Recombinant Human IL-12 Protein

Product Discontinued

Recombinant Human IL-12 Protein Summary

• Description: A biologically active protein corresponding to the signal peptide and the mature IL-12 alpha chain sequence, and the signal peptideand the mature IL-12 beta chain sequence of IL12A.Source: modified human 293 cells
• Protein/Peptide Type: Biologically Active Protein
• Gene: IL12A

Applications/Dilutions

• Dilutions:
  • Block/Neutralize
  • Functional
  • Western Blot
• Application Notes: This protein is functionally active and can be used for Blocking and Neutralizing. It can also be used for Western Blot

Reactivity Notes

This is a Human protein

Packaging, Storage & Formulations

• Storage: Store at -80C. Avoid freeze-thaw cycles.
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute with 0.5 ml sterilized PBS. After reconstitution the buffer solution will contain 1% human serum albumin and 10% trehalose already present in the vial.

Alternate Names for Recombinant Human IL-12 Protein

• CLMF p35
• CLMF1
• Cytotoxic lymphocyte maturation factor 35 kDa subunit
• IL-12 subunit p35
• IL12
• IL-12
• IL-12, subunit p35
• IL12A
• interleukin 12, p35
• interleukin 12A (natural killer cell stimulatory factor 1, cytotoxic lymphocytematuration factor 1, p35)
• interleukin-12 alpha chain
• interleukin-12 subunit alpha
• natural killer cell stimulatory factor 1, 35 kD subunit
• NF cell stimulatory factor chain 1
• NK cell stimulatory factor chain 1
• NKSF1
• p35

Background

Human interleukin 12 (IL-12, IL12) is a pro-inflammatory cytokine that consists of a heterodimer comprising two disulfide-linked subunits, the alpha chain (the p35 subunit, IL-12A) and the beta chain (the p40 subunit, IL-12B). IL-12A is synthesized as a 219 amino acid peptide including a 22 amino acid signal sequence and has 2 potential N-linked glycosylation sites and a theoretical molecular mass of approximately 22 kDa. IL-12B is synthesized as a 328 amino acid peptide including a 22 amino acid signal sequence and has two potential N-linked glycosylation sites and a theoretical molecular mass of 35 kDa. Expression of the alpha chain and beta chain is regulated independently as the genes for the different subunits are located on different chromosomes. The majority of cell types have the ability to express the alpha chain. However, beta chain expression is restricted to dendritic cells, phagocytic cells and cells of the monocyte/macrophage lineage and B cells. It is these cells that predominantly express functional IL-12. IL-12 production is induced by both innate and adaptive immune responses. Induction via the innate immune response involves pathogen products such as bacterial LPS and various cell wall components, CpG nucleic acids and double stranded RNA. Additionally, the process of phagocytosis of bacteria also induces IL-12. The induction of IL-12 expression via the adaptive immune response involves the interaction of antigen presenting cells (APC) with TH cells, through CD40-CD40L interaction. Additionally, cross-linking of MHC II by TCR or CD4 induces IL-12. Importantly, at least two different signals are required for the induction of IL-12: CD40 ligation and a co-stimulatory cytokine, a bacterial product and IFN gamma, or CD40L and bacterial product. IL-12 plays a crucial role in regulating both cell mediated and innate immunity. Specifically, it is the major cytokine responsible for inducing T helper 1 (TH1) cell, cytotoxic T-cell (CTL) and natural killer (NK) cell immune responses. Furthermore, IL-12 acts on T cells, and NK cells, stimulating proliferation and inducing the production of interferon-gamma (IFN-gamma). IL-12 also promotes the proliferation and differentiation of naive CD4+ T cells into TH1 cells that produce IFN-gamma, which in turn enhances IL-12 production in dendritic cells and phagocytes resulting in a strong positive feedback mechanism leading to a powerful cell mediated immune response. This is a HCX protein. HCX Expression System Details HCX proteins mimic the proteins in the human body because they are expressed from human, rather than animal, insect or bacterial cells. This process gives them human post-translational modifications. Recombinant DNA techniques allow a human protein with the correct amino acid sequence to be expressed in a non-human cell line. However, non-human cells lack the appropriate cellular machinery, such as specific glycosyltransferases, necessary to produce the correct human post-translational modifications of a protein. An extreme example is seen in E. coli cells, which produce recombinant proteins with no glycosylation, as the above figure illustrates. Rodent and yeast cells are able to glycosylate proteins, but they are still different from glycosylation in human cells. Expression System Resultant Proteins Human (e.g. K562, HEK293) Correct amino acid sequence Human post-translational modifications Rodent (e.g. CHO, NSO) Correct amino acid sequence Some natural glycosylation - not human-like Yeast (e.g. Pichia) Correct amino acid sequence Some natural glycosylation - not human-like E.Coli Correct amino acid sequence No PTMs Although there have been significant attempts to make non-human cell derived cytokines more human-like, there is a growing awareness that in many instances, particularly in therapeutics, cytokines should mimic those found in the body as closely as possible.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 2 years from date of receipt.

Bioinformatics

• Gene Symbol: IL12A