IFN-beta Protein, Human (CHO)

IFN-beta is a secretory cytokine produced by cells under viral infection or nucleic acid stimulation. IFNβ binds to cell surface heterodimeric receptors (IFNAR1/IFNAR2), activates the JAK-STAT signaling pathway, and induces the expression of interferon-stimulated genes (ISGs) (such as PKR, 2'5'-OAS). IFN-beta inhibits viral proliferation, regulates immune responses (such as inhibiting Th1 cell polarization, reducing pro-inflammatory cytokine secretion), inhibits the proliferation of vascular smooth muscle cells and tumor cells. IFN-beta has anti-atherosclerotic and vascular remodeling effects. IFN-beta Protein, Human (CHO) is a recombinant interferon-beta protein (CHO), expressed by CHO, without a tag.

IFN-beta belongs to the type I interferon family^[2][3][7]. IFN-beta is a secreted cytokine produced by cells in response to viral infection or nucleic acid stimulation^[2][5][7]. IFN-beta binds to cell surface heterodimeric receptors (IFNAR1/IFNAR2), activates the JAK-STAT signaling pathway, and induces the expression of interferon-stimulated genes (ISGs) (such as PKR, 2'5'-OAS)^[2][3][4][7]. IFN-beta inhibits viral proliferation, regulates immune responses (such as inhibiting Th1 cell polarization and reducing the secretion of pro-inflammatory cytokines), inhibits the proliferation of vascular smooth muscle cells and tumor cells. IFN-beta has anti-atherosclerotic and vascular remodeling effects^[2][5][6][7]. IFN-beta is expressed in tissues such as the spleen, lungs, and kidneys, as well as in vascular endothelial cells and immune cells^[5][7]. IFN-beta, Human is a 166-amino acid protein with 35% sequence identity to the consensus sequence of IFN-α and 50% sequence identity to murine IFN-β (muIFN-β)^[8].

IFN-beta Protein, Human (10 U/mL; 48-96 h) inhibits bFGF mRNA and protein expression in a cell density-dependent manner in human renal cell carcinoma SN12PM6 cells^[5].

IFN-beta Protein, Human (25 μg; i.p.; 3 times; days 1, 3, and 10) induces T cell proliferative responses to human IFNβ in BALB/cByJ mice^[4].

1.Measured in antiviral assays using WISH cells infected with vesicular stomatitis virus and the ED₅₀ is 1-20 pg/mL.
2.Determined by a cytotoxicity assay using human TF-1 cells. The ED₅₀ for this effect is <0.1 ng/mL, corresponding to a specific activity of >1 x 10⁷ units/mg.

• 
  Determined by a cytotoxicity assay using human TF-1 cells. The ED₅₀ for this effect is 0.07167 ng/mL, corresponding to a specific activity of 1.395 x 10⁷ units/mg.

Human

CHO

Tag Free

P01574 (M22-N187)

3456  [NCBI]

Full Length of Mature Protein

MSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN

Approximately 20-23 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1. Lyophilized from a 0.22 μm filtered solution of acetate buffer solution 5% trehalose, 5% mannitol, 0.01% Tween-80.
2. Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
3. Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
4. Lyophilized from a 0.22 μm filtered solution of 40 mM Arg, 0.12 mg/ml DL-Methionine, 146 mg/ml sucrose, 0.1% PF₆₈, pH 4.5, 5% trehalose, 5% mannitol, 0.01% Tween-80.
5. Lyophilized from a 0.22 μm filtered solution of 10 mM NaAC, 40 mM Arg, 0.12 mg/ml DL-Methionine, 146 mg/ml sucrose, 0.1% PF68, pH 4.5, 5% trehalose, 5% mannitol, 0.01% Tween-80 .
Please refer to the lot-specific COA for specific buffer information.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. 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]. Jeannin S, et al. Response to interferon-Beta treatment in afro-caribbeans with multiple sclerosis. Mult Scler Int. 2011;2011:950126.  [Content Brief]

  [2]. Stübgen JP. Recombinant interferon-beta therapy and neuromuscular disorders. J Neuroimmunol. 2009 Jul 25;212(1-2):132-41.  [Content Brief]

  [3]. Abraham A K, et al. Mechanisms of interferon-β effects on bone homeostasis. Biochemical pharmacology, 2009, 77(12): 1757-1762.

  [4]. Yeung VP, et al. Elimination of an immunodominant CD4+ T cell epitope in human IFN-beta does not result in an in vivo response directed at the subdominant epitope. J Immunol. 2004 Jun 1;172(11):6658-65.  [Content Brief]

  [5]. Singh R, et al. Cell density-dependent modulation of basic fibroblast growth factor expression by human interferon-beta. Int J Oncol. 1996 Apr;8(4):649-56.  [Content Brief]

  [6]. Fraser-Smith EB, et al. Enhanced efficacy of the acyclic nucleoside 9-(1,3-dihydroxy-2-propoxymethyl)guanine in combination with beta-interferon against herpes simplex virus type 2 in mice. Antimicrob Agents Chemother. 1984 May;25(5):563-5.  [Content Brief]

  [7]. Zhang LN, et al. Interferon-beta attenuates angiotensin II-accelerated atherosclerosis and vascular remodeling in apolipoprotein E deficient mice. Atherosclerosis. 2008 Mar;197(1):204-11.  [Content Brief]

  [8]. Karpusas M, et al. The crystal structure of human interferon beta at 2.2-A resolution. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11813-8.  [Content Brief]