Recombinant Human Interferon-Alpha2c, Yeast

2-1-1-green-tea-extract-1

Recombinant Human Interferon-Alpha2c, Yeast

Cat. No.: SPODRP01358
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Product Details

Source: Yeast
Molecular Weight: Approximately 19.3 kDa, a single polypeptide chain containing 165 amino acids.
AA Sequence: CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE
Purity: > 97% by SDS-PAGE and HPLC analyses.
Biological Activity: Fully biologically active when compared to standard. The activity is determined by the cytopathic effect inhibition assay.
Physical Appearance: Sterile filtered white lyophilized (freeze-dried) powder.
Formulation: Lyophilized from a 0.2 µm filtered solution in PBS, pH7.4, with 0.02% Tween-20.
Endotoxin: Less than 0.1 EU/µg of rHuIFN-α2c, Yeast as determined by LAL method.
Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
1 month, 2 to 8°C under sterile conditions after reconstitution.
3 months, -20 to -70°C under sterile conditions after reconstitution.
Background: IFN-αs are proteins released by leukocytes, primarily active in the innate immune response against viral infections. The IFN-α family comprises 13 subtypes and 23 different variants. These proteins typically range in molecular mass from 19 to 26 kDa and are composed of 156-166 or 172 amino acids. They share a conserved sequence region from amino acid positions 115 to 151, while their amino-terminal ends vary. Many IFN-α subtypes differ by only one or two amino acid positions in their sequences. Additionally, naturally occurring variants include proteins truncated by 10 amino acids at the carboxy-terminal end.

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