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Recombinant Human GPA33 / A33 Protein, His-Tag, 50 µg  

Recombinant Human GPA33 / A33 Protein, His-Tag, 50 µg

Recombinant Human GPA33 / A33 Protein, expressed from human HEK293 cells, His-Tag

Synonyms:recombinant, human, protein, GPA33,A33

More details

GP3-H5224-50

312,00 €

Background
Glycoprotein A33 (GPA33) is also known as Cell surface A33 antigen, is a single-pass type I membrane protein which is expressed in normal gastrointestinal epithelium and in 95% of colon cancers. GPA33 The predicted mature protein has a 213-amino acid extracellular region, a single transmembrane domain, and a 62-amino acid intracellular tail. The sequence of the extracellular region contains 1 Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain characteristic of the CD2 subgroup of the immunoglobulin (Ig) superfamily, which contains. GPA33 may play a role in cell-cell recognition and signaling.

Source
Human GPA33 / A33 Protein (Human GPA33, His Tag) Ile 22 - Val 235 (Accession # AAH74830) was produced in human 293 cells (HEK293)

Molecular Characterization
Human GPA33, His Tag is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 24.5 kDa. The predicted N-terminus is Ile 22. DTT-reduced Protein migrates as 35-40 kDa in SDS-PAGE due to glycosylation.

Endotoxin
Less than 1.0 EU per μg of the Human GPA33, His Tag by the LAL method.

Purity
>96% as determined by SDS-PAGE.

Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.

Reconstitution
See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower. Please avoid repeated freeze-thaw cycles. No activity loss is observed after storage at: 4-8°C for 12 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution.

References

(1) Heath JK., et al., 1997, Proc Natl Acad Sci U S A 94 (2): 469–74.
(2) Ritter G., et al., 1997, Biochem Biophys Res Commun 236 (3): 682–6.