GPHA2 Proteins, Antibodies, cDNA Clones Research Reagents

GPHA2 (Glycoprotein Hormone Subunit Alpha 2, also known as A2; GPA2; ZSIG51), located on 11q13.1, is a Protein Coding gene. The gene produces a 14163 Da protein composed of 129 amino acids. GPHA2 is a cystine knot-forming polypeptide and a subunit of the dimeric glycoprotein hormone family. GPHA2 and glycoprotein hormone beta 5 (GPHB5) can form a noncovalent heterodimer. GPHA2 shares only 35% amino acid identity with GPA1 (CGA). Diseases such as Salt And Pepper Syndrome and Norrie Disease are associated with GPHA2.

GPHA2 Protein (2)

    GPHA2 Antibody (3)

      GPHA2 cDNA Clone (13)

      NM_130769.3

      クローニングベクター cDNA 製品

      In lentiviral vector

      GPHA2 qPCR Primer (1)

      GPHA2 Lysate (2)

        GPHA2 の背景知識

        GPHA2 is a member of the glycoprotein hormones subunit alpha family. Glycoprotein hormones consist of two subunits, the common alpha- and specific beta-subunits, which associate noncovalently to form a heterodimer. The alpha-subunit combines with four distinct beta-subunits giving rise to four biologically active hormones in the human: FSH, LH, TSH, and CG. GPHA2 and glycoprotein hormone beta 5 (GPHB5) can form a noncovalent heterodimer. GPHA2 can be detected in a variety of tissues. Recombinant A2/B5 heterodimeric glycoproteins activate human TSH receptors, but not LH and FSH receptors, and shows high affinity to TSH receptors in a radioligand receptor assay. The heterodimer also stimulates cAMP production and thymidine incorporation by cultured thyroid cells and increases serum thyroxine levels in TSH-suppressed rats in vivo. This new heterodimeric glycoprotein hormone was named Thyrostimulin based on its thyroid-stimulating activity. The expression of Thyrostimulin in the anterior pituitary known to express TSH receptors suggested a paracrine mechanism.

        GPHA2 の参考文献

        • Hsu SY. et al., 2002, Science. 295 (5555): 671-4.
        • Suzuki C. et al., 2007, Regul Pept. 142 (1-2): 60-7.
        • Breous E. et al., 2006, Mol Cell Endocrinol. 245 (1-2): 169-80.

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