Recombinant Mouse Thrombospondin-2 (THBS2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04487P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Thbs2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Thbs2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Thbs2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Thbs2.

Recombinant Mouse Thrombospondin-2 (THBS2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04487P
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Product Overview

Description Recombinant Mouse Thrombospondin-2 (THBS2) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q03350
Target Symbol THBS2
Synonyms Thbs2; Tsp2; Thrombospondin-2
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence GDHVKDTSFDLFSISNINRKTIGAKQFRGPDPGVPAYRFVRFDYIPPVNTDDLNRIVKLARRKEGFFLTAQLKQDRKSRGTLLVLEGPGTSQRQFEIVSNGPGDTLDLNYWVEGNQHTNFLEDVGLADSQWKNVTVQVASDTYSLYVGCDLIDSVTLEEPFYEQLEVDRSRMYVAKGASRESHFRGLLQNVHLVFADSVEDILSKKGCQHSQGA
Expression Range 19-232aa
Protein Length Partial
Mol. Weight 28.1kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties.
Protein Families Thrombospondin family
Database References

KEGG: mmu:21826

STRING: 10090.ENSMUSP00000128308

UniGene: PMID: 28789925

  • TWIST2 induces miR-221-3p expression and consequently suppresses its direct target, THBS2, in lymphatic metastasis cervical cancer. PMID: 29242498
  • TSP2 deficiency imparted a brittle phenotype on cortical bone. electron microscopy revealed less intensely stained collagen fibrils with altered morphology in the extracellular matrix assembled by osteoblasts on the anterior surface of TSP2-KO femora. PMID: 26272319
  • Enhanced levels of TSP-2 in the skin result in reduced susceptibility to chemically-induced skin carcinogenesis. PMID: 24507936
  • in the context of osteoblast differentiation, TSP2 promotes the assembly of a type-I collagen-rich matrix by facilitating pro-collagen processing. PMID: 23763373
  • The proposed mechanism for the shift in stem cell fate in fracture healing is that increased vascular density and hence oxygen availability in TSP2-null mice regulates differentiation. PMID: 23775935
  • The upregulation of TSP-2 mediated by increased oxidative stress contributes to angiogenesis dysfunction in diabetic bone marrow derived angiogenic cells. PMID: 23723366
  • TSP2 is a negative regulator of ischemic fracture healing, and in the absence of TSP2 bone regeneration is enhanced. PMID: 23280580
  • Using a TSP-2-knockout mouse model and cardiac cell transplantation, we found significantly reduced fibrosis and increased endothelial cell density in the peri-graft region. PMID: 22512900
  • the two TSP2 isforms are differentially modulated at injured and noninjured skeletal sites in an animal undergoing fracture healing. PMID: 22362307
  • TSP-2 has a protective role against cardiac inflammation, injury, and dysfunction in acute viral myocarditis. PMID: 22308237
  • astrocyte-derived TSP-2 is critical for the maintenance of physiological MMP-2 and MMP-9 levels during the foreign body response and contributes to the repair of the BBB PMID: 21704005
  • Endothelial nitric oxide synthase controls the expression of the angiogenesis inhibitor thrombospondin 2 PMID: 21949402
  • The secreted protein is an autocrine inhibitor of marrow stromal cell proliferation. PMID: 11874233
  • Megakaryocytes require this protein for normal platelet formation and function. PMID: 12732502
  • Thrombospondin 2 regulates cell proliferation induced by Rac1 redox-dependent signaling PMID: 12861025
  • TSP2-null mice provide an animal model to assist in the understanding of the molecular basis of spontaneous, premature softening of the uterine cervix. PMID: 14561659
  • Delay in expression of TSP2 and metalloproteinase 2 in the wounds of aged mice could contribute to their impaired rate of wound healing. PMID: 14996433
  • CD36 mediates the antiangiogenic effect of thrombospondin-2, which is modulated by histidine-rich glycoprotein PMID: 15748999
  • the absence of TSP2 protects against ovariectomy-induced bone loss by two complementary processes: increased formation and decreased resorption. PMID: 15979292
  • Mutations targeting intermodular interfaces or calcium binding destabilize the thrombospondin-2 signature domain. PMID: 18682400
  • TSP-2 was found to be present in some, but not all, annulus cells of the human annulus and the mouse annulus. PMID: 18718009
  • Taken together, our observations support a role for TSP2 as critical determinant of the brain response to biomaterials. PMID: 19020342
  • TSP-2 expression in the heart protects against age-dependent dilated cardiomyopathy. PMID: 19805649
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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