Recombinant Human LH alpha/beta Heterodimer Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human LH alpha/beta Heterodimer Protein Summary

Details of Functionality
Measured by its ability to induce cAMP accumulation in MLTC‑1 mouse Leydig tumor cells. Rebois, R.V. et al. (1982) J. Cell Biol. 94:70. The ED50 for this effect is 0.25-2.5 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human LH alpha/beta Heterodimer protein
Ala25-Ser116 ( alpha chain) & Ser21-Leu141 ( beta chain)
Accession #
N-terminal Sequence
Ala25 ( alpha chain), Ser21 ( beta chain)
Structure / Form
Non-covalent heterodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
10 kDa ( alpha chain), 13 kDa ( beta chain).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
15-26 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human LH alpha/beta Heterodimer Protein

  • LH alpha/beta Heterodimer

Background

Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha  and beta  chains. The alpha  subunit (CG alpha ) is also a component of Follicle-Stimulating Hormone (FSH), Thyroid-Stimulating Hormone, and Chorionic Gonadotropin. The unique beta  subunit confers the protein’s specific biological action and is responsible for the interaction with its receptor (1, 2). The approximately 20 kDa human CG alpha subunit shares 73% and 72% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively. The approximately 18 kDa human LH beta subunit shares 71% and 72% aa sequence identity with the mouse and rat orthologs, respectively. Multiple isoforms of LH exist due to differences in the post-translational glycosylation, sialylation, and sulphation modifications of its subunits (3-6). The composition, longevity, and activity of the different LH isoforms vary throughout a woman’s menstrual cycle and reproductive life cycle (7). LH is produced and secreted by the anterior pituitary gland. Its secretion is controlled by Gonadotropin-Releasing Hormone from the hypothalamus; however, LH secretion can also be stimulated by estradiol (7, 8). LH works in concert with FSH to regulate female reproduction; FSH stimulates follicular growth and LH induces ovulation (9). LH also drives formation of the corpus luteum by promoting progesterone production (7). Additionally, LH has been suggested to stimulate the adrenal gland in postmenopausal women to induce secretion of sulfated DHEA, a precursor to androgens (10, 11). In the testis, LH induces Leydig cell production of testosterone (7). Hypersecretion of LH has been shown to occur in women with polycystic ovary syndrome and is associated with an increased risk of infertility and miscarriage (12, 13). Additionally, increased serum LH levels are associated with decreased cognition and have been implicated in the development and progression of Alzheimer’s disease (14, 15).
  1. Keutmann, H.T. et al. (1987) Proc. Natl. Acad. Sci. USA 84:2038.
  2. Keutmann, H.T. et al. (1992) Mol. Endocrinol. 6:904.
  3. Wilson, C.A. et al. (1990) J. Endocrinol. 125:3.
  4. Stanton, P.G. et al. (1993) J. Endocrinol. 138:529.
  5. Stanton, P.G. et al. (1996) Mol. Cell. Endocrinol. 125:133.
  6. Bergendah, M. and J.D. Veldhuis (2001) Hum. Reprod. 16:1058.
  7. Choi, J. and J. Smitz (2014) Mol. Cell. Endocrinol. 383:203.
  8. Marshall, J.C. et al. (1993) Trans. Am. Clin. Climatol. Assoc. 104:31.
  9. Raju, G.A. et al. (2013) J. Hum. Reprod. Sci. 6:227.
  10. Alevizaki, M. et al. (2006) Eur. J. Endocrinol. 154:875.
  11. Moran, F.M. et al. (2013) Menopause 20:329.
  12. Balen, A.H. (1995) J. R. Soc. Med. 88:339P.
  13. Blank, S.K. et al. (2006) Hum. Reprod. Update 12:351.
  14. Webber, K.M. et al. (2007) Clin. Med. Res. 5:177.
  15. Blair, J.A. et al. (2015) Front. Endocrinol. (Lausanne) 6:45.

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