Gibco

Human IGFBP-4 Recombinant Protein, PeproTech®

Product Details

350-05B-20UG

Applications

Tested Dilution

Publications

Functional Assay (Functional)

Assay-dependent

In vitro Assay (IV)

View 4 publications 4 publications

Product Specifications

Species

Human

Published species

Human

Expression System

Insect cells

Amino acid sequence

DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE

Molecular weight

25.7 kDa

Class

Recombinant

Type

Protein

Purity

≥ 95% by SDS-PAGE gel and HPLC analyses.

Endotoxin concentration

<1 EU/µg

Activity

Determined by its ability to inhibit IGF-I induced proliferation of FDC-P1 cells.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

purified

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Ambient

Product Specific Information

350-05B-1MG will be provided as 4 x 250 µg (350-05B-250UG).

350-05B-500UG will be provided as 2 x 250 µg (350-05B-250UG).

Recombinant Human IGF-BP4 is a 25.7 kDa protein consisting of 237 amino acid residues including, the IGF-BP domain and thyroglobulin type-I domain.

This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Target Information

This gene is a member of the insulin-like growth factor binding protein family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors I and II and circulates in the plasma in both glycosylated and non-glycosylated forms. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

Product References

Significant polyomic and functional upregulation of the PAPP-A/IGFBP-4/5/IGF-1 axis in chronic rhinosinusitis with nasal polyps.

International forum of allergy & rhinology

Mueller SK,Nocera AL,Workman A,Libermann T,Dillon ST,Stegmann A,Wurm J,Iro H,Wendler O,Bleier BS

Wed Apr 01 00:00:00 EDT 2020

Neural Precursor-Derived Pleiotrophin Mediates Subventricular Zone Invasion by Glioma.

Cell

Qin EY,Cooper DD,Abbott KL,Lennon J,Nagaraja S,Mackay A,Jones C,Vogel H,Jackson PK,Monje M

Thu Aug 24 00:00:00 EDT 2017

Heparin-binding domain of fibrin(ogen) binds growth factors and promotes tissue repair when incorporated within a synthetic matrix.

Proceedings of the National Academy of Sciences of the United States of America

Martino MM,Briquez PS,Ranga A,Lutolf MP,Hubbell JA

Tue Mar 19 00:00:00 EDT 2013

Cyr61/CCN1 displays high-affinity binding to the somatomedin B(1-44) domain of vitronectin.

PloS one

Francischetti IM,Kotsyfakis M,Andersen JF,Lukszo J

Fri Feb 26 00:00:00 EST 2010

Bioinformatics

Protein Aliases: IBP-4; IGF-binding protein 4; IGFBP; Insulin like growth factor binding protein; insulin-like growth factor binding protein 4; Insulin-like growth factor-binding protein 4