Recombinant Human IGF-1 was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a single band at 8.5 kDa.

Product Specifications

FormLyophilized
ReconstitutionReconstitute with phosphate buffered saline.Store lyophilized form at room temperature. Reconstitute, aliquot and store at -80°C for 12 months or +4°C for 1 week.Avoid repeated freeze-thaw. Lyophilized contents may appear as either a translucent film or a
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageStable at -20℃ to 24 months, stable at 2-8 ℃ to 4 weeks. Prepared as 100μg/ml storage solution, 2~8℃ can be stably stored for a week. Upon delivery aliquot. Avoid freeze/thaw cycle.

Certificates

Certificate of Analysis(COA)

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3 results found

Lot NumberCertificate TypeDateItem
ZJ24F0102336Certificate of AnalysisJan 30, 2024 rp147252
ZJ23F0400100Certificate of AnalysisApr 06, 2023 rp147252
ZJ23F0400101Certificate of AnalysisApr 06, 2023 rp147252

Related Documents

References

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2. Sato, A A and 7 more authors..  (1992)  1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution..  Journal of biochemistry,      [PMID:1319992]
3. Sandberg-Nordqvist, A C AC, Ståhlbom, P A PA, Lake, M M and Sara, V R VR..  (1992)  Characterization of two cDNAs encoding insulin-like growth factor 1 (IGF-1) in the human fetal brain..  Brain research. Molecular brain research,      [PMID:1372070]
4. Steenbergh, P H PH, Koonen-Reemst, A M AM, Cleutjens, C B CB and Sussenbach, J S JS..  (1991)  Complete nucleotide sequence of the high molecular weight human IGF-I mRNA..  Biochemical and biophysical research communications,    (15):   [PMID:2018498]
5. Cooke, R M RM, Harvey, T S TS and Campbell, I D ID..  (1991)  Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study..  Biochemistry,    (4):   [PMID:2036417]
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7. Le Bouc, Y Y, Dreyer, D D, Jaeger, F F, Binoux, M M and Sondermeyer, P P..  (1986)  Complete characterization of the human IGF-I nucleotide sequence isolated from a newly constructed adult liver cDNA library..  FEBS letters,    (3):   [PMID:2935423]
8. Rotwein, P P, Pollock, K M KM, Didier, D K DK and Krivi, G G GG..  (1986)  Organization and sequence of the human insulin-like growth factor I gene. Alternative RNA processing produces two insulin-like growth factor I precursor peptides..  The Journal of biological chemistry,    (15):   [PMID:2937782]
9. de Pagter-Holthuizen, P P and 6 more authors..  (1986)  Organization of the human genes for insulin-like growth factors I and II..  FEBS letters,    (20):   [PMID:3002851]
10. Raschdorf, F F, Dahinden, R R, Maerki, W W, Richter, W J WJ and Merryweather, J P JP..  (1988)  Location of disulphide bonds in human insulin-like growth factors (IGFs) synthesized by recombinant DNA technology..  Biomedical & environmental mass spectrometry,      [PMID:3242681]
11. and Rotwein, P P..  (1986)  Two insulin-like growth factor I messenger RNAs are expressed in human liver..  Proceedings of the National Academy of Sciences of the United States of America,      [PMID:3455760]
12. Blundell, T L TL, Bedarkar, S S and Humbel, R E RE..  (1983)  Tertiary structures, receptor binding, and antigenicity of insulinlike growth factors..  Federation proceedings,      [PMID:6189745]
13. Jansen, M M and 8 more authors..  (1983)  Sequence of cDNA encoding human insulin-like growth factor I precursor..  Nature,      [PMID:6358902]
14. Dull, T J TJ, Gray, A A, Hayflick, J S JS and Ullrich, A A..  (1984)  Insulin-like growth factor II precursor gene organization in relation to insulin gene family..  Nature,      [PMID:6382022]
15. Sandberg-Nordqvist, A C AC and 5 more authors..  (1993)  Characterization of insulin-like growth factor 1 in human primary brain tumors..  Cancer research,    (1):   [PMID:8495408]
16. Woods, K A KA, Camacho-Hübner, C C, Savage, M O MO and Clark, A J AJ..  (1996)  Intrauterine growth retardation and postnatal growth failure associated with deletion of the insulin-like growth factor I gene..  The New England journal of medicine,    (31):   [PMID:8857020]
17. Cargill, M M and 17 more authors..  (1999)  Characterization of single-nucleotide polymorphisms in coding regions of human genes..  Nature genetics,      [PMID:10391209]
18. Scherer, Steven E SE and 216 more authors..  (2006)  The finished DNA sequence of human chromosome 12..  Nature,    (16):   [PMID:16541075]
19. Saegusa, Jun J and 7 more authors..  (2009)  The direct binding of insulin-like growth factor-1 (IGF-1) to integrin alphavbeta3 is involved in IGF-1 signaling..  The Journal of biological chemistry,    (4):   [PMID:19578119]
20. Wang, Lei L and 5 more authors..  (2010)  The SRC homology 2 domain protein Shep1 plays an important role in the penetration of olfactory sensory axons into the forebrain..  The Journal of neuroscience : the official journal of the Society for Neuroscience,    (29):   [PMID:20881139]
21. Zoidis, E E, Ghirlanda-Keller, C C and Schmid, C C..  (2011)  Stimulation of glucose transport in osteoblastic cells by parathyroid hormone and insulin-like growth factor I..  Molecular and cellular biochemistry,      [PMID:21076856]
22. Fujita, Masaaki M and 7 more authors..  (2012)  Cross-talk between integrin α6β4 and insulin-like growth factor-1 receptor (IGF1R) through direct α6β4 binding to IGF1 and subsequent α6β4-IGF1-IGF1R ternary complex formation in anchorage-independent conditions..  The Journal of biological chemistry,    (6):   [PMID:22351760]
23. Fujita, Masaaki M, Takada, Yoko K YK and Takada, Yoshikazu Y..  (2013)  Insulin-like growth factor (IGF) signaling requires αvβ3-IGF1-IGF type 1 receptor (IGF1R) ternary complex formation in anchorage independence, and the complex formation does not require IGF1R and Src activation..  The Journal of biological chemistry,    (1):   [PMID:23243309]
24. Fujita, Masaaki M and 13 more authors..  (2013)  An integrin binding-defective mutant of insulin-like growth factor-1 (R36E/R37E IGF1) acts as a dominant-negative antagonist of the IGF1 receptor (IGF1R) and suppresses tumorigenesis but still binds to IGF1R..  The Journal of biological chemistry,    (5):   [PMID:23696648]
25. Shcheglovitov, Aleksandr A and 10 more authors..  (2013)  SHANK3 and IGF1 restore synaptic deficits in neurons from 22q13 deletion syndrome patients..  Nature,    (14):   [PMID:24132240]
26. Shaheen, Ranad R and 8 more authors..  (2014)  Genomic analysis of primordial dwarfism reveals novel disease genes..  Genome research,      [PMID:24389050]

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