Sex Hormone Binding Globulin (SHBG) Antibody - With BSA and Azide
Mouse Monoclonal Antibody [Clone SPM605 ]
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| IHC, IF, FC |
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Primary Accession | P04278 |
Other Accession | 6462, 632235 |
Reactivity | Human |
Host | Mouse |
Clonality | Monoclonal |
Isotype | Mouse / IgG1 |
Clone Names | SPM605 |
Calculated MW | 45kDa |
Gene ID | 6462 |
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Other Names | Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG |
Storage | Store at 2 to 8°C.Antibody is stable for 24 months. |
Precautions | Sex Hormone Binding Globulin (SHBG) Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SHBG (HGNC:10839) |
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Function | Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration. |
Cellular Location | Secreted. Note=In testis, it is synthesized by the Sertoli cells, secreted into the lumen of the seminiferous tubule and transported to the epididymis. |
Tissue Location | Isoform 1 and isoform 2 are present in liver and testis |

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Provided below are standard protocols that you may find useful for product applications.
Background
Recognizes a protein of 45kDa, identified as SHBG. It functions as an androgen transport protein, but may also be involved in receptor-mediated processes. Each dimer binds one molecule of steroid. It is specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. SHBG regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration. In testis, it is synthesized by the Sertoli cells, secreted into the lumen of the seminiferous tubule and transported to the epididymis.
References
Grishkovskaya, I., et al. 2000. Crystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domain. EMBO. J. 19: 504-512. |

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