prospec

IFN g Human

  • Name
  • Description
  • Pricings
  • Quantity
  • IFN g Human
  • Interferon-Gamma Human Recombinant
  • Shipped at Room temp.

Catalogue number

CYT-206

Synonyms

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Introduction

IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

Description

Interferon-gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa.
The IFN-gamma is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation

The protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 4.6.

Solubility

It is recommended to reconstitute the lyophilized Interferon-gamma in sterile distilled water or 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability

Lyophilized Interferon gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Amino acid sequence

MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFQGR RASQ.

Biological Activity

The specific activity as determined in a viral resistance assay is < 0.05 ng/ml, corresponding to a specific activity of 2.0 x 10,000,000 IU/mg.

Protein content

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.640 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
2. Analysis by RP-HPLC, using a calibrated solution of IFN-g as a Reference Standard.

Usage

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

References

1.Title:Candida albicans abrogates the expression of interferon-?-inducible protein-10 in human keratinocytes.
Publication:Article first published online: 18 JUL 2008DOI: 10.1111/j.1574-695X.2008.00457.x
Link:http://onlinelibrary.wiley.com/doi/10.1111/j.1574-695X.2008.00457.x/full

2. Title: Rifampin Augments Cytokine-Induced Nitric Oxide Production in Human Alveolar Epithelial Cells
Publications:  Antimicrobial agents and chemotherapy 50.1 (2006): 396-398
Link: http://aac.asm.org/content/50/1/396.full

3.Title: Selective Activation of Human Dendritic Cells by OM-85 through a NF-kB and MAPK Dependent Pathway
Publications:  PloS one 8.12 (2013): e82867
Link: http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0082867#pone-0082867-g005

4.Title: A New Strategy to Induce Effective Antitumour Response In Vitro and In Vivo
Publications:   Scandinavian journal of immunology 68.3 (2008): 287-296
Link:  http://onlinelibrary.wiley.com/doi/10.1111/j.1365-3083.2008.02140.x/full

5.Title: Capture of Tumor Cell Membranes by Trogocytosis Facilitates Detection and Isolation of Tumor-Specific Functional CTLs
Publication:  Cancer research 68.6 (2008): 2006-2013.
Link: http://cancerres.aacrjournals.org/content/68/6/2006.full

6. Title: Curcumin induces maturation-arrested dendritic cells that expand regulatory T cells in vitro and in vivo
Publication:   Clinical & Experimental Immunology 162.3 (2010): 460-473.
Link: http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2249.2010.04232.x/full

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