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Human GHR/Growth Hormone R Protein 4155

$270.00$900.00

Summary

  • Expression: HEK293
  • Pure: Yes (HPLC)
  • Amino Acid Range: Ala27-Tyr264
SKU: 4155parent Categories: , Tag:
Weight 1 lbs
Dimensions 9 × 5 × 2 in
accession

P10912

express system

HEK293

product tag

C-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

Pegvisomant, a growth hormone receptor (GHR) antagonist, is a well-known drug that was designed to treat acromegaly. However, recent studies have indicated that the GHR is a "moonlighting" protein that may exhibit dual functions based on its localization in the plasma membrane and nucleus.

molecular weight

The protein has a predicted MW of 28.8 kDa. Due to glycosylation, the protein migrates to 45-60 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human GHR/Growth Hormone R Protein 4155

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Pegvisomant, a growth hormone receptor (GHR) antagonist, is a well-known drug that was designed to treat acromegaly. However, recent studies have indicated that the GHR is a "moonlighting" protein that may exhibit dual functions based on its localization in the plasma membrane and nucleus.
Protein names
Growth hormone receptor (GH receptor) (Somatotropin receptor) [Cleaved into: Growth hormone-binding protein (GH-binding protein) (GHBP) (Serum-binding protein)]
Gene names
GHR,GHR
Protein family
Type I cytokine receptor family, Type 1 subfamily
Mass
9606Da
Function
Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway (By similarity).; 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.
Catalytic activity
#N/A
Subellular location
Cell membrane; Single-pass type I membrane protein. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway.; [Isoform 2]: Cell membrane; Single-pass type I membrane protein. Note=Remains fixed to the cell membrane and is not internalized.; [Growth hormone-binding protein]: Secreted. Note=Complexed to a substantial fraction of circulating GH.
Tissues
Expressed 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.
Structure
On growth hormone (GH) binding, forms homodimers and binds JAK2 via a box 1-containing domain. Binding to SOCS3 inhibits JAK2 activation, binding to CIS and SOCS2 inhibits STAT5 activation. Interacts with ADAM17.
Post-translational modification
The 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 (By similarity).; 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 (By similarity).
Domain
Th
Target Relevance information above includes information from UniProt accession: P10912
The UniProt Consortium

Data

HPLC of Human GHR/Growth Hormone R Protein
The purity of Human GHR is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human GHR/Growth Hormone R Protein
Human GHR on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Publications

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We haven't added any publications to our database yet.
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

Protocols

relevant to this product

Documents

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