Cat. No.: | SPODRP01358 |
Size: | |
Quantity: |
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Pricey: | Inquiry |
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. |