PIP Protein

Prolactin-Induced Protein Human Recombinant
Cat. No.
BT29699
Source
Escherichia Coli.
Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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In Stock

Description

PIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (29-146 a.a.) and having a molecular mass of 15.9kDa.
PIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Prolactin-inducible protein (PIP), a major protein found in benign breast gross cysts, serves as a significant breast cancer indicator. Its presence is observed in approximately half of all breast cancer specimens. PIP expression is found in exocrine glands, various pathological conditions, and particularly in breast cysts and cancers with apocrine characteristics. Notably, PIP and prostate-specific antigen exhibit co-expression in androgen receptor-positive breast tumors.
Description
Recombinant human PIP, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 141 amino acids (specifically, residues 29-146). It has a molecular weight of 15.9 kDa. This PIP protein is fused to a 23 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The PIP protein solution is provided at a concentration of 1 mg/ml and contains the following components: 20 mM Tris-HCl buffer (pH 8.0), 10% glycerol, and 0.4 M Urea.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein like 0.1% HSA or BSA is advisable for long-term storage. It's important to avoid repeated freezing and thawing of the product.
Purity
The purity of the PIP protein is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQDNTRKI IIKNFDIPKS VRPNDEVTAV LAVQTELKEC MVVKTYLISS IPLQGAFNYK YTACLCDDNP KTFYWDFYTN RTVQIAAVVD VIRELGICPD DAAVIPIKNN RFYTIEILKV E.

Product Science Overview

Introduction

Prolactin-Induced Protein (PIP) is a glycoprotein with a molecular weight of approximately 15-17 kDa. It was initially identified as a highly secreted protein in T47D breast cancer cells following treatment with prolactin and androgens . PIP is expressed abundantly in breast cancer cells but is generally low or absent in normal breast cells .

Biological Function

PIP is considered a valuable biomarker associated with both benign and malignant pathological conditions of the mammary gland . It plays a role in modulating immune responses and has been implicated in breast tumorigenesis . PIP expression in breast cancer has been shown to correlate with better prognosis and patient response to chemotherapy . However, some studies suggest that PIP may also play a role in metastasis .

Preparation Methods

Recombinant human prolactin protein, including PIP, is typically produced using E. coli expression systems. The protein is purified to a high degree, with purity levels exceeding 97% as determined by SDS-PAGE . The recombinant protein is often lyophilized and can be reconstituted in sterile solutions for use in various applications .

Chemical Reactions and Analysis

PIP has been shown to modulate antitumor immune responses and metastasis in breast cancer models . In vitro studies have demonstrated that stable expression of PIP in breast cancer cell lines does not significantly alter their proliferation, migration, or response to anticancer drugs compared to control cells . However, in vivo studies using mouse models have shown that PIP-expressing tumors display delayed onset and reduced growth, which is associated with higher percentages of natural killer cells and reduced percentages of type 2 T-helper cells in the tumor environment . Paradoxically, PIP expression has also been associated with a higher number of metastatic colonies in the lungs .

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