Recombinant Human Somatotropin (GH1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-11275P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Somatotropin (GH1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-11275P
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Product Overview

Description Recombinant Human Somatotropin (GH1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P01241
Target Symbol GH1
Synonyms gH; GH-N; GH1; GHB5; GHN; Growth hormone 1; Growth hormone; Growth hormone B5; Growth hormone; normal; Growth hormone; pituitary; HG1; hGH-N; IGHD1B; Pituitary growth hormone; RNGHGP; SOMA_HUMAN; Somatotropin
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His
Target Protein Sequence FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
Expression Range 27-217aa
Protein Length Full Length of Mature Protein
Mol. Weight 25.7 kDa
Research Area Developmental Biology
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
Subcellular Location Secreted.
Protein Families Somatotropin/prolactin family
Database References

HGNC: 4261

OMIM: 139250

KEGG: hsa:2688

STRING: 9606.ENSP00000312673

UniGene: PMID: 29179911

  • Patients examined at 1 year or several years from complicated mild traumatic brain injury had a similarly high occurrence of isolated GH deficiency PMID: 27878771
  • Single nucleotide variant in GH1 gene is associated with isolated growth hormone deficiency. PMID: 28910730
  • In newborns, serum PRL and hGH levels show a positive correlation that can be explained by common regulatory factors or a drift phenomenon. A higher gestational week is associated with a higher PRL/hGH ratio. PMID: 28700563
  • This review describes the endocrine profile of centenarians concerning the GH/IGF-I/insulin system, focusing on the relevance of this pathway on the modulation of ageing and longevity. PMID: 27932301
  • Data suggest that patients with NICTH (non-islet cell tumor hypoglycemia) exhibit low serum growth hormone levels during hypoglycemic episodes. [Retrospective Study & REVIEW of Case Reports] PMID: 28529277
  • Homozygous GH1 deletion is associated with growth hormone deficiency. PMID: 28525353
  • Human Growth Hormone Inhibits CLAUDIN-1 Expression Through Activation of Signal Transducer and Activator of Transcription 3 (STAT3). PMID: 28617312
  • Serum GH was unrelated to type 2 diabetes, fasting blood glucose, or HbA1c level. PMID: 27060213
  • GH1 and GHRHR screening revealed eleven variations in 24 (21%) patients with isolated growth hormone deficiency of which, four were novel deleterious, one novel non-pathogenic and six reported changes. PMID: 27114065
  • The results suggest that GH regulates energy metabolism directly in myocytes and that UCP2 participates in the signal transduction pathway that functions downstream of the GHR/JAK/STAT. PMID: 27150070
  • These results implicate TIMP3 as a modulator of cell surface GHR abundance and the ability of GH to promote cellular signaling. PMID: 27075707
  • Children with GH excess underwent medical treatment with lanreotide and a minimum clinical/biochemical follow up of 2 years is reported. The present study demonstrates that GH excess should be considered as a relative frequent endocrine manifestation in NF1 patients, similarly to central precocious puberty PMID: 28631895
  • Thus, GHRH analogs of the Miami series powerfully suppress tumor growth, but have only a weak endocrine GH inhibitory activity. The suppression of tumor growth could be induced in part by the downregulation of GHRH receptors levels. PMID: 28130121
  • the levels and kinetics of phosphorylation mediated by the main signalling proteins triggered by 22K-GH or 20K-GH were not exactly the same. PMID: 28427901
  • A negative regulation of locally produced GH by androgens/AR in Prostate cancer cells following treatment with AR agonists (R1881) and antagonists (enzalutamide, bicalutamide). PMID: 28444169
  • The intrinsic amyloidogenicity of growth hormone, in the presence of contaminating prion protein (and perhaps prolactin as well) and amyloid-beta contained in some cadavers' pituitaries, may have led to the observed co-occurring of Creutzfeldt-Jakob disease and Alzheimer's disease. PMID: 27214308
  • GH potentially negatively modulates the maturation and accumulation of lipid in adipocytes. PMID: 27802441
  • To our knowledge, c.-223C>T is the first homozygous point mutation in the GH1 promoter that leads to short stature due to idiopathic growth hormone deficiency. PMID: 27252485
  • Data show that the recombinant protein produced by the plasmid-free E coli strain was purified and characterized to be human growth hormone (hGH). PMID: 27542624
  • Our results suggest that the known protective effect of GH signaling deficiency on neoplastic tissue growth is mediated, at least partially, by regulating p53 expression PMID: 27226307
  • evidence that hGH synthesis follows a diurnal rhythm and of dynamic associations of the circadian machinery with a component of a chromosomal structure of the hGH1 locus that is essential for efficient expression. PMID: 27151213
  • Gene polymorphism of leptin (loci rs7799039) and leptin receptor (loci rs1137101) are correlated with Growth hormone deficiency susceptibility. PMID: 26915772
  • These results showed that hybrid training system on a cycle ergometer (CE) was more efficient in stimulating acute increases in GH, lactate and IL-6 than CE at the same workload. PMID: 26522057
  • Growth Hormone 1 T1663A Polymorphism were at a decreased risk of breast cancer. PMID: 26225688
  • This is the first report of a family suffering from short stature caused by autosomal dominant form of GH deficiency II, which severely affects intracellular GH folding and stability as well as secretion PMID: 26485222
  • GH and IGF-1 suppression is maintained for up to 25 months during pasireotide LAR treatment of acromegaly. PMID: 25103549
  • In women with normal somatotroph function, GH levels do not change in the first trimester of pregnancy. PMID: 25179796
  • These data on pregnancy outcomes in a large group of women with hypopituitarism revealed no relationship between GH replacement therapy regimens and pregnancy outcomes. PMID: 26256649
  • Effect of oral glucose administration on rebound growth hormone release in normal and obese women: the role of adiposity, insulin sensitivity and ghrelin. PMID: 25782001
  • the phenotype of MIP-FoxM1-hGH mice is due primarily to hGH activity and that the FoxM1 protein remains largely inactive PMID: 26202070
  • Case Report: of Klinefelter sydnrome with short stature due to growth hormone deficiency. PMID: 25241616
  • Suggest growth hormone deficiency may be common feature in vernal keratoconjuntivitis patients. PMID: 25079463
  • Human Growth Hormone stimulates the microRNA 96-182-183 cluster, which promotes the epithelial-mesenchymal transition and invasion in breast cancer PMID: 25873390
  • The results demonstrate that activation of noncoding transcription reflects an autonomous activity of the human growth hormone long-range enhancer that is fully independent of interactions with linked gene promoters and occurring in spatial and temporal synchrony with initiation of GH expression in the embryonic pituitary. PMID: 25662214
  • Analysis of GH1 in a cohort of Brazilian patients revealed that the autosomal recessive form of isolated growth hormone deficiency(IGHD) was more common than the dominant one, and both were found only in severe IGHD. PMID: 25116472
  • Recipients showed a rapid recovery of the GH/IGF1 hormonal axis and liver function after LDLT, whereas donors showed altered GH signaling and regenerative delay in the early days after living donation. PMID: 24889799
  • JAK2 is activated by growth hormone and other cytokines. (Review) PMID: 25656053
  • Genotyping contributed to the diagnosis of children with suspected growth hormone insensitivity and short stature. PMID: 25411237
  • hGH production is extremely sensitive to increased caloric intake. PMID: 25295535
  • After LT, GH levels correlate with the extent of cytolysis, while IGF-1 is an indicator of liver synthetic function recovery. IGF-1 levels >90 mug/L (day 15-30) seem to be an indicator of short-term survival. PMID: 24804205
  • In this review we highlight the evidence of extrapituitary synthesis of GH in humans. [review] PMID: 24642386
  • This review summarizes findings of growth hormone's influence on in utero and neonatal cellular and metabolic profiles related to bone and adipose tissue. PMID: 25015810
  • The study presents experimental data for the mechanism of thiol-disulfide exchange in tryptic peptides derived from human growth hormone in aqueous solution. PMID: 24549831
  • we present the results of screening for mutations in GH1 and GHRHR genes in a large cohort of Argentinian patients with IGHD. These suggest that the p.Arg183His mutation associated with the type II dominant form of IGHD might be relatively common. PMID: 23789946
  • In the first family a novel splice site mutation in GH1 was identified (c.172-1G>C, IVS2-1G>C). In two other families a previously reported splice site mutation (c.291+1G>A, IVS3+1G>A) was found. PMID: 24280736
  • Bilateral involvement of a pituitary adenoma and severely decreased immediate postoperative serum GH levels at 72 hours after transsphenoidal adenomectomy may be independent risk factors for accelerated GH deficiency in acromegalic patients. PMID: 24972779
  • The activity of autocrine GH may be distinct from that of endocrine GH in prostate cancer cells. PMID: 23238889
  • robust GH-stimulated hepatic Igf1 gene transcription utilizes tissue-specific mechanisms of epigenetic regulation that are established independent of GH signaling. PMID: 24109593
  • meta-analysis indicates that GH1 T1663A polymorphism may contribute to the risk of colorectal cancer, especially among Asian populations PMID: 24464925

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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