Recombinant IFN-γ, Human 
Datasheet
COA
MSDS
SHIP
Recombinant :
Recombinant IFN-γ, Human Source :
Escherichia coli. Molecular Weight :
17kDa, observed by reducing SDS‐PAGE. Purity :
> 95% as analyzed by reducing SDS‐PAGE. Biological Activity :
ED50<0.05ng/ml, measured by cytotoxicity assay using HT‐29 cells. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
MQDPYVKEA ENLKKYFNAG HSDVADNGTL FLGILKNWKE ESDRKIMQSQ IVSFYFKLFK NFKDDQSIQK SVETIKEDMN VKFFNSNKKK RDDFEKLTNY SVTDLNVQRK AIHELIQVMA ELSPAAKTGK RKRSQMLFRG RRASQ Endotoxin :
<1 EU/μg, determined by LAL Reconstitution :
Reconstituted in ddH2O or PBS at 100 μg/ml. Storage :
Lyophilized recombinant human Interferon gamma (rhIFN‐γ) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhIFN-γ should be stable up to 1 week at 4°C or up to 2 months at -20°C. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
Human Interferon gamma (hIFN-γ) is amacrophage‐activating factor and the lone member of Interferon type II.The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and sets off IFN-γ/JAK/STAT pathway. IFN-γ signaling does diverse biological functions primarily related to host defense and immune regulation, including antiviral and antibacterial defense, apoptosis, inflammation, and innate and acquired immunity. While IFN-γ–induced inflammatory cascade summons a variety of immune‐related cell types, such as macrophages, natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), IFN-γ is also implicated in resistance to NK cell and CTL responses and in immune escape in a variety of cancers.Recombinant human Interferon gamma (rhIFN-γ) produced in E.coli is a non‐glycosylated polypeptide chain of 144 amino acids. A fully biologically active molecule, rhIFN-γ has a molecular mass of 17 kDa analyzed by reducing SDS‐PAGE and is obtained by proprietary refolding and chromatographic techniques at GenScript.
Recombinant IFN-γ, Human Source :
Escherichia coli. Molecular Weight :
17kDa, observed by reducing SDS‐PAGE. Purity :
> 95% as analyzed by reducing SDS‐PAGE. Biological Activity :
ED50<0.05ng/ml, measured by cytotoxicity assay using HT‐29 cells. Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
MQDPYVKEA ENLKKYFNAG HSDVADNGTL FLGILKNWKE ESDRKIMQSQ IVSFYFKLFK NFKDDQSIQK SVETIKEDMN VKFFNSNKKK RDDFEKLTNY SVTDLNVQRK AIHELIQVMA ELSPAAKTGK RKRSQMLFRG RRASQ Endotoxin :
<1 EU/μg, determined by LAL Reconstitution :
Reconstituted in ddH2O or PBS at 100 μg/ml. Storage :
Lyophilized recombinant human Interferon gamma (rhIFN‐γ) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhIFN-γ should be stable up to 1 week at 4°C or up to 2 months at -20°C. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
Human Interferon gamma (hIFN-γ) is amacrophage‐activating factor and the lone member of Interferon type II.The active form of IFN-γ is an antiparallel dimer that interacts with the receptor IFN-γR1 and sets off IFN-γ/JAK/STAT pathway. IFN-γ signaling does diverse biological functions primarily related to host defense and immune regulation, including antiviral and antibacterial defense, apoptosis, inflammation, and innate and acquired immunity. While IFN-γ–induced inflammatory cascade summons a variety of immune‐related cell types, such as macrophages, natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), IFN-γ is also implicated in resistance to NK cell and CTL responses and in immune escape in a variety of cancers.Recombinant human Interferon gamma (rhIFN-γ) produced in E.coli is a non‐glycosylated polypeptide chain of 144 amino acids. A fully biologically active molecule, rhIFN-γ has a molecular mass of 17 kDa analyzed by reducing SDS‐PAGE and is obtained by proprietary refolding and chromatographic techniques at GenScript.
Blocking peptide available as BK0080-100μgP