SDF 1a Human

Stromal Cell-Derived Factor-1 Alpha Human Recombinant (CXCL12)
Cat. No.
BT23211
Source
Escherichia Coli.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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

Stromal Cell-Derived Factor-1 alpha Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 8004 Dalton.
The SDF-1a is purified by proprietary chromatographic techniques.

Product Specs

Introduction
SDF-1, or stromal cell-derived factor-1, is a chemokine officially known as Chemokine (C-X-C motif) ligand 12 (CXCL12). It exists in two isoforms, SDF-1α/CXCL12a and SDF-1β/CXCL12b, resulting from alternative splicing of the same gene. Chemokines are characterized by four conserved cysteines forming two disulfide bonds. CXCL12 proteins belong to the CXC chemokine group, where the first two cysteines are separated by a single amino acid. Demonstrating strong chemotactic activity for lymphocytes, CXCL12 plays a critical role in cell coordination during development, including directing hematopoietic cell migration from the fetal liver to bone marrow during embryogenesis. CXCL12 gene knockout mice exhibit lethality either prenatally or within an hour after birth. Furthermore, CXCL12a influences neuronal electrophysiology. Studies in mice reveal widespread CXCL12 expression across various tissues, including the brain, thymus, heart, lung, liver, kidney, spleen, and bone marrow. CXCL12 binds to the CXCR4 receptor, previously known as fusin. While this interaction was initially considered exclusive, recent findings suggest CXCL12 might also bind to the CXCR7 receptor. The gene encoding CXCL12 is located on human chromosome 10. Notably, both CXCL12 and CXCR4 exhibit high sequence identity between humans and mice, with 99% and 90% similarity, respectively.
Description
Recombinant Human Stromal Cell-Derived Factor-1 alpha, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 68 amino acids. With a molecular weight of 8004 Daltons, this SDF-1a protein is purified using proprietary chromatographic techniques.
Physical Appearance
White, sterile-filtered, lyophilized powder.
Formulation
The protein was lyophilized from a sterile solution at a concentration of 1 mg/ml, without any additives.
Solubility
Reconstitute the lyophilized Stromal Cell-Derived Factor-1a in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted with other aqueous solutions.
Stability
Lyophilized SDF-1a is stable at room temperature for up to 3 weeks. However, it is recommended to store it desiccated at temperatures below -18°C. After reconstitution, store CXCL12 at 4°C for 2-7 days. For long-term storage, freeze at -18°C, preferably with the addition of a carrier protein like HSA or BSA (0.1%). Avoid repeated freeze-thaw cycles.
Purity
Exceeds 98.0% purity, as determined by: (a) RP-HPLC analysis. (b) SDS-PAGE analysis.
Biological Activity
The specific activity, assessed by the ability to chemoattract PHA and IL-2 activated human peripheral T cells at a concentration range of 20-80 ng/ml, corresponds to 12,500-50,000 IU/mg.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.
Source
Escherichia Coli.
Amino Acid Sequence

KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK 

Product Science Overview

Introduction

Stromal Cell-Derived Factor-1 Alpha (SDF-1α), also known as C-X-C motif chemokine 12 (CXCL12), is a chemokine protein encoded by the CXCL12 gene in humans. This protein plays a crucial role in various physiological and pathological processes, including immune response, tissue regeneration, and cancer metastasis .

Gene and Protein Structure

The CXCL12 gene is located on chromosome 10 at the band 10q11.21 and contains four exons . This gene produces seven isoforms through alternative splicing, with SDF-1α and SDF-1β being the most studied . The protein belongs to the intercrine alpha (chemokine CXC) family, characterized by the presence of four conserved cysteines that form two disulfide bonds . The initial pair of cysteines in CXC chemokines are separated by one intervening amino acid .

Function and Mechanism

CXCL12 is ubiquitously expressed in many tissues, including the brain, thymus, heart, lung, liver, kidney, spleen, platelets, and bone marrow . It is strongly chemotactic for lymphocytes and plays a vital role in directing the migration of hematopoietic cells from the fetal liver to the bone marrow during embryogenesis . The protein’s N-terminal residues serve as a receptor binding site, with Lys-1 and Pro-2 directly participating in receptor activation .

Clinical Significance

CXCL12 signaling has been observed in several cancers, including breast cancer, where it is implicated in metastasis . Mutations in the CXCL12 gene are associated with resistance to human immunodeficiency virus type 1 (HIV-1) infections . Additionally, the CXCL12 gene contains one of 27 single nucleotide polymorphisms (SNPs) associated with an increased risk of coronary artery disease .

Recombinant CXCL12

Recombinant human CXCL12 is produced using various expression systems to study its function and potential therapeutic applications. For instance, a novel recombinant antibody specific to full-length SDF-1α has been developed for biomarker studies in conditions characterized by tissue hypoxia, such as myocardial infarction and ischemic cardiomyopathy . This recombinant antibody facilitates the investigation of full-length SDF-1α kinetics and its role in disease .

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