Recombinant Human IFN-gamma, Animal-Free Protein
Recombinant Human IFN-gamma, Animal-Free Protein Summary
Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.
Product Specifications
The specific activity of recombinant human IFN-gamma is >2.0 x 107 IU/mg, which is calibrated against the human IFN-gamma Standard (NIBSC code: 87/586).
Gln24-Gln166, with an N-terminal Met
Based on MALDI-TOF mass spectrometric analysis, truncation of four amino acid residues from the C-terminus may be observed in the recombinant protein preparation.
Produced using non-animal reagents in an animal-free laboratory.
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
AFL285
Formulation | Lyophilized from a 0.2 μm filtered solution in Sodium Succinate, Mannitol and Tween® 80. |
Reconstitution | Reconstitute at 0.2 mg/mL in sterile, deionized water. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.
Scientific Data
Recombinant Human IFN-gamma (Catalog # AFL285) has a molecular weight (MW) of 34.1 kDa as analyzed by SEC-MALS, suggesting that this protein is a homodimer. MW may differ from predicted MW due to post-translational modifications (PTMs) present (i.e. Glycosylation).
Reconstitution Calculator
Background: IFN-gamma
Interferon-gamma (IFN-gamma ), also known as type II or immune interferon, exerts a wide range of immunoregulatory activities and is considered to be the prototype proinflammatory cytokine (1, 2). Mature human IFN-gamma exists as a non-covalently linked homodimer of 20‑25 kDa variably glycosylated subunits (3). It shares 90% amino acid (aa) sequence identity with rhesus IFN-gamma, 59%‑64% with bovine, canine, equine, feline, and porcine IFN‑ gamma, and 37%‑43% with cotton rat, mouse, and rat IFN-gamma. IFN-gamma dimers bind to IFN-gamma RI ( alpha subunits) which then interact with IFN-gamma RII ( beta subunits) to form the functional receptor complex of two alpha and two beta subunits. Inclusion of IFN-gamma RII increases the binding affinity for ligand and the efficiency of signal transduction (4, 5). IFN-gamma is produced by a variety of immune cells under inflammatory conditions, notably by T cells and NK cells (6). It plays a key role in host defense by promoting the development and activation of Th1 cells, chemoattraction and activation of monocytes and macrophages, up‑regulation of antigen presentation molecules, and immunoglobulin class switching in B cells. It also exhibits antiviral, antiproliferative, and apoptotic effects (6, 7). In addition, IFN-gamma functions as an anti-inflammatory mediator by promoting the development of regulatory T cells and inhibiting Th17 cell differentiation (8, 9). The pleiotropic effects of IFN-gamma contribute to the development of multiple aspects of atherosclerosis (7).
- Billiau, A. and P. Matthys (2009) Cytokine Growth Factor Rev. 20:97.
- Pestka, S. et al. (2004) Immunol. Rev. 202:8.
- Gray, P.W. and D.V. Goeddel (1982) Nature 298:859.
- Marsters, S.A. et al. (1995) Proc. Natl. Acad. Sci. 92:5401.
- Krause, C.D. et al. (2000) J. Biol. Chem. 275:22995.
- Schroder, K. et al. (2004) J. Leukoc. Biol. 75:163.
- McLaren, J.E. and D.P. Ramji (2009) Cytokine Growth Factor Rev. 20:125.
- Muhl, H. and J. Pfeilschifter (2003) Int. Immunopharmacol. 3:1247.
- Kelchtermans, H. et al. (2008) Trends Immunol. 29:479.
Manufacturing Specifications
Animal-Free Manufacturing ConditionsOur dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.
Production
- All molecular biology procedures use animal-free media and dedicated labware.
- Dedicated fermentors are utilized in committed animal-free areas.
Purification
- Protein purification columns are animal-free.
- Bulk proteins are filtered using animal-free filters.
- Purified proteins are stored in animal-free containers in a dedicated cold storage room.
- Low Endotoxin Level.
- No impairment of biological activity.
- High quality product obtained under stringent conditions.
- For ex vivo research or bioproduction, additional documentation can be provided.
FAQs
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