Activin-A Human Plant-Active; Activin-A Human Recombinant, Plant-Active; Inhba; Inhibin beta A; FSH releasing protein; Activin A Plant-Active

For Research Use Only. Not for use in diagnostic procedures.

Nicotiana benthamiana

Greater than 98% as obsereved by SDS-PAGE.

Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4
Lyophilized freeze dried powder.

For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.

Small volumes of INHBA recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Description: Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

Introduction: Activins are homodimers or heterodimers of the different beta subunit isoforms, part of the TGFbeta family. Mature Activin A has two 116 amino acids residues betaA subunits (betaA-betaA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

CYTOKINES AND GROWTH FACTORS; Growth Factors; Activin

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inhibin, beta A

inhibin beta A chain; FSH-releasing protein; Inhibin, beta-1; activin beta-A chain; erythroid differentiation factor; erythroid differentiation protein; follicle-stimulating hormone-releasing protein; inhibin, beta A (activin A, activin AB alpha polypeptide)

Inhibin beta A chain

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INHBA_HUMAN

The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome. [provided by RefSeq, Jul 2008]

INHBA: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. Belongs to the TGF-beta family.

Protein type: Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 7p15-p13

Cellular Component: extracellular region

Molecular Function: identical protein binding; protein binding; growth factor activity; protein heterodimerization activity; hormone activity; peptide hormone binding; cytokine activity; transforming growth factor beta receptor binding

Biological Process: positive regulation of transcription, DNA-dependent; positive regulation of cellular protein metabolic process; activin receptor signaling pathway; mesodermal cell differentiation; defense response; palate development; negative regulation of cell cycle; negative regulation of interferon-gamma biosynthetic process; odontogenesis; negative regulation of cell proliferation; cell surface receptor linked signal transduction; cell-cell signaling; ovarian follicle development; hair follicle development; erythrocyte differentiation; cell cycle arrest; cell differentiation; negative regulation of B cell differentiation; hemoglobin biosynthetic process; response to drug; nervous system development; regulation of follicle-stimulating hormone secretion; positive regulation of erythrocyte differentiation; male gonad development; progesterone secretion; negative regulation of follicle-stimulating hormone secretion; regulation of transcription from RNA polymerase II promoter; negative regulation of macrophage differentiation; regulation of MAPKKK cascade; negative regulation of phosphorylation; hemopoietic progenitor cell differentiation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of follicle-stimulating hormone secretion; negative regulation of cell growth; cell development; growth; G1/S transition of mitotic cell cycle

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