IL-12 beta Protein, Human (HEK293)

IL-12 beta Protein, also known as natural killer cell stimulatory factor 2, is a common subunit (p40) of IL-12 and IL-23. IL-12 is a inflammatory factor expressed by activated macrophages, and involves in Th1-type immune response against cancer^[1]. IL-12 beta Protein located outside the cell membrane, involves in singalling mediated by Jak-STAT^[3]. IL-12 beta Protein consists of 328 amino acids (M1-S328) with a fibronectin type-III domain (237-328 a.a). IL-12 beta Protein, Human (I23-S328) is produced in HEK293 cells with tag free.

IL-12 beta Protein, as known as IL12 p40 subunit or IL-12B, heterodimerizes with the IL-12 p35 subunit (IL-12A) to form IL-12 and with the IL23 p19 subunit to form IL-23, exerting different regulating functions^[1].
IL-12 and IL23 belong to IL-12 family, are involved in proinflammatory responses and expressed by activated macrophages that serve as an essential inducer of Th1 cells development^[2].
IL-12 signals via IL-12Rβ1 and IL-12Rβ2 mediated by p-STAT4, whereas IL-23 signals via IL-12Rβ1 and IL-23R mediated by p-STAT1 and p-STAT3^[3].
The sequence of amino acids in IL-12 beta proteins of human is very different from mouse (69.04%) and rat (69.04%).
Interleukin 12 (IL-12) family have been known to be inflammatory factors, induce autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis^[4].

Recombinant human (rh)IL-12 results in memory-like NK cell differentiation and enhanced responses against cancer^[5].
The combination of IL-12 (30 ng/mL) and IL-15 (100 ng/mL) induce IFN-γ secretion in natural killer (NK) cells^[6].

Human

HEK293

Tag Free

P29460 (I23-S328)

3593  [NCBI]

IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS

40-47 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. 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.

• [1]. Lu X. Impact of IL-12 in Cancer. Curr Cancer Drug Targets. 2017;17(8):682-697.  [Content Brief]

  [2]. Gunsten S, et al. IL-12 p80-dependent macrophage recruitment primes the host for increased survival following a lethal respiratory viral infection. Immunology. 2009 Apr;126(4):500-13.  [Content Brief]

  [3]. Gotthardt D, Trifinopoulos J, Sexl V, Putz EM. JAK/STAT Cytokine Signaling at the Crossroad of NK Cell Development and Maturation. Front Immunol. 2019 Nov 12;10:2590.  [Content Brief]

  [4]. Tait Wojno ED, Hunter CA, Stumhofer JS. The Immunobiology of the Interleukin-12 Family: Room for Discovery. Immunity. 2019 Apr 16;50(4):851-870.  [Content Brief]

  [5]. Becker-Hapak MK, et al. A Fusion Protein Complex that Combines IL-12, IL-15, and IL-18 Signaling to Induce Memory-Like NK Cells for Cancer Immunotherapy. Cancer Immunol Res. 2021 Sep;9(9):1071-1087.  [Content Brief]

  [6]. Krämer B, et al. Do lambda-IFNs IL28A and IL28B act on human natural killer cells? Proc Natl Acad Sci U S A. 2011 Aug 23;108(34):E519-20; author reply E521-2.  [Content Brief]