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MIF-H82E7-25ug MIF-H82E7-200ug

Biotinylated Human MIF Protein, His,Avitag™

ACROBiosystems

DETAILS

  • Tag: C-10×His & C-Avi
  • Host: HEK293
  • Size: 25ug
  • Buffer: 25 mM MES, 500 mM NaCl, pH6.5
  • Format: Powder
  • Purity: 90%
  • Storage: -20℃
  • Category: MABSol® Biotin Labeled Proteins
  • Molecule: MIF
  • Accession: NP_002406.1
  • Conjugate: Biotin-labeled
  • Stability: ● -20°C to -70°C for 12 months in lyophilized state; ● -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.
  • Background: Macrophage migration inhibitory factor(MIF) is also known as Glycosylation-inhibiting factor(GIF), L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase. Interacts with CXCR2 extracellular domain, CD74 extracellular domain, COPS5 and BNIPL. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity.
  • Exp Region: Pro 2 - Ala 115
  • Swiss-prot: P14174-1
  • Characteristics: This protein carries a polyhistidine tag at the C-terminus, followed by an Avi tag (Avitag™). The protein has a calculated MW of 16.0 kDa. The protein migrates as 20 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
  • Endotoxin Level: 1.0 EU per μg
  • Molecular Weight: 16.0 kDa
  • Shipping Condition: RT
  • Species Reactivity: Human
  • Extra Shippinghandling Fee: Please see 'Shipping-and-Payments' sheet. Website: https://www.acrobiosystems.com/A48-Shipping-and-Payments.html

DESCRIPTION

Biotinylated Human MIF, His,Avitag (MIF-H82E7) is expressed from human 293 cells (HEK293). It contains AA Pro 2 - Ala 115 (Accession # P14174-1).