Recombinant Human LIF, Biotinylated Protein

Carrier Free

Catalog # Availability Size / Price Qty
BT7734-025/CF

With Carrier

Catalog # Availability Size / Price Qty
BT7734-025

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Recombinant Human LIF, Biotinylated Protein Bioactivity
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Recombinant Human LIF, Biotinylated Protein Summary

Product Specifications

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 0.02-0.12 ng/mL.
Source
E. coli-derived human LIF protein
Pro24-Phe202
Accession #
N-terminal Sequence
Analysis
Pro24
Structure / Form
Biotinylated protein via amines
Predicted Molecular Mass
20 kDa (unlabeled)
SDS-PAGE
18-23 kDa, reducing conditions

Product Datasheets

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BT7734 (with carrier)

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BT7734/CF (carrier free)

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

BT7734

Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

BT7734/CF

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in PBS.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Data Image

Bioactivity Recombinant Human LIF, Biotinylated Protein Bioactivity View Larger

Both Recombinant Biotinylated Human LIF (Catalog # BT7734) and unlabeled Recombinant Human LIF (Catalog # 7734-LF) induce TF-1 human erythroleukemic cell proliferation. The ED50 for this effect is 0.02-0.12 ng/mL. The similarity in activity highlights that the biotinylated protein is fully functional.

Reconstitution Calculator

Reconstitution Calculator

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Background: LIF

LIF (leukemia inhibitory factor) is a widely expressed, highly and variably glycosylated, 32‑62 kDa, monomeric, pleiotropic cytokine in the IL‑6 family of helical cytokines (1‑4). The first exon encoding the signal sequence is alternately spliced, resulting in LIF-D, LIF-M, and LIF‑T mRNAs that produce secreted, extracellular matrix‑associated, and intracellular forms, respectively (5). LIF-D and LIF-M mRNAs produce identical 180 amino acid (aa) mature sequences (5). Mature human LIF (180 aa) shares 78%, 82%, 91%, 88 and 87% aa sequence identity with mouse, rat, canine, bovine, and porcine LIF, respectively. The LIF receptor is a heterodimer of a type I transmembrane ligand‑binding subunit, LIFR (gp190), and the type I transmembrane signal transducing subunit, gp130, signaling especially through STAT3 and JAK kinases (3, 4, 6). Gp130 and members of the LIFR family also mediate the biological effects of Oncostatin M, Cardiotrophin‑1, Galectin‑10, CNTF, IL‑6,
IL‑11, and IL‑27 (3, 6). A soluble LIFR has been reported in the mouse (7). Depending on the cells and their context, LIF either opposes or favors differentiation (3, 8). LIF produced by the uterine endometrium supports successful implantation of the embryo, promotes proliferation and maintenance of pluripotency in embryonic stem cells, and favors proliferation of progenitor cell types such as hematopoietic stem cells (3, 6, 8). However, excess LIF blocks differentiation of embryoid bodies, indicating the importance of LIF regulation (3, 6). LIF is produced by CD4+ T cells in response to activation, and is required by the thymic epithelium to support T cell maturation (3, 4). LIF expression is up‑regulated by neuronal injury, and promotes motor neuron survival and oligodendrocyte myelination (3, 4, 9). LIF is produced by the adrenal cortex and likely enhances its production of cortisol and aldosterone (10). LIF can function as an autocrine growth factor in some pancreatic cancers, but induces differentiation in the myeloid leukemic cell line M1 (2, 11). Tumor LIF can also induce formation of immunosuppressive tumor‑associated macrophages (12). LIF promotes endometrial remodeling and differentiation of adipocytes and cardiac smooth muscle cells (3, 4). It promotes regulatory T cell and inhibits Th17 cell differentiation, thus promoting tolerance, down‑regulating inflammation, and contributing to immune tolerance during pregnancy and in the nervous system (3, 4, 6, 8).

References
  1. Gough, N.M. et al. (1988) Proc. Natl. Acad. Sci. USA 85:2623.
  2. Moreau, J.F. et al. (1988) Nature 336:690.
  3. Trouillas, M. et al. (2009) Eur. Cytokine Netw. 20:51.
  4. Metcalfe, S.M. (2011) Genes Immun. 12:157.
  5. Voyle, R.B. et al. (1999) Exp. Cell Res. 249:199.
  6. Cheng, J.G. et al. (2001) Proc. Natl. Acad. Sci. USA 98:8680.
  7. Tomida, M. et al. (1993) FEBS lett. 334:193.
  8. Paiva, P. et al. (2009) Cytokine Growth Factor Rev. 20:319.
  9. Slaets, H. et al. (2010) Trends Mol. Med. 16:493.
  10. Bamberger, A.M. et al. (2000) Mol. Cell. Endocrinol. 162:145.
  11. Kamohara, H. et al. (2007) Int. J. Oncol. 30:977.
  12. Duluc, D. et al. (2007) Blood 110:4319.
Long Name
Leukemia Inhibitory Factor
Entrez Gene IDs
3976 (Human); 16878 (Mouse); 403449 (Canine)
Alternate Names
CDF; D Factor; DIA; differentiation inhibitory activity; differentiation stimulating factor; Differentiation-stimulating factor; Emfilermin; HILDA; HILDAcholinergic differentiation factor; leukemia inhibitory factor (cholinergic differentiation factor); leukemia inhibitory factor; LIF; Melanoma-derived LPL inhibitor; MLPLI

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