Recombinant Human CD43 protein (rFc Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg1761

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Validation Data Gallery

• 

  Purity of Recombinant Human CD43 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

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Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Human CD43 protein Ser20-Arg253 (Accession# P16150) with a rabbit IgG Fc tag at the C-terminus.
• GeneID: 6693
• Accession: P16150
• PredictedSize: 49.7 kDa
• SDS-PAGE: 52-100 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

CD43, also named leukosialin, sialophorin, galactoglycoprotein, leukocyte sialoglycoprotein, SPN, and is a mucin-like type I transmembrane protein. In humans, it is expressed in haematopoietic cells, including T lymphocytes, monocytes, granulocytes, natural killer cells, platelets, and haematopoietic stem cells, with the exception of mature erythrocytes and B cell subpopulations. CD43 can both induce and protect against apoptosis, and can either promote or block cell adhesion. The unglycosylated form of CD43 migrates on SDS-PAGE with a molecular weight of 54 kDa (PMID: 2943740), whereas CD43 from different haematopoietic cell lines displays increased molecular weights since it is glycosylated with O-linked chains that differ in core structure and sialylation.

References:

1. M Santamaría, et al. (1996) Cancer Res. 56(15):3526-9.
2. T J Brown, et al. (1996) J Biol Chem. 271(44):27686-95.
3. S R Carlsson, et al. (1986) J Biol Chem. 261(27):12779-86.