추천 제품
일반 설명
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.
애플리케이션
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.
생화학적/생리학적 작용
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).
물리적 형태
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.
제조 메모
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.
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
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
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
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)
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
Structural variants of prolactin: occurrence and physiological significance.
Endocrine reviews, 16(3), 354-369 (1995-06-01)
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
Maternal epidermal growth factor promotes neonatal claudin-2 dependent increases in small intestinal calcium permeability
Function (Oxford, England), (5), zqad033-zqad033 (2023)
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