Prolactin Human

Prolactin Human Recombinant

Recombinant Human Prolactin, expressed in E.Coli, is a non-glycosylated polypeptide chain consisting of 200 amino acids. With a molecular weight of 23007 Daltons, this single-chain protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30129
Source
Escherichia Coli.
Appearance
White, sterile-filtered powder obtained through lyophilization (freeze-drying).

Prolactin Human, Antagonist

Prolactin Antagonist Human Recombinant

Prolactin Human Recombinant Antagonist des 1-9, G129R, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 190 amino acids, an additional N-terminal Alanine, and has a molecular weight of approximately 22 kDa. This antagonist is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT30199
Source
Escherichia Coli.
Appearance
Sterile Filtered White Lyophilized Powder

PRL R Rainbow Trout

Prolactin Soluble Receptor Rainbow Trout Recombinant

Recombinant Prolactin Receptor Extracellular Domain from Rainbow Trout, produced in E. coli, is a non-glycosylated polypeptide chain composed of 210 amino acids, with a molecular weight of 24,034 Daltons. The Prolactin Receptor is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT29884
Source
Escherichia Coli.
Appearance
White, sterile-filtered lyophilized powder.

PRL R Rat

Prolactin Soluble Receptor Rat Recombinant

Recombinant Prolactin Receptor Rat Extracellular Domain, produced in E. coli, is a non-glycosylated polypeptide chain composed of 206 amino acids with a molecular weight of 24120 Daltons. The purification of Prolactin Receptor is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29939
Source
Escherichia Coli.
Appearance
White, sterile-filtered lyophilized powder.

Prolactin Chicken

Prolactin Chicken Recombinant

Recombinant Chicken Prolactin, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 199 amino acids, with an additional alanine residue at the N-terminus. Its molecular weight is approximately 23 kDa.

Purification of the Chicken Prolactin protein is achieved through proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT29998
Source
Escherichia Coli.
Appearance
Sterile Filtered White Lyophilized (Freeze-Dried) Powder.

PIP Human

Prolactin-Induced Protein Human

Derived from Human Seminal Plasma, the produced Prolactin-Induced Protein has a molecular mass of 13.52kDa (excluding glycosylation) and comprises 118 amino acid residues.
Shipped with Ice Packs
Cat. No.
BT29633
Source
Human Seminal Plasma.
Appearance
White, lyophilized powder after filtration.

PIP Protein

Prolactin-Induced Protein Human Recombinant

Recombinant human PIP, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 141 amino acids (specifically, residues 29-146). It has a molecular weight of 15.9 kDa. This PIP protein is fused to a 23 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29699
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

PRL R Human

Prolactin Soluble Receptor Human Recombinant

The Extracellular Domain of the human Prolactin Receptor, recombinantly produced in E. coli, is a non-glycosylated polypeptide chain containing 210 amino acids with a molecular mass of 23.97 kDa. The Prolactin Receptor is purified using proprietary chromatographic techniques following the methods described by Bignon et al. (1994) JBC 269; 3318-24 and its activity is assessed as per Gertler et al. (1996) JBC 271; 24482-91.
Shipped with Ice Packs
Cat. No.
BT29760
Source
Escherichia Coli.
Appearance
Sterile filtered white powder.

Leptin-A Tilapia

Leptin-A Tilapia Recombinant

Recombinant Leptin-A Tilapia, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 161 amino acids, with a molecular weight of 16,491 Daltons. The purification of Leptin-A Tilapia is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT29457
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder

Leptin-B Tilapia

Leptin-B Tilapia Recombinant

Recombinant Tilapia Leptin-B, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 152 amino acids, with a molecular weight of 15,243 Daltons. The purification process involves proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT29547
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.
Definition and Classification

Prolactin (PRL), also known as lactotropin and mammotropin, is a protein hormone primarily associated with lactation in mammals . It is encoded by the PRL gene and is secreted by the anterior pituitary gland . Prolactin belongs to the family of lactogenic hormones, which also includes growth hormone and placental lactogens .

Biological Properties

Key Biological Properties: Prolactin is a multifunctional hormone with over 300 known biological activities . It is involved in reproductive, metabolic, osmoregulatory, and immunoregulatory processes .

Expression Patterns: Prolactin is primarily produced by lactotroph cells in the anterior pituitary gland, but it is also synthesized in various extrapituitary sites, including the immune system, brain, and mammary glands .

Tissue Distribution: Prolactin receptors are widely distributed throughout the body, including the mammary glands, liver, ovaries, prostate, and immune cells .

Biological Functions

Primary Biological Functions: Prolactin’s primary role is to stimulate milk production (lactation) in mammals . It also plays a crucial role in the regulation of the immune system, pancreatic development, and metabolism .

Role in Immune Responses and Pathogen Recognition: Prolactin acts as a cytokine-like molecule, influencing the immune response by modulating the activity of immune cells and enhancing pathogen recognition .

Modes of Action

Mechanisms with Other Molecules and Cells: Prolactin exerts its effects by binding to prolactin receptors (PRLR) on the surface of target cells . This binding activates several intracellular signaling pathways, including the JAK2/STAT5, MAPK, and PI3K/AKT pathways .

Binding Partners and Downstream Signaling Cascades: Upon binding to its receptor, prolactin induces receptor dimerization and activation of downstream signaling cascades, leading to changes in gene expression and cellular functions .

Regulatory Mechanisms

Control of Expression and Activity: Prolactin secretion is primarily regulated by dopamine, which inhibits its release from the pituitary gland . Other factors, such as estrogen and thyrotropin-releasing hormone, can stimulate prolactin release .

Transcriptional Regulation and Post-Translational Modifications: The expression of prolactin is controlled at the transcriptional level by various promoters and regulatory elements . Post-translational modifications, such as phosphorylation, also play a role in modulating prolactin’s activity .

Applications

Biomedical Research: Prolactin is widely studied in biomedical research for its roles in lactation, reproduction, and immune regulation .

Diagnostic Tools: Measurement of prolactin levels is used in the diagnosis of pituitary tumors, infertility, and other endocrine disorders .

Therapeutic Strategies: Prolactin and its receptor are potential targets for therapeutic interventions in conditions such as breast cancer, hyperprolactinemia, and autoimmune diseases .

Role in the Life Cycle

Development to Aging and Disease: Prolactin plays a vital role throughout the life cycle, from prenatal development to aging . It is involved in the development of the mammary glands, regulation of the menstrual cycle, and maintenance of pregnancy . Prolactin levels can also influence the progression of certain diseases, such as prolactinomas and breast cancer .

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