Active Recombinant Mouse IL12A&IL12B protein, His-tagged

• Cat.No.: IL12A&IL12B-28M
• Product Overview: This product contains IL12A & IL12B heterodimer. A DNA sequence encoding the p35 subunit of mouse IL12, termed as IL12A (P43431) (Met 1-Ala 215) was fused with a polyhistidine tag at the C-terminus, constructed the plasmid 1; A DNA sequence encoding the p40 subunit of mouse IL12, termed as IL12B (P43432) (Met 1-Ser 335) was fused with a polyhistidine tag at the C-terminus, constructed the plasmid 2. The two plasmids were co-expressed and the heterodimer was purified.

Specification

• Source: HEK293
• Species: Mouse
• Tag: His
• Form: Lyophilized from sterile PBS, pH 7.4
• Bio-activity: 1. Measured by its ability to bind biotinylated recombinant mouse IL12A&IL12BRB2 in a functional ELISA.
  2. Measured by its ability to induce Interferon gamma secretion by human natural killer lymphoma NK-92 cells. The ED50 for this effect is 2-10 ng/mL.
• Molecular Mass: The recombinant mouse IL12A&IL12B heterodimer of IL12A&IL12BA/IL12A&IL12BB, comprises 528 (204 + 324) amino acids and has a calculated molecular mass of 60.3 (23.1 + 37.2) kDa. The apparent molecular mass of rh IL12A&IL12B heterodimer is approximately 28 & 47 kDa respectively in SDS-PAGE under reducing conditions.
• Protein Length: Met 1-Ala 215&Met 1-Ser 335
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Purity: > 90 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C
  Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Reviews

01/14/2021

Suitable for co-immunoprecipitation.

12/21/2020

Consistent in bioactivity.

11/16/2020

Good for receptor binding studies.

Q&As

How do mass spectrometry-based techniques reveal post-translational modifications on IL12A?

Mass spectrometry identifies IL12A's post-translational modifications and their roles.

What strategies validate IL12A's role in immune response modulation using knockout models?

Knockout models validate IL12A's roles in immune response modulation.

How do protein footprinting assays unveil IL12A's binding interfaces with receptor partners?

Protein footprinting assays reveal IL12A's binding interfaces with receptors.

What experimental methods quantify IL12A's secretion kinetics and stability in cell culture?

ELISA and stability assays quantify IL12A secretion and stability in culture.

Can you discuss the use of SPR in characterizing IL12A's interactions with antibodies and inhibitors?

SPR characterizes IL12A's interactions with antibodies and inhibitors.

What cellular assays assess IL12A's ability to induce cytokine production in immune cells?

Cellular assays gauge IL12A's cytokine induction in immune cells.

How does isothermal titration calorimetry provide insights into IL12A's binding affinity with receptors?

Isothermal titration calorimetry measures IL12A's binding affinity with receptors.

What techniques evaluate the impact of IL12A genetic variants on protein structure and function?

Structural biology techniques analyze IL12A genetic variant impacts.

Could you elaborate on the use of site-directed mutagenesis in probing IL12A's functional domains?

Site-directed mutagenesis probes IL12A's functional domains and interactions.

How does in vivo bioluminescence imaging track IL12A expression dynamics in living organisms?

Bioluminescence imaging tracks IL12A expression dynamics in vivo.