This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogène
This INHBA antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 85-112 amino acids from the N-terminal region of human INHBA.
INHBA
Reactivité: Humain, Souris
WB, IHC, ICC, IF
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
For WB starting dilution is: 1:1000
For IHC-P starting dilution is: 1:10~50
For IF starting dilution is: 1:10~50
For FACS starting dilution is: 1:10~50
Restrictions
For Research Use only
Format
Liquid
Concentration
0.5 mg/mL
Buffer
Supplied in PBS with 0.09 % (W/V) sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C,-20 °C
Stockage commentaire
Store at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
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.