Basic Description

Product Name	Recombinant Human IGF-1 Protein, ＞95% SDS-PAGE, high purity, CAS No.67763-96-6
Synonyms	IGF-I \| Mechano growth factor \| MGF \| Somatomedin-C
Grade	ActiBioPure™, Animal Free, Bioactive, Carrier Free, GMP, High Performance
Product Description
Specifications & Purity	Animal Free, Carrier Free, Bioactive, ActiBioPure™, High Performance, GMP, ≥95%(SDS-PAGE)
Biochemical and Physiological Mechanisms	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 synthe
Purity	＞95% SDS-PAGE
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
Expression System	Pichia pastoris
Species	Human
Amino Acids	49-118 aa
Sequence	GP ETLCGAELVD ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSA
Protein Tag	No tag
N-terminal Sequence	Gly
Protein Length	Full length protein
Accession #	P05019
Source	Recombinant
Predicted molecular weight	7.7 kDa
SDS-PAGE	8.5 kDa, under reducing conditions; 8.5 kDa, under non-reducing conditions.

Images

Protein Bioactivity: Recombinant Human IGF-1 Protein (rp147252)

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.

SDS-PAGE: Recombinant Human IGF-1 Protein (rp147252)

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

Shape	Lyophilized
Reconstitution	Reconstitute 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 white powder. This variance does not affect the quality of the product.
Storage Temp	Store at -20°C,Avoid repeated freezing and thawing
Shipped In	Ice chest + Ice pads
Stability And Storage	Stable 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 receipt, it is recommended to aliquot. Avoid freeze/thaw cycle.
CAS	67763-96-6

Certificates（CoA,COO,BSE/TSE and Analysis Chart)

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Analytical Chart:

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3 results found

Lot Number	Certificate Type	Date	Item
ZJ24F0102336	Certificate of Analysis	Jan 30, 2024	rp147252
ZJ23F0400100	Certificate of Analysis	Apr 06, 2023	rp147252
ZJ23F0400101	Certificate of Analysis	Apr 06, 2023	rp147252

Specifications

Specification Sheet

FAQs and Articles

References

1. Rinderknecht, E E and Humbel, R E RE.. (1978) The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin.. The Journal of biological chemistry, (25): [PMID:632300]
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]
6. Tobin, G G, Yee, D D, Brünner, N N and Rotwein, P P.. (1990) A novel human insulin-like growth factor I messenger RNA is expressed in normal and tumor cells.. Molecular endocrinology (Baltimore, Md.), [PMID:2082190]
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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SKU	Size	Availability	Price
rp147252-100μg	100μg	5	$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

Recombinant Human IGF-1 Protein, ＞95% SDS-PAGE, high purity, CAS No.67763-96-6