重组人干扰素- alpha 2a（rHuIFN-a 2a）

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CYT-204 重组人干扰素- alpha 2a（rHuIFN-a 2a）  20μg/100μg/1mg   Prospec

 

 

Background:
  At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.
 
Description :
  Recombinant Human IFN-alpha 2a produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19241 Dalton.
Interferon-alpha 2a gene was obtained from human leukocytes.
The IFN-a is purified by proprietary chromatographic techniques.
 
Physical Appearance:
  Sterile Filtered White lyophilized （freeze-dried） powder.
 
Formulation:
  Recombinant IFN-a is lyophilized from （1mg/ml） solution containing 7.21 sodium chloride and 0.77mg ammonium acetate.
Solubility:
  It is recommended to reconstitute the lyophilized IFN-alpha-2a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
 
Stability:
  Lyophilized IFN-alpha-2a although stable at room temperature for 3 weeks, should be stored desiccated below -18 C. Upon reconstitution IFN-alpha-2a 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 avoid freeze-thaw cycles.
 
Purity:
  Greater than 98.0% as determined by:
（a） Analysis by RP-HPLC.
（b） Anion-exchange FPLC.
（c） Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.
 
Amino acid sequence:
  The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Gln, conforming to the sequence of native human IFN-alpha . N-terminal methionine has been compley removed enzymatically.
 
Dimers and aggregates:
  Less than 1% as determined by silver-stained SDS-PAGE gel analysis.
 
Biological Activity:
  ProSpec's IFN-alpha 2a is fully biologically active when compared to standard. The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 2.7 x 108.
 
Endotoxin:
  Less than 0.1 ng/µg （IEU/µg） of rHuIFN-α 2a.
 
Protein content:
  Protein quantitation was carried out by two independent methods:

1. UV spectroscopy at 280 nm using the absorbency value of 0.924 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 （InliGenetics）.
2. Analysis by RP-HPLC, using a standard solution of IFN-alpha（2a） 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.

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