Mouse AGR2 / AG-2 Protein, His Tag (MALS verified)

製品番号/仕様
価格
Availability
数量
AG2-M52H6-100ug
$390.00
AG2-M52H6-1mg (500ug X 2)
$2,720.00
AG2-M52H6
製品金額 :
$ 0
推奨新製品 Request Quote
Contact Us
Contact Us
製品金額:
$ 0
  • 製品詳細
  • データ表示
  • Reviews & Citations
  • Important Statement
  • Resources
Synonyms

Anterior gradient protein 2 homolog, AG-2, hAG-2, HPC8, Secreted cement gland protein XAG-2 homolog, AGR2

Source

Mouse AGR2, His Tag (AG2-M52H6) is expressed from human 293 cells (HEK293). It contains AA Lys 21 - Leu 175 (Accession # O88312-1).

Predicted N-terminus: Lys 21

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 19.8 kDa. The protein migrates as 23 kDa and 24 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

The protein is designed as a dimer.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>95% as determined by SDS-PAGE.

>95% as determined by SEC-MALS.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Shipping and Storage

This product is shipped at ambient temperature.

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

バックグランド

Anterior gradient 2 (AGR2) is a normal endoplasmic reticulum protein that has two important abnormal functions, amphibian limb regeneration and human cancer metastasis promotion. These normal intracellular and abnormal extracellular roles can be attributed to the multidomain structure of AGR2. The NMR structure shows that AGR2 consists of an unstructured N-terminal region followed by a thioredoxin fold.