Recombinant Human IL-12 Biotinylated Protein, CF

Biotinylated, Linked Heterodimer, GS Linker, Defined heterodimer stoichiometry
Catalog # Availability Size / Price Qty
BT10018-025
Recombinant Human IL-12 Biotinylated Protein Binding Activity.
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Recombinant Human IL-12 Biotinylated Protein, CF 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 by its binding ability in a functional ELISA. Whe Recombinant Human IL-12 R beta 1 Fc Chimera Protein  (Catalog # 839-B1) is immobilized at 1.00 µg/mL (100uL/well), Biotinylated Recombinant Human IL‑12 (Catalog # BT10018) binds with an ED50 of 40.0-400 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human IL-12 protein
Human IL-12p40
(Ile23-Ser328)
Accession # P29460.1
GSGSSRGGSGSGGSGGGGSKHuman IL-12p35
(Arg23-Ser219)
Accession # P29459.2
N-terminusC-terminus
Accession #
N-terminal Sequence
Analysis
Ile23
Structure / Form
GS-linked heterodimer
Biotinylated via Amines
Predicted Molecular Mass
59 kDa
SDS-PAGE
68-80 kDa, under reducing conditions.

Product Datasheets

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BT10018

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.

BT10018

Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 250 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.

Data Images

Binding Activity Recombinant Human IL-12 Biotinylated Protein Binding Activity. View Larger

Measured by its binding ability in a functional ELISA. When Recombinant Human IL-12 R beta 1 Fc Chimera Protein (839-B1) is immobilized at 1.00 µg/mL (100µL/well), Biotinylated Recombinant Human IL‑12 Protein (Catalog # BT10018) binds with an ED50 of 40.0-400 ng/mL

SDS-PAGE Recombinant Human IL-12 Biotinylated Protein SDS-PAGE. View Larger

2 μg/lane of Recombinant Human IL-12 Biotinylated Protein (Catalog # BT10018) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 68-80 kDa.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background:

Interleukin 12, also known as natural killer cell stimulatory factor (NKSF) or cytotoxic lymphocyte maturation factor (CLMF), is a pleiotropic cytokine originally identified in the medium of activated human B lymphoblastoid cell lines (1). The p40 subunit of IL-12 has been shown to have extensive amino acid sequence homology to the extracellular domain of the human IL-6 receptor while the p35 subunit shows distant but significant sequence similarity to IL-6, G-CSF, and chicken MGF (2, 3). These observations have led to the suggestion that IL-12 might have evolved from a cytokine/soluble receptor complex. Human and murine IL-12 share 70% and 60% amino acid sequence homology in their p40 and p35 subunits, respectively. IL-12 apparently shows species specificity with human IL-12 reportedly showing minimal activity in the murine system. IL-12 is produced by macrophages and B lymphocytes and has been shown to have multiple effects on T cells and natural killer (NK) cells (4). These effects include inducing production of IFN-gamma and TNF by resting and activated T and NK cells, synergizing with other IFN‑gamma inducers at both the transcriptional and post-transcriptional levels. This interaction induces IFN-gamma gene expression, enhancing the cytotoxic activity of resting NK and T cells, inducing and synergizing with IL-2 in the generation of lymphokine-activated killer (LAK) cells, acting as a co-mitogen to stimulate proliferation of resting T cells, and inducing proliferation of activated T and NK cells (5). Current evidence indicates that IL‑12, produced by macrophages in response to infectious agents, is a central mediator of the cell‑mediated immune response by its actions on the development, proliferation, and activities of TH1 cells. In its role as the initiator of cell-mediated immunity, it has been suggested that IL-12 has therapeutic potential as a stimulator of cell-mediated immune responses to microbial pathogens, metastatic cancers, and viral infections such as AIDS.

References
  1. Gubler, U. et al. (1991) Proc. Natl. Acad. Sci. 88:4143.
  2. Gearing, D. et al. (1991) Cell 66:9.
  3. Merberg, D. et al. (1992) Immunology Today 13:78.
  4. Wolf, S.F. et al. (1991) Journal of Immunology 146:3074.
  5. Airoldi, I. et al. (2000) Journal of Immunology 165:6880.

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