SRP3065
IGF-Binding Protein 6 human
recombinant, expressed in (BTI-Tn-5B1-4) High-5 Insect Cells, ≥95% (SDS-PAGE), ≥95% (HPLC), suitable for cell culture
Sinónimos:
IBP-6
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About This Item
Código UNSPSC:
51111800
NACRES:
NA.32
En este momento no podemos mostrarle ni los precios ni la disponibilidad
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origen biológico
human
recombinante
expressed in (BTI-Tn-5B1-4) High-5 Insect Cells
Ensayo
≥95% (HPLC)
≥95% (SDS-PAGE)
Formulario
lyophilized
potencia
0.1-0.4 μg/mL
mol peso
23.0-30.0
envase
pkg of 20 μg
técnicas
cell culture | mammalian: suitable
impurezas
<0.1 EU/μg endotoxin, tested
color
white to off-white
Nº de acceso UniProt
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
Información sobre el gen
human ... IGFBP6(3489)
Categorías relacionadas
Descripción general
The IGFBP6 (insulin-like growth factor-binding protein 6) gene is mapped to human chromosome 12q13.[1] It belongs to the IGFBP family of proteins. The protein has a IGF (insulin-like growth factor)-binding site and a thyroglobulin type-1 domain.[2] IGFBPs are mainly required to regulate IGFs activities. IGFBP6 strongly interacts with IGF-2, but also interacts with IGF-1. It is also a hypoxia-inducible gene.[3][4]
Recombinant human IGF-BP6 has a calculated mass of 22.3kDa and consists of 213 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Recombinant human IGF-BP6 has a calculated mass of 22.3kDa and consists of 213 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Acciones bioquímicas o fisiológicas
IGFBP6 (insulin-like growth factor-binding protein 6) can suppress growth of various IGF-2 (insulin-like growth factor 2)-dependent tumors. However, it also exhibits IGF-independent activities.[3] IGFBP is suggested as a serum biomarker for proliferative vitreoretinopathy.[5] HIV (human immunodeficiency virus) infection results in downregulation of IGFBP6 via differential methylation.[6]
Secuencia
RCPGCGQGVQ AGCPGGCVEE EDGGSPAEGC AEAEGCLRRE GQECGVYTPN CAPGLQCHPP KDDEAPLRAL LLGRGRCLPA RAPAVAEENP KESKPQAGTA RPQDVNRRDQ QRNPGTSTTP SQPNSAGVQD TEMGPCRRHL DSVLQQLQTE VYRGAQTLYV PNCDHRGFYR KRQCRSSQGQ RRGPCWCVDR MGKSLPGSPD GNGSSSCPTG SSG
Forma física
Lyophilized from 10 mM Sodium Citrate, pH 3.5.
Reconstitución
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.
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Kininogen 1 and insulin-like growth factor binding protein 6: candidate serum biomarkers of proliferative vitreoretinopathy.
Yu J, et al.
Clinical & Experimental Optometry : Journal of the Australian Optometrical Association, 97, 72-72 (2014)
Whole genome methylation array reveals the down-regulation of IGFBP6 and SATB2 by HIV-1.
Zhang Y, et al.
Scientific Reports, 5, 10806-10806 (2015)
Leon A Bach
Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society, 15(3), 185-192 (2005-05-26)
Insulin-like growth factor binding protein (IGFBP)-6 is unique among IGFBPs for its IGF-II binding specificity. IGFBP-6 inhibits growth of a number of IGF-II-dependent cancers, including rhabdomyosarcoma, neuroblastoma and colon cancer. Although the major action of IGFBP-6 appears to be inhibition
IGF binding protein-6 expression in vascular endothelial cells is induced by hypoxia and plays a negative role in tumor angiogenesis.
Zhang C, et al.
International Journal of Cancer. Journal International Du Cancer, 130, 2003-2003 (2012)
Prohibitin-2 binding modulates insulin-like growth factor-binding protein-6 (IGFBP-6)-induced rhabdomyosarcoma cell migration.
Fu P, et al.
The Journal of Biological Chemistry, 288, 29890-29890 (2013)
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