IGFBP6 (28-240) Human

Insulin Like Growth Factor Binding Protein-6 (28-240 a.a.) Human Recombinant
Cat. No.
BT16855
Source
E.coli.
Synonyms
Insulin-like growth factor-binding protein 6, IBP-6, IGF-binding protein 6, IGFBP-6, IGFBP6, IBP6.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

IGFBP6 Human Recombinant produced in E. coli is a single polypeptide chain containing 236 amino acids (28-240) and having a molecular mass of 25.0kDa (Molecular size on SDS-PAGE will appear higher).
IGFBP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
IGFBP6 is a protein that has a role in lipoprotein assembly and the absorption of cholesterol from the diet. In addition to its acyltransferase activity, it may function as a ligase. It may supply cholesteryl esters needed for lipoprotein secretion from hepatocytes and intestinal mucosa.
Description
Recombinant Human IGFBP6, produced in E. coli, is a single polypeptide chain consisting of 236 amino acids (28-240). It has a molecular mass of 25.0 kDa. Note that the molecular size on SDS-PAGE will appear higher. This IGFBP6 protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile filtered solution.
Formulation
The IGFBP6 solution is provided at a concentration of 0.5 mg/ml and contains 20 mM Tris-HCl buffer (pH 8.0), 0.15 M NaCl, 20% glycerol, and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For longer storage periods, it is recommended to store the product frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 85% by SDS-PAGE analysis.
Synonyms
Insulin-like growth factor-binding protein 6, IBP-6, IGF-binding protein 6, IGFBP-6, IGFBP6, IBP6.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRCPGCGQ GVQAGCPGGC VEEEDGGSPA EGCAEAEGCL RREGQECGVY TPNCAPGLQC HPPKDDEAPL RALLLGRGRC LPARAPAVAE ENPKESKPQA GTARPQDVNR RDQQRNPGTS TTPSQPNSAG VQDTEMGPCR RHLDSVLQQL QTEVYRGAQT LYVPNCDHRG FYRKRQCRSS QGQRRGPCWC VDRMGKSLPG SPDGNGSSSC PTGSSG.

Product Science Overview

Structure and Function

IGFBP-6 is an O-linked glycoprotein that binds IGF-II with marked preferential affinity over IGF-I . The protein prolongs the half-life of IGFs and can either inhibit or stimulate their growth-promoting effects on cell culture . It alters the interaction of IGFs with their cell surface receptors, thereby modulating their biological activity . IGFBP-6 is involved in various cellular processes, including cell migration and the positive regulation of the stress-activated MAPK cascade .

Recombinant Human IGFBP-6

Recombinant human IGFBP-6 (rhIGFBP-6) is synthesized using eukaryotic expression systems, such as COS-7 monkey kidney cells . This recombinant form is similar to IGFBP-6 purified from human cerebrospinal fluid in terms of IGF binding and O-glycosylation . The recombinant protein has been used in various studies to understand its role in cellular differentiation and its interaction with IGFs.

Biological Implications

IGFBP-6 has been shown to inhibit IGF-II-induced differentiation of L6A1 myoblasts in a dose-dependent manner . This inhibition is complete when rhIGFBP-6 is present in a slight molar excess. In contrast, rhIGFBP-6 does not affect IGF-I-induced differentiation, even when present in a five-fold molar excess . These findings highlight the specificity of IGFBP-6 for IGF-II and its potential role in regulating IGF-II-mediated cellular processes.

Clinical Significance

IGFBP-6 is implicated in various diseases and conditions. It is a biomarker for breast cancer, in situ carcinoma, leiomyoma, and neovascular inflammatory vitreoretinopathy . Additionally, it is involved in obesity and has been studied for its role in cell migration and the activation of the MAPK signaling pathway .

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