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Recombinant Human CD5 Protein, His Tag, 100µg  

Recombinant Human CD5 Protein, His Tag, 100µg

Recombinant Human CD5 /LEU1 Protein, Arg 25 - Pro 372, produced in human 293 cells (HEK293), His Tag

Synonym
recombinant, human, protein, CD5,LEU1

More details

CD5-H52H5-100

Availability: within 7 days

300,00 €

Background
T-cell surface glycoprotein CD5 is also known as Lymphocyte antigen T1/Leu-1 and LEU1,which is phosphorylated on tyrosine residues by LYN,so CD5 can create binding sites for PTPN6/SHP-1.CD5 may act as a receptor in regulating T-cell proliferation. CD5 is expressed at various developmental and activation stages on human B cells.CD5 is a well established negative regulator of TCR and BCR signalling.CD5-positive cells may also prevent the emergence of autoimmunity by provision of cytokines such as IL-10. Development,selection and function of different B- and T-cell subsets or their preferential survival may be directly or indirectly dependent on different glycan structures associated with CD5 or CD5-like molecules.

Source
Recombinant Human CD5 /LEU1 Protein (rh CD5 /LEU1) Arg 25 - Pro 372 (Accession # NP_055022) was produced in human 293 cells (HEK293) at ACROBiosystems.

Molecular Characterization
rh CD5 /LEU1 is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 40.5 kDa. The predicted N-terminus is Arg 25. DTT-reduced Protein migrates as 48-55 kDa in SDS-PAGE due to glycosylation.

Endotoxin
Less than 1.0 EU per μg of the rh CD5 /LEU1 by the LAL method.

Purity
>95% 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
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).

References

(1) van de Velde H., et al., 1991, Nature 351:662-665.
(2) Brill L.M., et al., 2004, Anal. Chem. 76:2763-2772.
(3) Rodamilans B., et al., 2007, J. Biol. Chem. 282:12669-12677.