Growth Hormone Receptor (GHR) (AA 27-264) (Active) protein (Biotin,His tag)

Details for Product No. ABIN2181160, Supplier: Log in to see
Protein Name
  • GHBP
  • AA986417
  • GHR/BP
  • GHR
  • ghr
  • growth hormone receptor
  • growth hormone receptor L homeolog
  • GHR
  • Ghr
  • ghr.L
  • ghr
Protein Characteristics
AA 27-264
8
3
3
3
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Origin
Human
22
9
6
5
3
3
1
1
1
1
1
1
1
1
1
Source
HEK-293 Cells
15
13
10
6
4
1
1
Protein Type
Recombinant
Biological Activity
Active
Purification tag / Conjugate
This Growth Hormone Receptor protein is labelled with Biotin,His tag.
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Brand MABSol®,UltraLys
Specificity The primary amines in the side chains of lysine residues and the N-terminus of the protein are conjugated with biotins using standard chemical labeling method. A standard biotin reagent (13.5 angstroms) is used in this product.
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 28.5 kDa. The protein migrates as 40-60 kDa on a SDS-PAGE gel under reducing (R) condition due to glycosylation.
Purity >95 % as determined by reduced SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Grade Ultra Sensitive
Background Growth hormone receptor (GHR) is also known as somatotropin receptor, growth hormone-binding protein (GHBR), which belongs to the type I cytokine receptor family or Type 1 subfamily. GHR contains one fibronectin type-III domain. GHR / GHBR is expressed in various tissues with high expression in liver and skeletal muscle. The soluble form (GHBP) is produced by phorbol ester-promoted proteolytic cleavage at the cell surface (shedding) by ADAM17/TACE. GHR is receptor 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.
Molecular Weight 28.5 kDa
UniProt P10912
Pathways NF-kappaB Signaling, JAK-STAT Signaling, Response to Growth Hormone Stimulus
Comment

A chemically labeled biotinylated protein with ultra sensitivity.
The product is produced using a chemical labeling approach. The primary amines in the side chains of lysine residues and the N-terminus of protein are conjugated with biotins.
Chemical labeling usually results in multiple biotin attachment on a single protein molecule, which could potentially lead to higher detection sensitivity.

Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Growth Hormone Receptor (GHR) (AA 27-264) (Active) protein (Biotin,His tag) (ABIN2181160) Biotinylated Human Growth Hormone R on SDS-PAGE under reducing (R) condition. The gel...
Background publications Ghizzoni, Duquesnoy, Torresani, Vottero, Goossens, Bernasconi: "Isolated growth hormone deficiency type IA associated with a 45-kilobase gene deletion within the human growth hormone gene cluster in an Italian family." in: Pediatric research, Vol. 36, Issue 5, pp. 654-9, 1995 (PubMed).

Duquesnoy, Sobrier, Duriez, Dastot, Buchanan, Savage, Preece, Craescu, Blouquit, Goossens et al.: "A single amino acid substitution in the exoplasmic domain of the human growth hormone (GH) receptor confers familial GH resistance (Laron syndrome) with positive GH-binding activity by abolishing ..." in: The EMBO journal, Vol. 13, Issue 6, pp. 1386-95, 1994 (PubMed).

Urbanek, Russell, Cooke, Liebhaber: "Functional characterization of the alternatively spliced, placental human growth hormone receptor." in: The Journal of biological chemistry, Vol. 268, Issue 25, pp. 19025-32, 1993 (PubMed).

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