Growth hormone receptor protein (Fc Chimera) (ab83991)
Constituents: 10% Trehalose, 1% Human serum albumin
Our Abpromise guarantee covers the use of ab83991 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ab83991 migrates as a broad band between 65 and 85 kDa in SDS-PAGE due to post-translation modifications, in particular glycosylation. This compares with the unmodified protein that has a predicted molecular mass of 54.3 kDa. ab83991 consists of 15-35% carbohydrate by weight.
ab83991 separates into a number of isoforms with a pI between 5.0 and 7.7 in 2D PAGE due to post-translational modifications, in particular glycosylation. This compares with the unmodified protein that has a predicted pI of 6.90.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
- GH receptorGH-binding proteinGHBP
- GHRGHR_HUMANGrowth hormone binding proteinGrowth hormone receptorGrowth hormone receptor precursorGrowth hormone-binding proteinSerum binding proteinSerum-binding proteinSomatotropin receptor
The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling.
Isoform 2 up-regulates the production of GHBP and acts as a negative inhibitor of GH signaling.
Defects in GHR may be a cause of idiopathic short stature autosomal (ISSA) [MIM:604271]. Short stature is defined by a subnormal rate of growth.
Contains 1 fibronectin type-III domain.
The box 1 motif is required for JAK interaction and/or activation.
The extracellular domain is the ligand-binding domain representing the growth hormone-binding protein (GHBP).
The ubiquitination-dependent endocytosis motif (UbE) is required for recruitment of the ubiquitin conjugation system on to the receptor and for its internalization.
modificationsThe soluble form (GHBP) is produced by phorbol ester-promoted proteolytic cleavage at the cell surface (shedding) by ADAM17/TACE. Shedding is inhibited by growth hormone (GH) binding to the receptor probably due to a conformational change in GHR rendering the receptor inaccessible to ADAM17.
On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2.
On ligand binding, ubiquitinated on lysine residues in the cytoplasmic domain. This ubiquitination is not sufficient for GHR internalization.
Growth hormone receptor protein (Fc Chimera) images
Lane 1 – MW markers; Lane 2 – ab83991; Lane 3 – ab83991 treated with PNGase F to remove potential N-linked glycans; Lane 4 – ab83991 treated with a glycosidase cocktail to remove potential N- and O-linked glycans. 10 µg protein loaded per lane; Deep Purple™ stained.Drop in MW after treatment with PNGase F indicates presence of N-linked glycans. Additional bands in lane 3 and lane 4 are glycosidase enzymes.
Post-translational modifications result in protein heterogeneity. The densitometry scan demonstrates the purified human cell expressed protein exists in multiple isoforms, which differ according to their level of post-translational modification. Triangle indicates theoretical pI and MW of the protein.
References for Growth hormone receptor protein (Fc Chimera) (ab83991)
ab83991 has not yet been referenced specifically in any publications.