What are the molecular formula, molecular weight and CAS number of IGF-DES?

IGF-DES: molecular formula C319H495N91O96S7, molecular weight ~7,365 g/mol (~7.4 kDa) and CAS number 112603-35-7.

What is the sequence of IGF-DES?

TLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA.

IGF-DES

A truncated insulin-like growth factor variant studied as a binding-protein-decoupled tool in cellular research models.

Updated August 20, 2026

Quick answers

What is IGF-DES?

IGF-DES is a truncated insulin-like growth factor variant studied as a binding-protein-decoupled tool in cellular research models. It is a truncated protein variant (67 residues) with a molecular weight of ~7,365 g/mol (~7.4 kDa) and the formula C319H495N91O96S7.

How much published research cites IGF-DES?

The Luvaminos IGF-DES record cites 19 published references, dated 1986 to 1996. Each is listed on this page with a link to its source.

Does Luvaminos test IGF-DES, and where is the certificate?

Luvaminos does not currently stock IGF-DES. Every peptide lot Luvaminos sells is tested by Freedom Diagnostics Testing, PLLC, an independent laboratory, and its certificate is published at luvaminos.com/coa under the lot number printed on the vial.

What modifications does IGF-DES carry?

IGF-DES: N-terminal truncation of human IGF-1: residues 4-70, with the Gly-Pro-Glu tripeptide absent from the N-terminus; three intramolecular disulfide bonds retained from the parent protein.

How is IGF-DES powder stored?

Sealed IGF-DES powder: -20°C, protected from light; lyophilized powder stable long term. Disulfide-bonded protein; sensitive to repeated freeze-thaw and oxidation.

How is IGF-DES different from IGF-1 LR3?

IGF-DES and IGF-1 LR3 are different compounds: IGF-DES has 67 amino acids, a molecular weight of ~7,365 g/mol (~7.4 kDa) and formula C319H495N91O96S7; IGF-1 LR3 has 83 amino acids, a molecular weight of ~9,117 g/mol (~9.1 kDa) and formula C400H625N111O115S9. IGF-DES: N-terminal truncation of human IGF-1: residues 4-70, with the Gly-Pro-Glu tripeptide absent from the N-terminus.

Molecular Profile

Type: Truncated protein variant (67 residues)
Molecular formula: C319H495N91O96S7
Molecular weight: ~7,365 g/mol (~7.4 kDa)
CAS number: 112603-35-7
Amino acids: 67
Sequence: TLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Modification: N-terminal truncation of human IGF-1: residues 4-70, with the Gly-Pro-Glu tripeptide absent from the N-terminus; three intramolecular disulfide bonds retained from the parent protein.

Mechanism & Target Class

An N-terminally truncated form of insulin-like growth factor 1 (IGF-1) corresponding to residues 4-70, lacking the Gly-Pro-Glu tripeptide at the N-terminus, with the three intramolecular disulfide bonds of the parent protein retained. The absence of this tripeptide - and of Glu3 in particular - lowers its affinity for the IGF-binding proteins (IGFBPs) while leaving its receptor-binding surface intact, which is the structural basis for its use as a binding-protein-decoupled comparator in molecular research.

Storage & Handling

Lyophilized: -20°C, protected from light; lyophilized powder stable long term.
Handling: Disulfide-bonded protein; sensitive to repeated freeze-thaw and oxidation.

Primary Database

PubChem SID 135331146 ↗

References (19)

Reviews
1
Ballard FJ, Wallace JC, Francis GL, Read LC, Tomas FM. (1996). Int J Biochem Cell Biol
DOI: 10.1016/1357-2725(96)00056-8 PubMed 8930132
Primary research
2
Heding A, Gill R, Ogawa Y, De Meyts P, Shymko RM. (1996). J Biol Chem
DOI: 10.1074/jbc.271.24.13948 PubMed 8662901
3
Lemmey AB, Ballard FJ, Martin AA, Tomas FM, Howarth GS, Read LC. (1994). Growth Factors
PubMed 7803042
4
Francis GL, Ross M, Ballard FJ, Milner SJ, Senn C, McNeil KA, Wallace JC, King R, Wells JR. (1992). J Mol Endocrinol
DOI: 10.1677/jme.0.0080213 PubMed 1378742
5
Tomas FM, Knowles SE, Owens PC, Chandler CS, Francis GL, Read LC, Ballard FJ. (1992). Biochem J
DOI: 10.1042/bj2820091 PubMed 1371669
6
Cooke RM, Harvey TS, Campbell ID. (1991). Biochemistry
DOI: 10.1021/bi00236a022 PubMed 2036417
7
Tomas FM, Knowles SE, Owens PC, Read LC, Chandler CS, Gargosky SE, Ballard FJ. (1991). Biochem J
DOI: 10.1042/bj2760547
8
Tomas FM, Knowles SE, Owens PC, Read LC, Chandler CS, Gargosky SE, Ballard FJ. (1991). J Endocrinol
PubMed 1999680
9
Lemmey AB, Martin AA, Read LC, Tomas FM, Owens PC, Ballard FJ. (1991). Am J Physiol
PubMed 1996625
10
Martin AA, Tomas FM, Owens PC, Knowles SE, et al. (1991). Am J Physiol-Renal
DOI: 10.1152/ajprenal.1991.261.4.F626
11
Gillespie C, Read LC, Bagley CJ, Ballard FJ. (1990). J Endocrinol
DOI: 10.1677/joe.0.1270401 PubMed 2280209
12
Bagley CJ, May BL, Szabo L, McNamara PJ, Ross M, Francis GL, Ballard FJ, Wallace JC. (1989). Biochem J
DOI: 10.1042/bj2590665
13
Ross M, Francis GL, Szabo L, Wallace JC, Ballard FJ. (1989). Biochem J
Source
14
Carlsson-Skwirut C, Lake M, Hartmanis M, Hall K, Sara VR. (1989). Biochim Biophys Acta
DOI: 10.1016/0167-4889(89)90209-7 PubMed 2469478
15
Francis GL, Upton FM, Ballard FJ, McNeil KA, Wallace JC. (1988). Biochem J
DOI: 10.1042/bj2510095 PubMed 3390164
16
Szabo L, Mottershead DG, Ballard FJ, Wallace JC. (1988). Biochem Biophys Res Commun
DOI: 10.1016/0006-291x(88)90580-3
17
Ballard FJ, Francis GL, Ross M, Bagley CJ, May B, Wallace JC. (1987). Biochem Biophys Res Commun
DOI: 10.1016/0006-291x(87)90380-9
18
Sara VR, Carlsson-Skwirut C, Andersson C, Hall E, Sjögren B, Holmgren A, Jörnvall H. (1986). Proc Natl Acad Sci USA
DOI: 10.1073/pnas.83.13.4904 PubMed 3460078
19
Francis GL, Read LC, Ballard FJ, Bagley CJ, Upton FM, Gravestock PM, Wallace JC. (1986). Biochem J
DOI: 10.1042/bj2330207 PubMed 3954725

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