Human Growth hormone receptor protein fragment (ab83991)
- Product nameHuman Growth hormone receptor protein fragmentSee all Growth hormone receptor proteins and peptides ...
- Amino Acid Sequence
- SequenceTheoretical sequence: FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKC RSPERETFSC HWTDEVHHGTKNLGPIQLFYTRRNTQEW TQEWKECPDYVSAGENSCYF NSSFTSIWIPYCIKLTSN GGTVDEKCFSVDEIVQPDPPIALNWTLLNV SLTGIHAD IQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPI LTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLY VTLPQMRIPK VDKKVEPKSCDKTHTCPPCPAPELLGGP SVFLFPPKPKDTLMISRTPE VTCVVVDVSHEDPEVKFN WYVDGVEVHNAKTKPREEQYNSTYRVVSVL TVLHQDWL NGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYK TTPPVLDSDG SFFLYSKLTVDKSRWQQGNVFSCSVMHE ALHNHYTQKSLSLSPGK
- Amino acids19 to 254
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.
- Purity> 95
% by SDS-PAGE.
- Concentration information loading...
Preparation and Storage
- Stability and Storage
Shipped at 4°C. After reconstitution store at -20ºC. Avoid freeze / thaw cycles.
Constituents: 10% Trehalose, 1% Human serum albumin
- ReconstitutionIt is recommended that 0.5 ml of sterile phosphate-buffered saline be added to the vial. Following reconstitution short-term storage at 4°C is recommended, and longer-term storage of aliquots at -18 to -20°C. Repeated freeze thawing is not recommended.
- GH receptor
- GH-binding protein
- GHBP, included
- Growth hormone binding protein
- Growth hormone receptor
- Growth hormone receptor precursor
- Growth hormone-binding protein
- Growth hormone-binding protein, included
- Increased responsiveness to growth hormone, included
- Serum binding protein
- Serum-binding protein
- Somatotropin receptor
- 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.
Human Growth hormone receptor protein fragment 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 Human Growth hormone receptor protein fragment (ab83991)
ab83991 has not yet been referenced specifically in any publications.