产品编号:I-374-1
产品描述:Recombinant Human IGFBP-5
反应种属:
实验方法:
标记:
规格:1mg
供应商:Leinco
价格(RMB):面议
订购:
说明书:
Recombinant Human Insulin-Like Growth Factor Binding Protein 5 (IGFBP-5)
Purified No Carrier Protein
(BP5)
Prod. No.: I-374
Source NSO Cells
Pkg. Size: 1 mg, 25 µg
Storage: -20°C to -70°C
Description
Background:
Insulin-like growth factor binding protein 5, also known as IGFBP5 is a member of the insulin-like growth factor binding protein (IGFBP) family that are cysteine-rich proteins that act as a carrier protein. It is expressed highly in the kidney. IGFBP-5 has an autonomous role in the regulation of cell fate in development and in tumourigenesis.1
Source
NSO Cells
Molecular Weight
The predicted molecular weight of Recombinant Human IGFBP-5 is Mr 28 kDa. However, the actual molecular weight as observed by migration on SDS Page is Mr 34 kDa.
State of Matter
Lyophilized
Formulation
This recombinant protein was lyophilized from a 0.2 μm filtered solution in 35% acetonitrile (CH3CN) and 0.1% trifluoroacetic acid (TFA).
Purity
>90% by SDS-PAGE and analyzed by silver stain.
Storage and Stability
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
Endotoxin
<1.0 EU/µg as determined by the LAL method
Biological Activity
The biological activity of Human IGFBP-5 was determined by by its ability to inhibit the biological activity of rhIGF-I or rhIGF-II on MCF-7 cells (Karey, K.P. et al., 1988, Cancer Research 48:4083). The expected ED50 for this effect is typically 0.5 - 1.5 μg/ml in the presence of 14 ng/ml rhIGF-II.
Each investigator should determine their own optimal working dilution for specific applications.
Amino Acid Sequence
epc dekalsmcpp splgcelvke pgcgccmtca laegqscgvy tercaqglrc lprqdeekpl hallhgrgvc lneksyreqv kierdsrehe epttsemaee tyspkifrpk htriselkae avkkdrrkkl tqskfvggae ntahpriisa pemrqeseqg pcrrhmeasl qelkasprmv pravylpncd rkgfykrkqc kpsrgrkrgi cwcvdkygmk lpgmeyvdgd fqchtfdssn ve
References
1. Jennifer M. Pell et al. (2004) J of Cell Science 117: 1737