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Human CG alpha / CGA Protein  pdf  pdf  pdf


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CGA-H52H2-100ug
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Synonym

CGA,TSH-alpha,LSH-alpha,CG-alpha,FSH-alpha

Source

Human CG alpha, His Tag (CGA-H52H2) is expressed from human 293 cells (HEK293). It contains AA Ala 25 - Ser 116 (Accession # AAH20782).

Predicted N-terminus: Ala 25

Molecular Characterization

CG alpha(Ala 25 - Ser 116)AAH20782
Poly-his

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

The protein has a calculated MW of 12.1 kDa. The protein migrates as 22-26 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method.

Purity

>92% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.

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.

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:

  1. 4-8°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.
 

SDS-PAGE

Human CG alpha, His Tag (Cat. No. CGA-H52H2) SDS-PAGE gel

Human CG alpha, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 92%.

 

Background

Chorionic gonadotrophin subunit alpha (CGA),a member of the glycoprotein hormones subunit alpha family, is also known as glycoprotein hormones alpha chain, choriogonadotropin alpha chain, follicle-stimulating hormone alpha chain (FSH-alpha), luteinizing hormone alpha chain (LSH-alpha) and thyroid-stimulating hormone alpha chain (TSH-alpha). The hormones human chorionic gonadotropin (hCG), luteinizing hormone (LH), follicle-stimulating hormone (FSH), and thyroid-stimulating hormone (TSH) are dimers consisting of alpha and beta subunits that are associated noncovalently. The alpha subunits (CGA) of these four human glycoprotein hormones are nearly identical, however, their beta chains are unique and confer biological specificity.

References

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