SDF-1 beta/CXCL12 Protein, Mouse

SDF-1 beta (Stromal-derived factor-1β, SDF-1β) is a stromal derived CXC chemokine that signal through the CXCR4 receptor. SDF-1β has chemotactic activity on B and T cells^[1][2]. SDF-1 beta/CXCL12 Protein, Mouse is produced in E. coli, and consists of 72 amino acids (K22-M93).

The chemokine stromal-derived factor-1 (SDF-1), which is constitutively expressed in most tissues as SDF-1α and SDF-1β resulting from alternative gene splicing, regulates hematopoiesis, lymphocyte homing, B-lineage cell growth, and angiogenesis^[1][2]. SDF-1β is assigned to the intercrine cytokine family (chemokines) which is characterized by four conserved cysteines that form two disulfide bonds. Furthermore its expression is found in all organs except in blood cells^[3].
SDF-1β which is virtually the same as SDF-1α, except in that the fourth exon consists of only four residues attached to a C-terminus, shows very similar activity in vitro and in tissues, but is twice as potent in the blood. 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^[1][2]. In addition, SDF-1β is shown to be a sufficient factor capable of supporting rodent B-cell lymphopoiesis. SDF-1β is expressed less abundantly and seems to be related to the vascular system. Its greater resistance to proteolysis within the blood predispose it to this role^[3].
Endothelial cells of cerebral microvessels in mice express SDF-1β selectively. Its upregulation is found following focal cerebral ischemia and is associated with the infiltration of CXCR4-expressing peripheral blood cells, such as macrophages. SDF-1β also has a greater effect on angiogenesis in human microvascular endothelial cells (HMEC)^[3]. Compared with SDF-1α, SDF-1β is more resistant to blood-dependent degradation, stimulates angiogenesis and is present in highly vascularized organs such as: the liver, spleen and kidneys^[4].

Recombinant mouse SDF-1β (5 mg/kg; tail vein; twice a week; for 3 months) injected into mice bearing type 2 diabetes (T2D). SDF-1β prevents T2D-induced cardiac dysfunction and fibrosis and T2D-down-regulated KLF15 expression in wild-type diabetic heart tissue^[5].

1. The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 50-100 ng/mL.
2. Measured by its ability to inhibit proliferation of Jurkat cells. The ED₅₀ this effect is 2.589 ng/mL, corresponding to a specific activity is 3.86×10^5 units/mg.
3. Measured by its ability to chemoattract BaF3 cells transfected with human CXCR4. The ED₅₀ for this effect is 0.8552 ng/mL, corresponding to a specific activity is 1.169×10^6 units/mg.

Mouse

E. coli

Tag Free

P40224-2 (K22-M93)

20315  [NCBI]

Full Length of Isoform-2 Mature Protein

KPVSLSYRCPCRFFESHIARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQEYLEKALNKRLKM

Approximately 10 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.

<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 from date of receipt. 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]. Maria De La Luz Sierra, et al. Differential processing of stromal-derived factor-1alpha and stromal-derived factor-1beta explains functional diversity. Blood. 2004 Apr 1;103(7):2452-9.  [Content Brief]

  [2]. 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]

  [3]. Miroslaw Janowski. Functional diversity of SDF-1 splicing variants. Cell Adh Migr. 2009 Jul-Sep;3(3):243-9.  [Content Brief]

  [4]. Kleanthis Fytianos, et al. Anti-Fibrotic Effect of SDF-1β Overexpression in Bleomycin-Injured Rat Lung. Pharmaceutics. 2022 Aug 27;14(9):1803.  [Content Brief]

  [5]. Yuanyuan Tian, et al. KLF15 negatively regulates cardiac fibrosis by which SDF-1β attenuates cardiac fibrosis in type 2 diabetic mice. Toxicol Appl Pharmacol. 2021 Sep 15;427:115654.  [Content Brief]