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>   首页   >   产品   >   一抗   >   癌症   >   INHBB Antibody (C-term)   

INHBB Antibody (C-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - INHBB Antibody (C-term) AP11131b
    All lanes : Anti-INHBB Antibody (C-term) at 1:1000 dilution Lane 1: A549 whole cell lysate Lane 2: SK-BR-3 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 45 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
IHC-P, WB, E
Primary Accession P09529
Other Accession P17491, P04088, Q04999, P27093, P42917, NP_002184.2
Reactivity Human, Rat, Mouse
Predicted Bovine, Chicken, Pig, Rat
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 45122 Da
Antigen Region 369-397 aa
Additional Information
Gene ID 3625
Other Names Inhibin beta B chain, Activin beta-B chain, INHBB
Target/Specificity This INHBB antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 369-397 amino acids from the C-terminal region of human INHBB.
Dilution IHC-P~~N/A
WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsINHBB Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name INHBB
Function 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. Inhibin B is a dimer of alpha and beta-B that plays a crucial role in the regulation of the reproductive system by inhibiting the secretion of follicle-stimulating hormone (FSH) from the anterior pituitary gland. Thereby, maintains reproductive homeostasis in both males and females. Acts as a more potent suppressor of FSH release than inhibin A (By similarity). Functions as competitive receptor antagonist binding activin type II receptors with high affinity in the presence of the TGF-beta type III coreceptor/TGFBR3L (By similarity).
Cellular Location Secreted.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

The inhibin beta B 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 tumour-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 B subunit forms a homodimer, activin B, and also joins with the beta A subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion.

REFERENCES

Canzian, F., et al. Hum. Mol. Genet. 19(19):3873-3884(2010)
Ewens, K.G., et al. J. Clin. Endocrinol. Metab. 95(5):2306-2315(2010)
Jugessur, A., et al. PLoS ONE 5 (7), E11493 (2010) :
Ahn, J., et al. Hum. Mol. Genet. 18(19):3749-3757(2009)
Makanji, Y., et al. Endocrinology 150(10):4784-4793(2009)

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