Mouse Alpha-2-HS-Glycoprotein (AHSG) Protein
234€ (2 µg)
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Name
Mouse Alpha-2-HS-Glycoprotein (AHSG) Protein
Category
Proteins and Peptides
Provider
Abbexa
Reference
abx680166
Tested Applications
SDS-PAGE
Description
Mouse Alpha-2-HS-Glycoprotein (AHSG) Protein is a recombinant protein produced in Sf9, Baculovirus cells.
Documentos del producto
Instrucciones
Data sheet
Especificaciones del producto
| Category | Proteins and Peptides |
| Immunogen Target | Alpha-2-HS-Glycoprotein (AHSG) |
| Host | Insect |
| Origin | Mouse |
| Conjugation | Unconjugated |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 2 µg |
| Size 2 | 10 µg |
| Size 3 | 1 mg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Dry Ice | No |
| Alias | AHSG A2HS,alpha-2-HS-glycoprotein,Fetuin A |
| Background | Protein AHSG |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. |
Background
Fetuin-A, also known as alpha-2-HS-glycoprotein (AHSG), is a circulating glycoprotein primarily synthesized by the liver. It plays diverse roles in the body, including regulation of mineral metabolism, inhibition of pathological calcification, modulation of insulin signaling, and regulation of inflammation. Fetuin-A functions as an inhibitor of ectopic mineralization by forming soluble complexes with calcium and phosphate ions, preventing their precipitation in soft tissues. Additionally, fetuin-A interacts with various receptors and signaling pathways, influencing insulin sensitivity and glucose homeostasis. Dysregulation of fetuin-A levels has been implicated in metabolic disorders such as diabetes, cardiovascular disease, and chronic kidney disease. Understanding the molecular mechanisms underlying fetuin-A function provides insights into its roles in health and disease, offering potential therapeutic targets for metabolic and cardiovascular conditions. Ongoing research continues to elucidate the multifaceted functions of fetuin-A and its implications for human health
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