Recombinant Human CG alpha/beta (HCG) Heterodimer Protein
Recombinant Human CG alpha/beta (HCG) Heterodimer Protein Summary
Product Specifications
Human CG beta (Ser21-Gln165) Accession # P01233 |
Human CG alpha (Ala25-Ser116) Accession # P01215 | ||
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
7727-CG
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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7727-CG/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: Chorionic Gonadotropin alpha/beta (HCG)
HCG (human chorionic gonadotropin) is a member of the glycoprotein hormone (GPH) family within the cystine knot growth factor superfamily (1‑5). It is a heterodimer of a 23‑32 kDa unique subunit, CGb, with a 14‑22 kDa alpha subunit, CGa (common glycoprotein hormone alpha) that is shared with GPH family members lutropin (LH), follitropin (FSH) and thyroid stimulating hormone (TSH) (1, 2). CGb occurs only in higher primates, while the most closely related hormone, LHb, is expressed in all mammals (6). Human CGb and LHb share a receptor, LH/CG‑R or LHR, and show 86% aa sequence identity between aa 21 and 133, before diverging into a 32 aa, highly O‑glycosylated (CGb) or 8 aa (LHb) C‑terminal tail (2). Mature human CGa shares 69%‑73% aa identity with dog, rabbit, rat, mouse, cow, sheep, pig, cat and horse CGa. Each subunit form a cystine knot structure with three disulfide bridges (5). A “seat‑belt” loop of CGb wraps around CGa, stabilizing subunit non‑covalent association and conferring receptor selectivity (5). CGb is encoded by six clustered, nonallelic genes that encode identical, but differentially expressed, proteins (2, 7). HGC produced by cytotrophoblast cells in early pregnancy is hyperglycosylated and sialylated, increasing its acidity and half‑life (3, 4, 8). Forms with lower glycosylation are produced by syncytiotrophoblasts in continuing pregnancy, and in small amounts by the pituitary where it is also sulfated (4, 8). Free, variably glycosylated CGb subunits are also reported (3, 4). The primary role of HCG is to act as an autocrine factor to establish pregnancy and control placental growth and function. HCG has also been shown to induce the angiogenic factor, EG‑VEGF/PK1, and contribute to immune privilege by increasing circulating regulatory T cells and anti‑inflammatory cytokines IL‑10 and IL‑27, via cAMP signaling (9, 10). In addition to pregnancy, large amounts of HCG are produced in gestational trophoblastic diseases such as choriocarcinoma and hydatiform mole (3, 4). HCG may also be produced by ovarian and testicular germ cell tumors and advanced cancers that have dedifferentiated (3, 4).
- Fiddes, J.C. and H.M. Goodman (1979) Nature 281:351.
- Policastro, P. et al. (1983) J. Biol. Chem. 258:11492.
- Stenman, U.H. et al. (2006) Human Reprod. Update 12:769.
- Cole, L.A. (2012) Am. J. Cancer Res. 2:22.
- Lapthorn, A.J. et al. (1994) Nature 369:455.
- Maston, G.A. and M. Ruvolo (2002) Mol. Biol. Evol. 19:320.
- Zimmerman, G. et al. (2012) Biol. Reprod. 86:1.
- Kovalevskaya, G. et al. (2007) Mol. Cell. Endocrinol. 260-262:237.
- Brouillet, S. et al. (2012) Cell. Mol. Life Sci. 69:1537.
- Koldehoff, M. et al. (2011) J. Leukoc. Biol. 90:1017.
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