SDF-1 alpha/CXCL12 Protein, Rat

SDF-1 alpha (Stromal Cell-Derived Factor-1α, SDF-1α) is a member of the chemokine α subfamily that lack the ELR domain. SDF-1α works as a chemoattractant for T- and B-lymphocytes and monocytes. SDF-1α is a ligand for CXCR4. The SDF-1α/CXCR4 signaling mediates many physiological processes including cell trafficking, angiogenesis, embryogenesis, tumor invasion and metastatic. It also controls the chemotaxis of hematopoietic stem cells homing to the bone marrow^[1][2]. SDF-1 alpha/CXCL12 Protein, Rat is produced in E. coli, and consists of 68 amino acids (K22-K89).

Stromal cell-derived factor-1 (SDF-1), an important member of the chemokine family, is expressed in two subtypes, SDF-1α and SDF-1β, with SDF-1α being the main subtype. SDF-1α is widely present in many tissues and organs of the human body, such as the lymph nodes, bone marrow, liver, lung, muscle, small intestine, kidney, and brain, and can sustainably exist in these organs and tissues. Studies have shown that SDF-1α plays an important role in the physiological mfunctions of migration, distribution, development, differentiation, and apoptosis of various cells. Moreover, SDF-1α plays a key role in the pathological process of some diseases, such as inflammation, tumor formation and metastasis, pathogen infection, and wound repair^[1][3].
SDF-1 has three isoforms, α, β, and γ, which are different at the splicing level, not at the transcriptional level. The analysis of the genomic structure of SDF-1 in human and mouse revealed two isoforms, SDF-1α and SDF-1β, which are encoded by a single gene and result from alternative splicing. SDF-1α comprises 3 exons and encodes a protein of 89 amino acids whereas SDF-1β consists of 4 exons and encodes a protein of 93 amino acids. Both isoforms are highly similar regarding their sequences with the only difference of 4 additional amino acids at the C-terminus of SDF1β. In adult rat brain, SDF-1α is the predominant one, present in astrocytes, microglia, as well as in neurons. SDF-1α is found positive in normal cholinergic neurons, such as in the medial septum and substantia innominata, and in dopaminergic neurons, such as in the substantia nigra (SN) pars compacta and the ventral tegmental area. SDF-1α is the only known ligand for CXCR4. CXCR4 is also a target for human immunodeficiency virus (HIV) binding^[1][2].
In vitro and in vivo studies using ischemic reperfusion models and a pretreatment with SDF-1α results in decreased infarct size and increases resistance to hypoxic damage and apoptotic cell death via activation of ERK-1/2 and AKT phosphorylation^[1]. The SDF-1α/CXCR4 signaling maintains central nervous system homeostasis through the interaction with the neurotransmitter and neuropeptide systems, the neuroendocrine systems^[2]. An increasing number of animal experiments have shown that SDF-1α can enhance the migration of BMSCs, mobilize BMSCs to diseased areas, and promote their proliferation and differentiation^[3].

Recombinant rat SDF-1α (0, 5, 10, 30, 50 or 100 ng/mL) activates PI-3K/Akt signaling, and consequently promotes the proliferation and chemotaxis in primary rat vascular smooth muscle cells (VSMCs) ^[4].

Recombinant rat SDF-1α (4 μg/4 μL; intracranial injection) ameliorates TBI-induced brain edema and blood-brain barrier disruption in Sprague-Dawley rats underwent traumatic brain injury (TBI) model. SDF-1α repressed inflammatory responses by inhibiting the expression of pro-inflammatory cytokines, such as TNF-α, IL-1β, and IL-6. SDF-1α attenuated the brain lesion by affecting the ERK and NF-κB signaling pathways after mechanical head trauma in rats^[5].

1. Full biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 50-100 ng/ml.
2. Measured in a cell proliferation assay using Jurkat cells. The ED₅₀ this effect is 3.323 ng/mL, corresponding to a specific activity is 3.01×10⁵ units/mg.
3. Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED₅₀ for this effect is ≤71.82 ng/mL, corresponding to a specific activity is ≥1.392×10⁴ U/mg.

• 
  Measured in a cell proliferation assay using Jurkat cells. The ED₅₀ for this effect is 3.323 ng/mL, corresponding to a specific activity is 3.01×10⁵ units/mg.

Rat

E. coli

Tag Free

Q9QZD1/Q80YV8 (K22-K89)

24772  [NCBI]

KPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKSNNRQVCIDPKLKWIQEYLDKALNK

Approximately 8-10.07 kDa

• 
  Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of 20 mM PB,150 mM NaCl, pH 7.4 or PBS, pH 7.0.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Santhosh K Ghadge, et al. SDF-1α as a therapeutic stem cell homing factor in myocardial infarction. Pharmacol Ther. 2011 Jan;129(1):97-108.  [Content Brief]

  [2]. Kryczek I, et al. Stroma-derived factor (SDF-1/CXCL12) and human tumor pathogenesis. Am J Physiol Cell Physiol. 2007 Mar;292(3):C987-95.  [Content Brief]

  [3]. Zheng Jiang, et al. Contribution of SDF-1α/CXCR4 signaling to brain development and glioma progression. Neurosignals. 2013;21(3-4):240-58.  [Content Brief]

  [4]. Zhiqiang Meng, et al. SDF Factor-1α Promotes the Migration, Proliferation, and Osteogenic Differentiation of Mouse Bone Marrow Mesenchymal Stem Cells Through the Wnt/β-Catenin Pathway. Stem Cells Dev. 2021 Jan 15;30(2):106-117.  [Content Brief]

  [5]. Wei Jie, et al. SDF-1α/CXCR4 axis is involved in glucose-potentiated proliferation and chemotaxis in rat vascular smooth muscle cells. Int J Exp Pathol. 2010 Oct;91(5):436-44.  [Content Brief]

  [6]. Weifeng Sun, et al. Intracranial injection of recombinant stromal-derived factor-1 alpha (SDF-1α) attenuates traumatic brain injury in rats. Inflamm Res. 2014 Apr;63(4):287-97.  [Content Brief]