Chorionic gonadotropin human
Catalog Number CG10
Storage Temperature –20 C
CAS RN 9002-61-3 The subunit has a molecular mass of 23 kDa, with a
Synonyms: hCG, Chorionogen polypeptide portion of 16.0 kDa and a carbohydrate
portion of 7.0 kDa is for the carbohydrate.
5,7,10,11
The
Product Description subunit is N-glycosylated at Asn and Asn . The
13 30 12
1
pI: 2.95 structure and location of the O-glycosidic carbohydrate
Extinction Coefficient: = 1.41 10 (280 nm)
2 M 4
units attached to the subunit of hCG, at Ser , Ser ,
121 127
1%
E = 3.6 (280 nm) 132 138
Ser , and Ser , have been investigated. The
13
subunit has been characterized by LC-MS. A
14
Human chorionic gonadotropin (hCG) is a glycoprotein MALDI mass spectrometry report on the glycoforms of
hormone produced by the chorionic tissue of the the hCG -core fragment has been published.
15
placenta. The glycoprotein hormone family includes
luteinizing hormone (LH), follicle-stimulating hormone When hCG was used in combination with recombinant
(FSH), and thyroid-stimulating hormone (TSH), in
interferon-, there was a significant cooperative
addition to hCG. The function of hCG is to maintain the
induction of nitric oxide synthesis (iNOS) in a dose-
corpus luteum and stimulate steroid secretion from the
dependent manner in mouse peritoneal macrophages.
ovary in the beginning stages of gestation. hCG
This suggests that hCG may provide a second signal
appears in the blood and urine during the first trimester 16
for synergistic induction of NO synthesis. hCG has
of early pregnancy, and levels decrease thereafter. It
3 been used as a biomarker for such conditions as
has been used for superovulation in animals. 17 18,19
epithelial cancer and germ cell tumors.
hCG consists of an subunit of 92 amino acids and a
Catalog Number CG10 is 0.2 m-filtered. A vial
subunit of 145 amino acids. The subunit is
1
contains 10,000 IU. The calculated value is based on
common among the family of glycoprotein hormones,
the USP method for human Chorionic Gonadotrophin to
whereas the hormone-specific subunit, which exhibits meet 10,000 IU per vial, with a tolerance of not less
different degrees of homology, may confer biologic than 80.0% (8,000 IU) and not more than 125.0%
1
specificity of the individual hormone. The amino acid (12,500 IU) of the potency stated.
sequences of the subunit and the subunit and
4,5 5,6
7
the crystal structure of hCG have been reported. NMR Preparation Instructions
studies of the subunit have been reported.
8,9
When the contents of a vial of CG10 are reconstituted
with water to an hCG concentration of 1,000 I.U./ml, the
The molecular mass of hCG is 37.9 kDa, with 31% hCG solution will also contain 0.01 M sodium
carbohydrate by weight. The theoretical molecular phosphate buffer, pH 7.2, and mannitol (stabilizer) at a
mass of 37.9 kDa is based on the native form, which concentration of 10 mg/mL. hCG is also soluble in
contains 2 subunits. The subunit has a molecular aqueous glycerol and glycols, and is insoluble in
mass of 14.9 kDa, with a polypeptide portion of 2
ethanol. Solutions should be sterile-filtered and not
10.2 kDa and a carbohydrate portion of 4.7 kDa. The autoclaved.
subunit is N-glycosylated at Asn and Asn .
52 78 8
Precautions and Disclaimer
This product is for R&D use only, and not for drug,
household, or other uses. Please consult the Safety
Data Sheet for information regarding hazards and safe
handling practices.
2
Storage/Stability 7. Lapthorn, A.J., et al., Nature, 369(6480), 455-461
Dilute aqueous solutions undergo rapid loss of activity (1994).
when stored frozen, or heated, or if excess acid or base 8. de Beer, T., et al., FEBS Lett., 348, 1-6 (1994).
is added. Gelatin and serum proteins help to stabilize 9. de Beer, T., et al., Eur. J. Biochem., 241(1), 229-
aqueous solutions of hCG. hCG is stable in a glycerol 242 (1996).
solution at 100 C for one hour.
20
10. Bahl, O.P., J. Biol. Chem., 244(4), 567-574 (1969).
11. Swaminathan, N., and Bahl, O. P., Biochem.
Solutions reconstituted in water can be stored at –20 C Biophys. Res. Commun., 40(2), 422-427 (1970).
as single-use aliquots. 12. Sisinni, L., and Landriscina, M., Adv. Exp. Med.
Biol., 867, 159-176 (2015).
References 13. Kessler, M.J., et al., J. Biol. Chem., 254(16), 7909-
1. The Merck Index, 13th ed., Entry# 2237. 7914 (1979).
2. Morgans, F.J., et al., Endocrinology, 94(6), 1601- 14. Black, R.S., and Bowers, L.D., Methods Mol. Biol.,
1606 (1974). 146, 337-354 (2000).
3. Hogan, B., et al., Manipulating the Mouse Embryo, 15. Jacoby, E.S., et al., Clin. Chem., 46(11), 1796-1803
A Laboratory Manual, 2nd ed., Cold Spring Harbor (2000).
Laboratory Press (Cold Spring Harbor, NY), p. 130 16. Kim, H. M., and Moon, Y. H., Biochem. Biophys.
(1994). Res. Commun., 229(2), 548-552 (1996).
4. Bellisario, R., et al., J. Biol. Chem., 248(19), 6796- 17. Iles, R.K., Mol. Cell. Endocrinol., 260-262, 264-270
6809 (1973). (2007).
5. Morgan, F.J., et al.,. J. Biol. Chem., 250(13), 5247- 18. Mitsios, J.V., et al., Clin. Biochem., 47(7-8), 632-
5258 (1975). 635 (2014).
6. Carlsen, R.B., et al., J. Biol. Chem., 248(19), 6810- 19. Barlow, L.J., et al., Nat. Rev. Urol., 7(11), 610-617
6827 (1973). (2010).
20. The Merck Index, 11th ed., Entry# 4534.
AI,GA,GCY,ARO,ALF,RXR,MAM 12/16-1
2016 Sigma-Aldrich Co. LLC. All rights reserved. SIGMA-ALDRICH is a trademark of Sigma-Aldrich Co. LLC, registered in the US and other
countries. Sigma brand products are sold through Sigma-Aldrich, Inc. Purchaser must determine the suitability of the product(s) for their
particular use. Additional terms and conditions may apply. Please see product information on the Sigma-Aldrich website at
www.sigmaaldrich.com and/or on the reverse side of the invoice or packing slip.
