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Description
Rat CGA Protein, His TagProduct Specification Species Rat Synonyms Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follicle stimulating hormone alpha chain (FSH alpha), Follitropin alpha chain, Luteinizing hormone alpha chain (LSH alpha), Lutropin alpha chain, Thyroid stimulating hormone alpha chain (TSH alpha), Thyrotropin alpha chain, Cga1 Accession P11962 Amino Acid Sequence Protein sequence (P11962, Leu25 Ser120, with C
Product Specification
| Species | Rat |
| Synonyms | Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follicle-stimulating hormone alpha chain (FSH-alpha), Follitropin alpha chain, Luteinizing hormone alpha chain (LSH-alpha), Lutropin alpha chain, Thyroid-stimulating hormone alpha chain (TSH-alpha), Thyrotropin alpha chain, Cga1 |
| Accession | P11962 |
| Amino Acid Sequence | Protein sequence (P11962, Leu25-Ser120, with C-His Tag) LPDGDLIIQGCPECKLKENKYFSKLGAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKSFTKATVMGNARVENHTDCHCSTCYYHKS |
| Expression System | HEK293 |
| Molecular Weight | Predicted MW: 12.3 kDa Observed MW: 24 kDa |
| Purity | ＞95% by SDS-PAGE |
| Endotoxin | <1EU/μg |
| Conjugation | Unconjugated |
| Physical Appearance | Lyophilized powder |
| Storage Buffer | Lyophilized from a 0.2 μm filtered solution of 0.2M PBS, pH7.4 with 3% trehalose. |
| Reconstitution | Reconstitute no more than 1 mg/mL according to the size in deionized water after rapid centrifugation. |
| Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied. |
Background
Glycoprotein hormones alpha chain (CGA) is a common subunit shared by several pituitary glycoprotein hormones, including thyroid-stimulating hormone (TSH), follicle-stimulating hormone (FSH), luteinizing hormone (LH), and chorionic gonadotropin (CG). It is encoded by a single gene and non-covalently associates with unique hormone-specific beta subunits to form biologically active heterodimers. This 14-20 kDa polypeptide is heavily modified by N-linked glycosylation, which is critical for proper protein folding, heterodimer assembly, and biological activity.
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