SRP9000
Prolactin human
human, recombinant, expressed in HEK 293 cells
Sinonimo/i:
PRL
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About This Item
Codice UNSPSC:
51111800
NACRES:
NA.32
Prodotti consigliati
Origine biologica
human
Livello qualitativo
Ricombinante
expressed in HEK 293 cells
Sterilità
non-sterile
Saggio
≥95% (SDS-PAGE)
Stato
liquid
Potenza
≤2 ng/mL Nb2-11 cells proliferation EC50
Durata
2 yr
PM
23 kDa
tecniche
cell culture | mammalian: suitable
Impurezze
≤1 EU/μg protein Endotoxin level
Temperatura di conservazione
−20°C
Informazioni sul gene
human ... prl(5617)
Descrizione generale
Prolactin is a lactogenic hormone that plays a role in breast cancer, regulation of reproductive function, and immunoregulation. The prolactin cDNA encodes a 227 amino acid residue protein with a putative 28 amino residue signal peptide. Removal of the signal peptide results in the mature hormone corresponding to amino acids 29-227 of natural prolactin. There are several natural occurring molecular forms of prolactin, including a monomer, a non-glycosylated form, and a glycosylated form.
Prolactin is manufactured using an all-human production system, with full chemically defined ingredients and with no serum. It is therefore completely animal- and xeno-component free.
Research Area: IMMUNO AND CKS
Prolactin (PRL) is a multifunctional polypeptide hormone primarily produced by the lactotrophic cells of the anterior pituitary gland in vertebrates.
Prolactin (PRL) is a multifunctional polypeptide hormone primarily produced by the lactotrophic cells of the anterior pituitary gland in vertebrates.
Applicazioni
Prolactin human has been used:
- in in vitro experiments to examine its effects in sleep-like concentrations on T-cell migration
- to study its effects on claudin 2 (CLDN2) expression in the Caco-2 intestinal epithelial cell model
- in microplate assays to demonstrate the specificity of the antibodies for vasoinhibin
Prolactin is glycosylated.
Azioni biochim/fisiol
Glycosylated human prolactin (G-hPRL) was first isolated and purified from human pituitaries by Lewis et al., with an estimated molecular mass of 25,000 Da and an immunological and biological activity of 25–50% that of non-glycosylated hPRL. The presence of a unique and partially occupied glycosylation site in Asn-31 in human, monkey, ovine, porcine, dromedary, equine and whale PRL makes it an ideal model of glycosylation for N-glycan studies since it exhibits the simplest type of glycosylation macroheterogeneity, with an occupancy range of 10-30% of G-hPRL relative to the total hPRL of either pituitary or recombinant origin. It has been postulated that hPRL glycosylation might possibly modulate the bioactivity of the circulating pool of the hormone, perhaps by selectively down regulating PRL action at individual target tissues.
Prolactin is recognized in breast milk and can enhance Ca2+ absorption through both transcellular and paracellular pathways in the small and large intestine. It is crucial for lactation and reproduction and is demonstrated to have numerous effects on growth, development, metabolism, immunoregulation, and protection. The prolactin signaling pathway begins with the binding of prolactin to the prolactin receptor (PRLR).
Stato fisico
This product is supplied as a solution in 0.2 μm filtered phosphate buffered saline with no additives or carrier proteins. It is aseptically filled.
Nota sulla preparazione
Briefly centrifuge the vial before opening. After initial thawing it is recommended to store the protein in working aliquots at -20°C. The product can be diluted in PBS.
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Repr. 1B
Codice della classe di stoccaggio
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
I Pellegrini et al.
Endocrinology, 122(6), 2667-2674 (1988-06-01)
Multiple forms of PRL differing in their physicochemical and biological characteristics have been described. We have analyzed the molecular forms of human (h) PRL released in culture by pure hPRL-secreting tumors with a particular attention to glycosylated hPRL. The prolactinoma
C R Soares et al.
Biotechnology and applied biochemistry, 32 ( Pt 2), 127-135 (2000-09-26)
Two eukaryotic human prolactin (hPRL) expression vectors, based on a selectable dihydrofolate reductase (dhfr) marker, were used to transfect dhfr(-) Chinese- hamster ovary (CHO) cells. One vector, p658-hPRL, contains the hepatitis-B virus-X cDNA coding for a viral transactivator and sequences
M E Freeman et al.
Physiological reviews, 80(4), 1523-1631 (2000-10-04)
Prolactin is a protein hormone of the anterior pituitary gland that was originally named for its ability to promote lactation in response to the suckling stimulus of hungry young mammals. We now know that prolactin is not as simple as
T Hoffmann et al.
Journal of endocrinological investigation, 16(10), 807-816 (1993-11-01)
To analyze the role of individual glycosylation pattern on PRL biopotency, monomeric prolactin (PRL), secreted by human prolactinoma cells in culture, was isolated by gel filtration and separated by affinity chromatography on Concanavalin A-Sepharose or Lentil-Agarose. These lectins allowed the
U J Lewis et al.
Endocrinology, 124(3), 1558-1563 (1989-03-01)
Two forms of glycosylated PRL (G-PRL) which differed in their binding properties to Concanavalin-A (Con-A) were isolated from human pituitary glands. One form, G1-hPRL, was only slightly retarded by Con-A; the other, G2-hPRL, was adsorbed by Con-A and could be
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