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Pregnant Mare Serum Gonadotropin CAS: 9002-70-4

Place of Origin: Sichuan,China (Mainland)
cas: 9002-70-4
Brand: MOSINTER
storage condition: -20°C
solubility: saline: 1 mL/vial
Merck: 13,2237
form: lyophilized powder

  • 9002-70-4
  • MOSINTER
  • 9002-70-4
Product Description

Payment & Shipping Terms

Supply Capacity

Payment Terms:

T/T, WU

Production Capacity:

500kg/year

Min. Order:

1 Gram

Packing:

according to the customer's requirements 

Means of Transport:

Ocean, Air, Land

Delivery Date:

7 days

 

Pregnant mare serum gonadotropin

CAS: 9002-70-4

Item

Index

Specification

CP/USP/EP

Appearance

lyophilized powder

Solubility

saline: 1 mL/vial

 Storage   Condition

−20°C

 

Gonadotropins (or glycoprotein hormones) are protein hormones secreted by gonadotrope cells of the anterior pituitary of vertebrates. This is a family of proteins, which include the mammalian hormones follicle-stimulating hormone (FSH), luteinizing hormone (LH), placental chorionic gonadotropins hCG and eCG and chorionic gonadotropin (CG), as well as at least two forms of fish gonadotropins. These hormones are central to the complex endocrine system that regulates normal growth, sexual development, and reproductive function.The hormones LH and FSH are secreted by the anterior pituitary gland, while hCG and eCG are secreted by the placenta.

 

Natural types and subunit structure

The two principal gonadotropins in vertebrates are luteinizing hormone (LH) and follicle-stimulating hormone (FSH), although primates produce a third gonadotropin called chorionic gonadotropin (CG). LH and FSH are heterodimers consisting of two peptide chains, an alpha chain and a beta chain. LH and FSH share nearly identical alpha chains (about 100 amino acids long), whereas the beta chain provides specificity for receptor interactions. These subunits are heavily modified by glycosylation.

The alpha subunit is common to each protein dimer (well conserved within species, but differing between them), and a unique beta subunit, which confers biological specificity. The alpha chains are highly conserved proteins of about 100 amino acid residues which contain ten conserved cysteines all involved in disulfide bonds, as shown in the following schematic representation.

 

 


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