Recombinant Human GH Protein

Name: Recombinant Human GH Protein
Brand: Beta LifeScience
SKU: BL-1826NP
Availability: InStock

BL-1826NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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Product Overview

Description	Recombinant Human Growth Hormone is produced by our E.coli expression system and the target gene encoding Phe27-Phe217 is expressed.
Accession	P01241
Synonym	GH1;Somatotropin;Growth hormone;GH;GH-N;Growth hormone 1;Pituitary growth hormone
Gene Background	Growth hormone (GH), also known as somatotropin, is a member of a family of growth factors. It 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. GH includes prolactin, placental lactogens, proliferins, and somatolactin. It is synthesized primarily by somatotropes in the anterior pituitary and is stored in secretory granules. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
Molecular Mass	22.1 KDa
Apmol Mass	20 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 5% Trehalose, 5% Mannitol, 0.02% Tween 80, pH8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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.

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