Recombinant Human CD207 (N-6His)

Recombinant Human CD207 (N-6His)

Size1:10μg price1:$98
Size2:50μg price2:$248
Size3:500μg price3:$1680
SKU: PHH2056 Category: Target Proteins Tags: ,

Datasheet

Name

Recombinant Human CD207 (N-6His)

Purity

Greater than 95% as determined by reducing SDS-PAGE

Endotoxin level

<1 EU/µg as determined by LAL test.

Construction

Recombinant Human C-type Lectin Domain Family 4 Member K is produced by our Mammalian expression system and the target gene encoding Tyr64-Pro328 is expressed with a 6His tag at the N-terminus.

Accession #

AAH22278.1

Host

Human Cells

Species

Human

Predicted Molecular Mass

31.5 KDa

Buffer

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Form

Lyophilized

Shipping

The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.

Stability&Storage

Store at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.

Reconstitution

Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

 

 

 

Alternative Names

CD207 antigen; langerin; CD207; C-type lectin domain family 4 member K

 

Background

Langerin (CD207) is a type II transmembrane glycoprotein which is member K of the C-type lectin domain family. Langerin is used as a marker for Langerhans cells (LCs) which represent the immature dendritic cells in the epidermis. Langerin is necessary and sufficient for Birbeck granule formation. Human langerin sequence contains a 43 aa cytoplasmic domain, a 21 aa transmembrane domain and a 264 aa extracellular domain (ECD) that contains a coiled-coil domain and a single C-type lectin domain. Human langerin shares 68%, 62%, 71% aa identity with mouse, rat and bovine langerin ECD, respectively. Trimerization greatly increases the lectin binding affinity. Langerin internalizes endogenous proteins such as type I procollagen. Internalization by LC is thought to lead to suppression of self reactions. Langerin also mediates endocytosis of non-peptide antigens containing mannose, N-acetyl glucosamine and fucose that are expressed by mycobacteria and fungae.

 

Note

For Research Use Only , Not for Diagnostic Use.