Human LIF Antibody

Catalog #: MAB2502 Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
MAB2502-100
MAB2502-SP

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Summary Data Examples Preparation and Storage Reconstitution Calculator Background Product Datasheets Related Research Areas

Human LIF Antibody Summary

Species Reactivity

Human

Specificity

Detects human LIF in direct ELISA

Source

Monoclonal Mouse IgG_2B Clone # 945842

Purification

Protein A or G purified from hybridoma culture supernatant

Immunogen

Human embryonic kidney cell, HEK293-derived human LIF
Met1-Phe202
Accession # P15018

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

ELISA

This antibody functions as an ELISA capture antibody when paired with Goat Anti-Human LIF Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF250).

This product is intended for assay development on various assay platforms requiring antibody pairs. We recommend the Human LIF DuoSet ELISA Kit (Catalog # DY7734-05) for convenient development of a sandwich ELISA.

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

ELISA

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Human LIF ELISA Standard Curve. Recombinant Human LIF protein was serially diluted 2-fold and captured by Mouse Anti-Human LIF Monoclonal Antibody (Catalog # MAB2502) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Human LIF Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF250) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).

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