Key features and details
- Expression system: Escherichia coli
- Purity: > 85% SDS-PAGE
- Tags: His tag C-Terminus
- Suitable for: SDS-PAGE
Product nameRecombinant Rhesus monkey Growth hormone receptor protein (His tag)
See all Growth hormone receptor proteins and peptides
Purity> 85 % SDS-PAGE.
Expression systemEscherichia coli
Protein lengthProtein fragment
SequenceFSGSEPTAAILSRASWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHW TDAVHHGSKSLGPIQLFYTRRNIQGQTQEWKECPDYVSAGENSCYFNSSF TSVWIPYCIKLTSNGDTVDGKCFSVDEIVQPDPPIALNWTLLNVSLTGIH ADILVRWEAPPNADIQKGWMVLEYELQYKEVNETKWKMMDPILSTSVPVY SLKVDKEYEVLVRSKRRNSRNYGEFSEVLYVTLPQMNQFTCEEDFY
Predicted molecular weight30 kDa including tags
Amino acids19 to 264
TagsHis tag C-Terminus
Additional sequence informationC-terminal 6xHis-tagged. Extracellular domain.
Our Abpromise guarantee covers the use of ab235711 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Constituents: Tris buffer, 50% Glycerol
- GH receptor
- GH-binding protein
FunctionReceptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway.
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.
Tissue specificityExpressed in various tissues with high expression in liver and skeletal muscle. Isoform 4 is predominantly expressed in kidney, bladder, adrenal gland and brain stem. Isoform 1 expression in placenta is predominant in chorion and decidua. Isoform 4 is highly expressed in placental villi. Isoform 2 is expressed in lung, stomach and muscle. Low levels in liver.
Involvement in diseaseDefects in GHR are a cause of Laron syndrome (LARS) [MIM:262500]. A severe form of growth hormone insensitivity characterized by growth impairment, short stature, dysfunctional growth hormone receptor, and failure to generate insulin-like growth factor I in response to growth hormone.
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.
Sequence similaritiesBelongs to the type I cytokine receptor family. Type 1 subfamily.
Contains 1 fibronectin type-III domain.
DomainThe WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
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.
Cellular localizationSecreted; Cell membrane. On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway and Cell membrane. Remains fixed to the cell membrane and is not internalized.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab235711 has not yet been referenced specifically in any publications.