Name :
Human LIF protein, Fc-fusion, biotinylated, recombinant
Description :
Leukemia inhibitory factor (LIF) is a member of a cytokine family that includes oncostatin M (OSM), granulocyte colony-stimulating factor (G-CSF), and interleukin 6 (IL-6). It shows a wide spectrum of biologic activities, including the growth promotion and differentiation of different types of cells, bone metabolism, cachexia, neural development, embryogenesis and inflammation. LIF has the capacity to induce differentiation in leukemic cells, embryonic stem cells, hematopoietic and neuronal cells. LIF is also a proinflammatory cytokine and induces the acute phase protein synthesis and affects the cell recruitment into the area of damage or inflammation. LIF has been implicate as an important factor for the development of the early embryo. LIF may also play a role in immune tolerance at the maternal-fetal interface. LIF supports the maintenance of mouse embryonic stem (ES) cell pluripotency and germline competency. LIF binds to the LIF receptor (LIFRα), which forms a heterodimer with a common β-subunit, GP130. This leads to activation and transduction of the JAK/STAT and MAPK signaling cascades. LIF is known as a direct transcriptional target of STAT5: STAT5 binds to LIF promoter and LIF expression is up-regulated after activation of the JAK2/STAT5 pathway. The LIF expression is significantly increased in patients with chronic myeloproliferative neoplasms. Owning to its pleiotropic functions, LIF has been involved in the pathogenesis of many diseases of various origins. Human LIF shows 80% sequence identity to mouse LIF.
Gene Symbol :
The recombinant human LIF-Fc fusion is expressed as a 419amino acid protein consisting of Ser23 – Phe202 region of (UniProt accession #P15018) and a C-terminal Fc from human IgG1, which exists as a dimer under non-reducing conditions.
NCBI Gene ID :
3976
Uniprot Entry :
P15018
Construct Details :
The recombinant human LIF-Fc fusion is expressed as a 419amino acid protein consisting of Ser23 – Phe202 region of (UniProt accession #P15018) and a C-terminal Fc from human IgG1, which exists as a dimer under non-reducing conditions.
Source :
Human cells stably expressing human LIF-Fc and growing in chemical-defined media with no animal components or antibiotics
Amino Acid Sequence: :
SPLPITPVNATCAIRHPCHNNLMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLDKLCGPNVTDFPPFH ANGTEKAKLVELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLCRLCSKYHVGHV DVTYGPDTSGKDVFQKKKLGCQLLGKYKQIIAVLAQAFGSTTENLYFQGSTGTHTCPPCPAPELLGGPSVF LFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQD WLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWES NGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
M.W. :
Calculated molecular mass (kDa): 46.5; Estimated by SDS-PAGE under reducing condition (kDa): 60-65 (probably due to glycosylation)
Calculated PI :
8.68
Calculated Extinction Coefficients :
(M-1 cm-1, at 280nm): 48080
Endotoxin Level :
>95% judged by SDS-PAGE under reducing condition (see the gel image above, labeled as DTT “+”)
Formulation :
Supplied at 0.5 mg/ml in sterile PBSpH7.4 (carrier & preservative free). The purified recombinant protein was labeled with Biotin (3-5 Biotin per molecule) using the standard procedure.
Endotoxin Level :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method
Biological Activity :
Stimulates TF-1 human erythroleukemic cell proliferation assay with an ED50 typically 0.1 – 0.2 ng/ml. Induce IL-6 secretion in M1 mouse myeloid leukemia cells. Supports the maintenance of embryonic stem (ES) cell pluripotency and germline competency.
Molecule Class :
Cytokine (secreted)
Gene Synonym :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method
Gene Family :
CDF; DIA; HILDA; MLPLI
Research Area :
Stem Cell
Pathway/Disease :
Cell Growth & Differentiation
Species :
Human
CD Antigen :
References :
1. EMBO J. 6:3995-4002 (1987) 2. Nature 336:690-692 (1988) 3. Proc. Natl. Acad. Sci. 85:2623-2627 (1988) 4. Cell 77:1101-1116 (1994) 5. Nat. Biotechnol. 22:707-716 (2004)
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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