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SRP9000

Sigma-Aldrich

Prolactin human

human, recombinant, expressed in HEK 293 cells

Synonym(s):

PRL

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About This Item

UNSPSC Code:
51111800
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in HEK 293 cells

sterility

non-sterile

Assay

≥95% (SDS-PAGE)

form

liquid

potency

≤2 ng/mL Nb2-11 cells proliferation EC50

shelf life

2 yr

mol wt

23 kDa

technique(s)

cell culture | mammalian: suitable

impurities

≤1 EU/μg protein Endotoxin level

storage temp.

−20°C

Gene Information

human ... prl(5617)

General description

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.

Application

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.

Biochem/physiol Actions

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).

Physical form

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.

Preparation Note

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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Repr. 1B

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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V Y Butnev et al.
Journal of protein chemistry, 15(5), 413-426 (1996-07-01)
Glycosylated equine prolactin (G-ePRL) and nonglycosylated ePRL were purified to homogeneity from side fractions obtained during isolation of LH/FSH from horse pituitaries. Both PRL forms were isolated together in high yield by the isolation procedure used for glycosylated porcine PRL/(G-pPRL)
Structural variants of prolactin: occurrence and physiological significance.
Y N Sinha
Endocrine reviews, 16(3), 354-369 (1995-06-01)
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
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
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

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