Recombinant Rat Prolactin Protein, >98%(SDS-PAGE)

Cat. No.: rp155196
AVAILABLE TO ORDER
GRADE & PURITY Animal Free ? Animal-free — produced without animal-derived components to reduce contamination risk. Use in biomanufacturing and culture avoiding animal-origin material. Carrier Free ? Carrier-free — supplied without added carrier protein/stabilizer. Use when carriers (e.g. BSA) would interfere with conjugation or sensitive assays. Bioactive ? Bioactive grade — verified to retain biological activity in functional assays. Use when the molecule must be functionally active, not just pure. ActiBioPure™ ? ActiBioPure™ — Aladdin's premier line for bioactive and recombinant products. Use when both high purity and preserved biological activity are required. High Performance ? High-performance grade with optimized purity and performance characteristics. Use for sensitive analyses where ordinary grades fall short. PBS Only ? PBS-only formulation — supplied in phosphate-buffered saline with no other additives. Use when you need a clean PBS buffer free of stabilizers/carriers. ≥98%(SDS-PAGE)
Expression System
E.coli
Accession #
P01237
Protein Tag
No tag
Expression system
E. coli
Endotoxin Concentration
<1.0 EU/μg
Bioactivity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using rat Nb2-11 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.
 ·  off list, applied to all prices below.
Size
Status
Price
Qty
10μg
rp155196-10μg
2
$139.90
50μg
rp155196-50μg
1
$309.90
100μg
rp155196-100μg
1
$579.90
1mg
rp155196-1mg
1-2 wks(?)
Item is derived from our semi-finished stock and is processed in 1-2 weeks.
$3,999.90
Enter a quantity for the sizes you want to add.
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Why this grade

Animal Free,Carrier Free,Bioactive,ActiBioPure™,High Performance,PBS Only,≥98%(SDS-PAGE) ActiBioPure™,Animal Free,Bioactive,Carrier Free,High Performance,PBS Only for sensitive chromatographic and analytical workflows requiring minimal baseline interference.

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Storage & shipping

Store at -20°C,Avoid repeated freezing and thawing Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.

📋

Quality documents

SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.

📚

Literature proof

Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.

Overview

Various hormones are secreted from the anterior pituitary during development and growth. Prolactin is a growth factor secreted by the anterior pituitary that is necessary for the proliferation and differentiation of the mammary glands.
Background
The neuroendocrine pituitary hormone Prolactin (PRL), also known as lactotrophin, mamotrophin, luteotropic hormone (LTH), or luteotropin, is a secreted hormone that affects reproduction and homeostasis in vertebrates. The functions of PRL can be placed in six broad categories: 1) reproduction and lactation; 2) growth and development; 3) endocrinology and metabolism; 4) brain and behavior; 5) immunomodulation; and 6) electrolyte balance. PRL is secreted by the anterior pituitary gland, mammary gland, placenta, brain, uterus, decidua, dermal fibroblasts, B cells, T cells, NK cells, and some breast cancer cell lines. Although the major form of PRL is a 23 kDa monomeric protein, splice variants of 14, 16, and 22 kDa have been identified. PRL has also been found to be glycosylated, phosphorylated, dimerized, and polymerized. Glycosylation, phosphorylation, dimerization, or polymerization of PRL result in lower activity.
Cell activation by PRL is mediated by a single chain membrane-bound protein belonging to the class 1 cytokine superfamily. The PRL receptor (PRL R) contains an extracellular, transmembrane, and intracellular domain. Transcriptional regulation of the PRL R gene results in several different species-dependent isoforms of PRL R being produced. Although the cytoplasmic domains of the different isoforms vary in length and composition, their extracellular domains are identical. In rats, three major PRL receptor isoforms have been described, a short (291 amino acid), an intermediate (393 amino acid), and a long (591 amino acid). PRL receptors are found in mammary tissue, pituitary gland, brain, heart, lung thymus, spleen, liver, pancreas, kidney, adrenal gland, uterus, skeletal muscle, and skin. A soluble form of PRL-R containing the 206NH2-terminal amino acids of the extracellular domain is secreted by mammary epithelial cells and is found in milk. Binding of the transmembrane PRL R results in ligand dimerization followed by binding and phosphorylation of Jak2. Jak2 then phosphorylates STAT and the long form of PRL R. C-src, fyn, and the Ras/Raf/MAP kinase pathway have also been found to be activated upon PRL R ligand binding.

Specifications

Product Name
Recombinant Rat Prolactin Protein, >98%(SDS-PAGE)
Synonyms
Decidual prolactin | GHA1 | Growth hormone A1 | Lactogenic hormone | Luteotropic hormone | Mammotropin | PRL | Prolactin | Prolactin precursor
Grade
ActiBioPure™, Animal Free, Bioactive, Carrier Free, High Performance, PBS Only
Specifications & Purity
Animal Free, Carrier Free, Bioactive, ActiBioPure™, High Performance, PBS Only, ≥98%(SDS-PAGE)
Purity
>98%(SDS-PAGE)
Bioactivity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using rat Nb2-11 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.
Endotoxin Concentration
<1.0 EU/μg
Expression System
E.coli
Species
Rat
Amino Acids
30-226 aa
Sequence
LPVCSGGDCQ TPLPELFDRV VMLSHYIHTL YTDMFIEFDK QYVQDREFIA KAINDCPTSS LATPEDKEQA QKVPPEVLLN LILSLVHSWN DPLFQLITGL GGIHEAPDAI ISRAKEIEEQ NKRLLEGIEK IISQAYPEAK GNEIYLVWSQ LPSLQGVDEE SKDLAFYNNI RCLRRDSHKV DNYLKFLRCQ IVHKNNC
Protein Tag
No tag
Accession #
Predicted molecular weight
22.6 kDa
SDS-PAGE
22.6 kDa
Molecule Type
Protein
Storage and Shipping
Shape
Lyophilized
Reconstitution
It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Storage
Store at -20°C,Avoid repeated freezing and thawing
Shipped In
Ice chest + Ice pads
Stability And Storage
Lyophilized protein should be stored at -20°C for 1 year. Upon reconstitution, store at 2°C to 8°C for up to 1 week. Further dilute in a buffer containing a carrier protein or stabilizer (e.g. 0.1% BSA, 10%FBS, 5%HSA or 5% trehalose solution), protein ali
Images

Recombinant Rat Prolactin Protein (rp155196)-Protein Bioactivity
Fully biologically active when compared to standard. The ED₅₀ as determined by a cell proliferation assay using rat Nb2-11 cells is less than 1.0 ng/mL, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.

Recombinant Rat Prolactin Protein (rp155196)-SDS-PAGE
Recombinant Rat Prolactin Protein was resolved with SDS-PAGE under reducing (R) and visualized by Coomassie® Blue staining. Showing a single band at 22.6 kDa.

Documentation

📋 Safety Data Sheet (SDS)

Comprehensive hazard, handling, storage, and regulatory compliance document.

Download SDS →

✅ Certificate of Analysis (COA)

Lot-specific quality data. Enter your lot number to retrieve the exact COA.

Look up COA →

📊 Datasheet

Quick-reference summary of product specifications and applications.

View datasheet →

🔬 Specification Sheet

Full quality attributes and acceptance criteria for this grade.

View spec sheet →

Advanced Data

Certificates(CoA,COO,BSE/TSE and Analysis Chart)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:

Find and download the COA for your product by matching the lot number on the packaging.

3 results found

Lot NumberCertificate TypeDateItem
ZJ23F0600454Certificate of AnalysisJun 17, 2026 rp155196
ZJ23F0600455Certificate of AnalysisJun 17, 2026 rp155196
ZJ23F0600456Certificate of AnalysisJun 17, 2026 rp155196
Documents & Articles
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