Recombinant Human IL12A

• Cat.No.: IL12A-219H

Specification

• Cat. No.: IL12A-219H
• Description: Interleukin 12 (IL-12, NK cell stimulatory factor, cytotoxic lymphocyte maturation factor) is a heterodimeric cytokine that is naturally produced by dendritic cells , macrophages and human B-lymphoblastoid cells (NC-37) in response to antigenic stimulation. IL-12 is involved in the differentiation of naive T cells into Th1 cells, which is important in resistance against pathogens. It is known as a T cell stimulating factor, which can stimulate the growth and function of T cells. It stimulates the production of IFN-γ and TNF-α from T and natural killer (NK) cells, and reduces IL-4 mediated suppression of IFN-γ. IL-12 also has anti-angiogenic activity, which can block the formation of new blood vessels. IL-12 binds to the IL-12 receptor and upon binding, IL-12R-β2 becomes tyrosine phosphorylated and provides binding sites for kinases, Tyk2 and Jak2. These are important in activating critical transcription factor proteins such as STAT4 which are implicated in IL-12 signaling in T cells and NK cells. IL-12 contributes to the antimycobacterial immune response by enhancing production of interferon-gamma, facilitating development of Th1 cells and augmenting cytotoxicity of antigen-specific T cells and natural killer cells.
• Source: Sf21 Insect Cells.
• Molecular Weight: The predicted molecular weight of Recombinant Human IL-12 is Mr 75 kDa.
• State Of Matter: Lyophilized.
• Formulation: This recombinant protein solution was 0.2 µm filtered and formulated in modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives present.
• Purity: > 97% by SDS Page and analyzed by silver stain.
• Endotoxin: < 1.0 EU/µg as determined by the LAL method.
• Biological Activity: The biological activity of Human Interleukin-12 is determined by the stimulation of IFN-gamma from NK cells co-stimulated with IL-18. The expected ED50 for this effect is <1.0 ng/ml, corresponding to a specific activity of >1 x 106 units/mg.
• Storage And Stability: This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
• Tag: Non

Gene Information

• Gene Name: IL12A interleukin 12A (natural killer cell stimulatory factor 1, cytotoxic lymphocyte maturation factor 1, p35) [ Homo sapiens ]
• Synonyms: NKSF1; CTL maturation factor (TCMF); Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35); TSF; Edodekin-alpha; IL-12 p35; SGT2; FLJ39002; CLMF; IL-12A; NFSK; P35; Cytotoxic lymphocyte maturation factor 35 kDa subunit; IL-12 subunit p35; IL-12, subunit p35; NF cell stimulatory factor chain 1; cytotoxic lymphocyte maturation factor 1, p35; interleukin 12, p35; interleukin 12A; interleukin 12A (natural killer cell stimulatory factor 1,cytotoxic lymphocytematuration factor 1, p35); interleukin-12 alpha chain; natural killer cell stimulatory factor 1, 35 kD subunit 2; IL12A
• Gene ID: 3592
• mRNA Refseq: NM_000822
• Protein Refseq: NP_000873
• UniProt ID: P29459
• Chromosome Location: 3q25.33-q26
• MIM: 161560
• Pathway: Allograft rejection; Cytokine-cytokine receptor interaction; Jak-STAT signaling pathway; RIG-I-like receptor signaling pathway; Toll-like receptor signaling pathway; Type I diabetes mellitus
• Function: contributes_to cytokine activity; contributes_to growth factor activity; interleukin-12 beta subunit binding; interleukin-12 receptor binding; interleukin-27 binding; protein binding; protein heterodimerization activity

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.