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Merck
CN

SRP9000

Sigma-Aldrich

催乳素 人

human, recombinant, expressed in HEK 293 cells

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别名:
PRL
UNSPSC代码:
51111800
NACRES:
NA.32

生物来源

human

质量水平

重组

expressed in HEK 293 cells

无菌性

non-sterile

检测方案

≥95% (SDS-PAGE)

形式

liquid

效能

≤2 ng/mL Nb2-11 cells proliferation EC50

技术

cell culture | mammalian: suitable

杂质

≤1 EU/μg protein Endotoxin level

储存温度

−20°C

一般描述

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.

应用

Prolactin is glycosylated.

生化/生理作用

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.

外形

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.

制备说明

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.

象形图

Health hazard

警示用语:

Danger

危险声明

预防措施声明

危险分类

Repr. 1B

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

监管及禁止进口产品

分析证书(COA)

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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
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)
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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