SDF2 Human

Stromal Cell-Derived Factor 2 Human Recombinant
Cat. No.
BT24149
Source
Escherichia Coli.
Synonyms
Stromal cell-derived factor 2, SDF-2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek'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

SDF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (19-211 a.a) and having a molecular mass of 23.7kDa.
SDF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Stromal Cell-Derived Factor 2 (SDF2) is a secreted protein that shares similarities with hydrophilic regions of yeast mannosyltransferases. SDF2 expression is widespread, and the gene is highly conserved in mammals. This gene undergoes alternative splicing, producing both protein-coding and non-coding variants.
Description
Recombinant human SDF2, expressed in E. coli, is a single-chain polypeptide lacking glycosylation. It comprises 216 amino acids (residues 19-211), resulting in a molecular weight of 23.7 kDa. For purification, a 23-amino acid His-tag is fused to the N-terminus, and proprietary chromatographic techniques are employed.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
SDF2 protein is supplied at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.4 M Urea.
Stability
For short-term storage (2-4 weeks), the product can be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
SDS-PAGE analysis confirms a purity exceeding 85%.
Synonyms
Stromal cell-derived factor 2, SDF-2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAEL.

Product Science Overview

Gene and Protein Structure

The SDF2 gene encodes a protein that is believed to be a secretory protein. It has regions of similarity to hydrophilic segments of yeast mannosyltransferases . The human recombinant form of SDF2 is produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 216 amino acids, with a molecular mass of approximately 23.7 kDa .

Biological Function

SDF2 is involved in the endoplasmic reticulum (ER) stress response and protein folding. It is part of the chaperone complex that assists in the proper folding of newly synthesized proteins and the refolding of misfolded proteins . This function is crucial for maintaining cellular homeostasis and preventing the accumulation of misfolded proteins, which can lead to various diseases.

Expression and Localization

The expression of SDF2 is ubiquitous, meaning it is found in various tissues throughout the body . It is primarily localized in the endoplasmic reticulum, where it performs its chaperone functions .

Clinical Significance

While the exact clinical implications of SDF2 are still being studied, its role in protein folding and ER stress response suggests that it could be involved in conditions related to protein misfolding and aggregation. These conditions include neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease.

Research and Applications

Recombinant human SDF2 is used in various research applications to study its function and potential therapeutic uses. Its role in the ER stress response makes it a target of interest for developing treatments for diseases caused by protein misfolding.

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