GHBP Human, Sf9

Growth Hormone Binding Protein Human Recombinant, Sf9

Human GHBP, produced in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. It consists of 254 amino acids (19-264aa) with a molecular weight of 29.4kDa. An 8 amino acid Histidine tag is fused to the C-terminus of the GHBP protein. Purification is achieved through proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT14978
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered solution, colorless.

GHBP Ovine

Growth Hormone Binding Protein Ovine Recombinant

Recombinant Ovine Growth Hormone Binding Protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 237 amino acids, resulting in a molecular weight of 28 kDa. The purification process of GHBP involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15048
Source
Escherichia Coli.
Appearance
White, sterile, lyophilized powder.

GHBP Rabbit

Growth Hormone Binding Protein Rabbit Recombinant

Recombinant Growth Hormone Binding Protein (GHBP) Rabbit Extracellular Domain, produced in E. coli, is a single, non-glycosylated polypeptide chain. This protein comprises 249 amino acids, resulting in a molecular weight of 28 kDa. The purification of GHBP Rabbit is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15118
Source
Escherichia Coli.
Appearance
Sterile Filtered White Lyophilized Powder

GHBP Rat

GH Binding Protein Rat Recombinant

Produced in Sf9 insect cells using baculovirus expression system, GHBP is a single, glycosylated polypeptide chain consisting of 255 amino acids (19-265.a.). It has a molecular mass of 29.4 kDa (appears approximately at 28-40 kDa on SDS-PAGE). This protein is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15178
Source
Sf9, Baculovirus cells.
Appearance
Sterile and colorless solution after filtration.

pGH 20kDa Human

Growth Hormone Placental 20kDa Human Recombinant

Recombinant Human Growth Hormone Placental 20kDa, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 177 amino acids. With a molecular mass of 20498 Daltons, it has a predicted isoelectric point (pI) of 8.20. Unlike pituitary GHs, GH 20K placental lacks lactogenic activity (mediated by the prolactin receptor). The purification of GH 20K placental is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15243
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

GH Antagonist Ovine

Growth Hormone Antagonist Ovine Recombinant

Somatotropin Ovine Antagonist Recombinant G119R, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 191 amino acids, with a molecular weight of 22 kDa. The purification of this recombinant antagonist is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11783
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

GH Human, HEK

Growth Hormone Human Recombinant, HEK

Recombinant Human Growth Hormone, produced in HEK cells, is a non-glycosylated monomer with a molecular weight of 22kDa. It undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13300
Source
HEK.
Appearance
White, sterile-filtered powder, lyophilized (freeze-dried).

GH Human, Plant

Growth Hormone Human Recombinant, Plant

Recombinant human Growth Hormone (GH), produced in Nicotiana benthamiana plants, is a single-chain protein comprised of 205 amino acids. Its molecular formula is C1025H1570N280O306S7, and it includes a 6-His-tag at the N-terminal. The protein has a molecular mass of 22.9 kDa.
Shipped with Ice Packs
Cat. No.
BT13413
Source
Nicotiana benthamiana plant
Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.

GH Mahi Mahi

Growth Hormone Mahi Mahi Recombinant

Recombinant Growth Hormone Mahi Mahi, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 190 amino acids, with a molecular weight of 21.81 kDa. Purification of GH is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13489
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.
Definition and Classification

Growth hormone (GH), also known as somatotropin or human growth hormone (hGH), is a peptide hormone that stimulates growth, cell reproduction, and cell regeneration in humans and other animals . It is secreted by the anterior lobe of the pituitary gland and plays a crucial role in human development . GH is classified as a mitogen, which is specific to certain types of cells .

Biological Properties

Key Biological Properties: GH is a 191-amino acid, single-chain polypeptide . It stimulates protein synthesis, increases fat breakdown, and opposes the action of insulin . GH also stimulates the production of insulin-like growth factor 1 (IGF-1), which mediates many of its growth-promoting effects .

Expression Patterns and Tissue Distribution: GH is synthesized and secreted by somatotropic cells in the anterior pituitary gland . It is released in a pulsatile manner, with surges occurring after the onset of deep sleep . GH receptors are widely distributed in various tissues, including the liver, muscle, and bone .

Biological Functions

Primary Biological Functions: GH stimulates the growth of essentially all tissues of the body, including bone . It plays a vital role in normal physical growth in children, with levels peaking during puberty . GH also promotes lipolysis, increases muscle mass, and enhances protein synthesis .

Role in Immune Responses and Pathogen Recognition: GH has been shown to stimulate immune function, although the exact mechanisms are not fully understood . It is believed to enhance the activity of immune cells and promote the production of cytokines .

Modes of Action

Mechanisms with Other Molecules and Cells: GH exerts its effects by binding to the growth hormone receptor (GHR) on target cells . This binding activates the JAK-STAT signaling pathway, leading to the transcription of GH-responsive genes . GH also stimulates the production of IGF-1, which acts in an autocrine and paracrine manner to promote growth .

Binding Partners and Downstream Signaling Cascades: GH binds to GHR, which then associates with Janus kinase 2 (JAK2), leading to the phosphorylation of both GHR and JAK2 . This activation triggers downstream signaling cascades, including the MAPK and PI3K/AKT pathways .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: GH secretion is regulated by the hypothalamic hormones growth hormone-releasing hormone (GHRH) and somatostatin . GHRH stimulates GH release, while somatostatin inhibits it . Additionally, GH secretion is influenced by metabolic factors, such as glucose and lipid levels, and peripheral hormones like insulin .

Transcriptional Regulation and Post-Translational Modifications: GH gene expression is regulated by transcription factors, including Pit-1 . Post-translational modifications, such as phosphorylation, also play a role in modulating GH activity .

Applications

Biomedical Research: GH is used in research to study growth disorders and metabolic diseases . It is also employed in experiments to understand its role in cell growth and differentiation .

Diagnostic Tools: GH levels are measured to diagnose growth hormone deficiency (GHD) and acromegaly . GH stimulation tests and IGF-1 measurements are commonly used diagnostic tools .

Therapeutic Strategies: Recombinant human growth hormone (rhGH) is used to treat children with growth disorders and adults with GH deficiency . GH therapy has also been explored for its potential to enhance fertility and improve outcomes in assisted reproductive technologies .

Role in the Life Cycle

Development: GH is essential for normal growth and development in children . It promotes the growth of bones and tissues, leading to increased height and muscle mass .

Aging and Disease: GH levels decline with age, which is associated with decreased muscle mass and increased fat accumulation . GH therapy has been investigated for its potential to counteract some of the effects of aging . Additionally, GH dysregulation is implicated in various diseases, including acromegaly and growth hormone deficiency .

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