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SRP3062

Sigma-Aldrich

IGF-Binding Protein 1 human

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

Synonym(s):

IBP-1, Placenta Protein 12 (PP12)

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About This Item

UNSPSC Code:
51111800
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

potency

<0.5 μg/mL

mol wt

25.4 kDa

packaging

pkg of 25 μg

technique(s)

cell culture | mammalian: suitable

impurities

<0.1 EU/μg endotoxin, tested

color

white to off-white

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... IGFBP1(3484)

General description

Insulin-like growth factor-binding proteins (IGF-BPs) form high affinity complexes with both insulin-like growth factor- I and II (IGF-I and IGF-II). Currently there are seven named IGF-BPs. Insulin-like growth factor-binding protein-1 (IGF-BP1) is a 25.4kDa cysteine-rich secreted protein. It is the most abundant IGF-BP in amniotic fluid and is expressed in liver, decidua and kidneys. Levels of IGF-BP1 in serum are lowest after food. It binds to both IGF-I and IGF-II with equal affinity. Phosphorylated IGF-BP1 hinders IGF actions, whereas non-phosphorylated IGF-BP1 is stimulatory. Recombinant human IGF-BP1 is a 25.4kDa protein consisting of 235 amino acid residues (Isoform A).

Biochem/physiol Actions

Insulin-like growth factor-binding proteins (IGF-BPs) control the distribution, function and activity of insulin-like growth factors (IGFs) in various cell tissues and body fluids. They prolong the half-life of IGFs. Insulin-like growth factor-binding protein-1 (IGF-BP1) has been shown to have a role in the development and advancement of cancers. It is downregulated in hepatocellular carcinoma.

Sequence

MAPWQCAPCS AEKLALCPPV SASCSEVTRS AGCGCCPMCA LPLGAACGVA TARCARGLSC RALPGEQQPL HALTRGQGAC VQESDASAPH AAEAGSPESP ESTEITEEEL LDNFHLMAPS EEDHSILWDA ISTYDGSKAL HVTNIKKWKE PCRIELYRVV ESLAKAQETS GEEISKFYLP NCNKNGFYHS RQCETSMDGE AGLCWCVYPW NGKRIPGSPE IRGDPNCQIY FNVQN

Physical form

Lyophilized from 10 mM Sodium Phosphate, pH 7.5.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Over-expression of insulin-like growth factor binding protein-related protein-1(IGFBP-rP1/mac25) in the M12 prostate cancer cell line alters tumor growth by a delay in G1 and cyclin A associated apoptosis.
Ezzat V.A., et al.
Diabetes, obesity & metabolism, 3, 198-211 (2008)
Hiroyasu Kamei et al.
PloS one, 3(8), e3091-e3091 (2008-09-05)
Gene duplication is the primary force of new gene evolution. Deciphering whether a pair of duplicated genes has evolved divergent functions is often challenging. The zebrafish is uniquely positioned to provide insight into the process of functional gene evolution due
Maaria Ikonen et al.
Proceedings of the National Academy of Sciences of the United States of America, 100(22), 13042-13047 (2003-10-17)
Insulin-like growth factor-binding protein-3 (IGFBP-3) regulates IGF bioactivity and also independently modulates cell growth and survival. By using a yeast two-hybrid screen to identify IGFBP-3-interacting proteins, we cloned humanin (HN) as an IGFBP-3-binding partner. HN is a 24-aa peptide that
Carnosine decreases IGFBP1 production in db/db mice through suppression of HIF-1.
Forsberg EA
The Journal of Endocrinology, 225(3), 159-167 (2015)
The extracellular regulation of growth factor action.
Flaumenhaft R
Molecular Biology of the Cell, 3(10), 1057-1065 (1992)

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