Periostin Human, HEK

Periostin Human Recombinant, HEK
Cat. No.
BT27980
Source
HEK 293.
Synonyms
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 38.0% as determined by SDS-PAGE.
Usage
Prospec's 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.
Shipped with Ice Packs
In Stock

Description

Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.

Product Specs

Introduction
Periostin, a 90 kDa disulfide-linked protein composed of 811 amino acids, was initially identified as an osteoblast-specific factor. It acts as a cell adhesion molecule for preosteoblasts and is believed to play a role in osteoblast recruitment, attachment, and spreading. Notably, periostin expression has been found to be significantly upregulated by both transforming growth factor beta-1 (TGFβ1) and bone morphogenetic protein (BMP-2). Structurally, OSF-2, another name for periostin, comprises a signal sequence, followed by a cysteine-rich domain, a fourfold repeat domain, and a C-terminal domain. The fourfold repeat domain exhibits homology to the insect protein fasciclin. Studies have revealed periostin mRNA expression in the developing mouse embryonic and fetal heart, specifically localized to the endocardial cushions responsible for dividing the primitive heart tube into a four-chambered heart.
Description
Recombinant Human Periostin, produced in HEK cells, is a single, glycosylated polypeptide chain encompassing amino acids Asn22 to Gln836 (totaling 821 amino acids). It has a calculated molecular mass of 91.8 kDa and incorporates a 6-amino acid His tag at the C-terminus.
Physical Appearance
White, lyophilized powder after filtration.
Formulation
The Periostin solution, at a concentration of 0.5 mg/ml in phosphate-buffered saline with 5% trehalose, was filtered through a 0.4 μm filter and subsequently lyophilized.
Solubility
To prepare a working stock solution of approximately 0.5 mg/ml, add deionized water to the lyophilized pellet and allow it to dissolve completely. Note that this Periostin is not sterile. Prior to cell culture use, it is crucial to filter the product through an appropriate sterile filter.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to prevent repeated freeze-thaw cycles. The reconstituted protein can be stored at 4°C for a limited period.
Purity
SDS-PAGE analysis determined a purity greater than 38.0%.
Synonyms
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
Source
HEK 293.
Amino Acid Sequence
NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH H.

Product Science Overview

Introduction

Periostin, also known as POSTN or osteoblast-specific factor 2 (OSF-2), is a secreted extracellular matrix (ECM) protein that plays a crucial role in various biological processes, including cell adhesion, migration, and tissue remodeling . The recombinant form of human periostin, expressed in HEK 293 cells, is widely used in research to study its functions and potential therapeutic applications.

Structure and Expression

Periostin is composed of four fasciclin domains, which are involved in protein-protein interactions and cell adhesion . The protein is encoded by the POSTN gene and is primarily expressed in cells of mesenchymal origin, such as osteoblasts and fibroblasts . The recombinant human periostin produced in HEK 293 cells is typically tagged with a His tag for purification purposes and has a high purity level of ≥95% .

Biological Functions

Periostin functions as a ligand for integrins, specifically alpha-V/beta-3 and alpha-V/beta-5 integrins, which are involved in cell adhesion and migration . It plays a significant role in the development and maintenance of various tissues, including bone, heart, and skin. In the context of bone, periostin is essential for osteoblast recruitment, spreading, and attachment, contributing to bone formation and remodeling .

Role in Disease

Periostin has been implicated in several pathological conditions, including cancer, cardiovascular diseases, and asthma. In cancer, periostin promotes tumor progression by enhancing cell survival, invasion, angiogenesis, and metastasis . It is often overexpressed in the tumor microenvironment, where it interacts with integrins on cancer cells to activate signaling pathways such as Akt/PKB and FAK .

In cardiovascular diseases, periostin is involved in the development of heart valves and the progression of degenerative valvular heart disease . It is upregulated in response to tissue injury and plays a role in tissue remodeling and repair. In asthma, periostin is associated with airway remodeling and inflammation, making it a potential target for therapeutic interventions .

Applications in Research

Recombinant human periostin expressed in HEK 293 cells is a valuable tool for studying the protein’s functions and mechanisms in various biological processes and diseases. It is used in a range of applications, including cell adhesion assays, migration studies, and tissue remodeling experiments . The high purity and endotoxin-free nature of the recombinant protein ensure reliable and reproducible results in research settings .

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