Human LIF Antibody

Catalog #: MAB2501 Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
MAB2501
MAB2501-SP

Detection of LIF in HepG2 Human Cell Line by Flow Cytometry.

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Human LIF Antibody Summary

Species Reactivity

Human

Specificity

Detects human LIF in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant mouse LIF, recombinant human (rh) CLC, rhCNTF, rhCardiotrophin-1, rhIL-6, rhIL-11, or rhOSM is observed.

Source

Monoclonal Mouse IgG₁ Clone # 9808

Purification

Protein A or G purified from hybridoma culture supernatant

Immunogen

E. coli-derived recombinant human LIF

Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Label

Unconjugated

Applications

Recommended Concentration

Sample

Western Blot

1 µg/mL

Recombinant Human LIF

CyTOF-ready

Ready to be labeled using established conjugation methods. No BSA or other carrier proteins that could interfere with conjugation.

Intracellular Staining by Flow Cytometry

0.25 µg/10⁶ cells

See below

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Intracellular Staining by Flow Cytometry

Detection of LIF antibody in HepG2 Human Cell Line antibody by Flow Cytometry.

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Detection of LIF in HepG2 Human Cell Line by Flow Cytometry. HepG2 human hepatocellular carcinoma cell line was stained with Mouse Anti-Human LIF Monoclonal Antibody (Catalog # MAB2501, filled histogram) or isotype control antibody (Catalog # MAB002, open histogram) followed by APC-conjugated Goat anti-Mouse IgG Secondary Antibody (Catalog # F0101B). To facilitate intracellular staining, cells were fixed and permeabilized with FlowX FoxP3 Fixation & Permeabilization Buffer Kit (Catalog # FC012). View our protocol for Staining Intracellular Molecules.

Reconstitution Calculator

Preparation and Storage

Reconstitution

Reconstitute at 0.5 mg/mL in sterile PBS.

Shipping

The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: LIF

LIF is a 36‑67 kDa highly glycosylated polypeptide (1, 2) produced by a variety of cells including T cells (3), monocytes (4), fibroblasts (5), osteoblasts (6) and mast cells (7). Consistent with its many synonyms, LIF exhibits a broad spectrum of effects on both hematopoietic and nonhematopoietic cells. For example, LIF inhibits the differentiation of embryonic stem cells (8), up regulates the synthesis of acute phase proteins in hepatocytes (9), down regulates lipoprotein lipase activity in adipocytes (10), and preferentially induces a cholinergic phenotype in sympathetic neurons (11). The receptor for LIF (LIF R) has been isolated and found to be a 190 kDa type I transmembrane glycoprotein (12). Although this molecule binds LIF, the resultant LIF-LIF R complex is not sufficient to transduce an intracellular signal. This capability is provided by a 130 kDa signal transducing subunit (gp130) that is common to the functional receptors for IL-6, IL-11, CNTF, and Oncostatin M (13, 14). Since gp130 is a ubiquitously expressed membrane protein, the presence of LIF R (membrane-bound or soluble form) ultimately determines the cell’s responsiveness to LIF. Cells known to express LIF R include osteoblasts (6), hepatocytes (15), macrophages (15), neurons (5), and megakaryocytes (16). Human and mouse LIF exhibit 78% sequence homology, and human LIF is biologically active on mouse cells.

References

Van-Vlasselaev, P. et al. (1992) Prog. Growth Factor Res. 4:337.
Gough, N.M. (1992) Growth Factors 7:175.
Anegon, N.M, I. et al. (1991) J. Immunol.147:3973.
Gillett, N.A. et al. (1993) Growth Factors 9:301.
Banner, L. R. and P.H. Patterson (1994) Proc. Natl. Acad. Sci. 91:7109.
Allen, E.H. et al. (1990) J. Cell. Physiol. 145:110.
Lorenzo, J.A. et al. (1994) Clin.Immunol. Immunopathol. 70:260.
Williams, R.L. et al. (1988) Nature 336:684.
Baumann, H. et al. (1989) J. Immunol. 143:1163.
Marshall, M.K. et al. (1994) Endocrinology 135:1412.
Ludham, W.H. et al. (1994) Dev. Biol. 164:5283.
Davis, S. et al. (1993) Science 260:18054.
Gearing, D.P. et al. (1991) EMBO J. 10:28395.
Gearing, D.P. et al. (1991) Science 255:1434.
Hilton, D.J. and N.A. Nicola (1992) J. Biol. Chem. 267:102286.
Hilton, D.J. et al. (1992) Ciba17. Foundation Symposium 167:2278.

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