LIFR Protein, Rat (HEK293, His)

LIFR protein is an important member of the type I cytokine receptor family, mediating cellular responses to a variety of cytokines, emphasizing its role in cell differentiation and immune regulation. LIFR Protein, Rat (HEK293, His) is the recombinant rat-derived LIFR protein, expressed by HEK293 , with C-His labeled tag.

The LIFR Protein is a significant member of the type I cytokine receptor family, specifically categorized within the Type 2 subfamily, highlighting its essential role in mediating cellular responses to various cytokines. As part of this receptor family, LIFR likely shares conserved structural and functional features with related receptors, emphasizing its involvement in transducing signals from specific type I cytokines. The classification within the type I cytokine receptor family underscores its specific designation within the broader context of cell signaling, providing insights into its unique contributions to processes such as cell differentiation and immune regulation. The study of LIFR contributes to our understanding of its role in physiological processes, offering potential applications in therapeutic interventions for conditions related to cell differentiation and immune response modulation. Further exploration of LIFR's role holds promise for enhancing our knowledge of its contributions to both normal cellular function and pathological conditions.

1.Measured by its binding ability in a functional ELISA. Immobilized Mouse LIF hFc at 2 μg/mL (100 μl/well) can bind Rat LIFR His , the EC₅₀ of Rat LIFR His is 300-700 ng/mL.
2.Measured by its ability to inhibit the recombinant human LIF mediated inhibition in the M1 mouse myeloid leukemia cells. The ED₅₀ for this effect is typically 5-40 ng/mL in the presence of 2 ng/mL recombinant human LIF.

Rat

HEK293

C-His

G3V7K2 (L44-S829)

81680  [NCBI]

Partial

LKRGVQQDLKCTTNNMRVWDCSWPAPLGVSPGTVKDICIKDRPHSCHRLETTNVKIPALSPGDHEVTINYQNGFQSKFTLNEKDVSLVPDTPEILSLSADFSTSTLQLKWNDKGSALPYPSNATWEVKVLQNPRTEPVALVSLNTVLSGKDKGHHWNWTSELPLQCATHSVSIRWHIDYPRFSGYKEWSEWSPLKNISWTRNTETNVFPQDKVVLAGSNMTICCISTTKVLSGQIGNTFRPLIHLYGETVAIHILNIPVSENSGSNVIFSTVDDVYGTVVFAGYPPDVPQKLSCETHDLKEIICSWNPGRITGLVGPRNTEYTLFESISGKSAVFHRFEELANETYWLTLKMAPDQEIHNFTLTARNPLGQTESAIVINATERVALHVPISLKVKDVNSTVVTLSWYLPGNFTKINLVCQIEICKANSKKEVRNVTMRGAEDSTYHVAVDKLNPYTIYTFRVRCSSETFWKWSKWSNEKRYLTTEATPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSSEETQSLSEILDPQHKAEIKVNKNDYIISVVARNSAGSSPPSKIASMEIPNDDITVEQAVGIGNRIFLSWQHNPNMTCDYVIKWCNSSWSEPCLLDWIKVPSNSTGTVIESDQFQPGVRYNFYLYGCTNQGYQLLRSTIGYIEELAPIVAPNFTVEDTSADSILVKWDDIPVEELRGFLRGYLFYFQKGERDTPKTRSLETSHSDIKLKNITDISQKTLRIADLQGKTSYHLVLRAYTHGGLGPEKSMFVVTKENS

Approximately 116 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 5% trehalose, 5% mannitol and 0.01% Tween 80.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.