Recombinant Mouse Osteocalcin (BGLAP) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02996P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Osteocalcin (BGLAP) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02996P
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Product Overview

Description Recombinant Mouse Osteocalcin (BGLAP) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P86546
Target Symbol BGLAP
Synonyms Bglap; Osteocalcin; Bone Gla protein; BGP; Gamma-carboxyglutamic acid-containing protein
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence YLGASVPSPDPLEPTREQCELNPACDELSDQYGLKTAYKRIYGITI
Expression Range 50-95aa
Protein Length Full Length of Mature Protein
Mol. Weight 21.1kDa
Research Area Signal Transduction
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 Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.
Subcellular Location Secreted.
Protein Families Osteocalcin/matrix Gla protein family
Database References

KEGG: mmu:12096

STRING: 10090.ENSMUSP00000075425

UniGene: PMID: 25279792

  • the uncarboxylated form of osteocalcin does not trigger Akt phosphorylation and glucose uptake by itself but promotes insulin-induced glucose uptake in myotubes, probably by up-regulating Akt signaling through ERK activation PMID: 25735975
  • The Twist2-Cre, Osterix-Cre and osteocalcin-Cre lines to generate conditional beta1 integrin deletions, were used to investigate the role of beta1 integrins on skeletal phenotype. PMID: 25183373
  • OCN is gamma-carboxylated by the gamma-carboxylase (GGCX) on three glutamic acid residues, a cellular process requiring reduction of vitamin K by a second enzyme, VKORC1. PMID: 25753038
  • results showed an increase in the expression of Cbfa1 and OCN in fibroblasts and osteoblasts exposed to fluoride. PMID: 24680482
  • Data indicate that Ca2+ binding triggered a similar conformational transition in both gamma-carboxyglutamic acid-containing protein osteocalcin (Gla-OCN) and Glu-OCN from a disordered structure to a more compact/stable form. PMID: 24896339
  • In primary adipocytes, both carboxylated and uncarboxylated osteocalcin increased basal and insulin-stimulated glucose transport. PMID: 24554534
  • Taken together, these findings demonstrate that SMILE negatively regulates osteocalcin via a direct interaction with RUNX2 PMID: 24389415
  • Osteoblast-specific expression of Fra-2/AP-1 controls adiponectin and osteocalcin expression and affects metabolism. PMID: 24046454
  • contribution of OC-OPN to fracture toughness is related to their presence at the extrafibrillar organic-mineral interfaces PMID: 24128197
  • Insulin resistance in osteoblasts led to a decrease in circulating levels of the active form of osteocalcin, thereby decreasing insulin sensitivity in skeletal muscle. PMID: 24642469
  • loss of osteocalcin/Gprc6a signaling has a profound effect on beta-cell mass accrual during late pancreas morphogenesis PMID: 24009262
  • This study reveals that the skeleton via osteocalcin influences cognition and contributes to the maternal influence on fetal brain development. PMID: 24074871
  • T3 stimulates the activation of Rho-kinase in osteoblasts, which functions as a negative regulator of T3-stimulated osteocalcin synthesis PMID: 23123502
  • Uncarboxylated osteocalcin acts via Gprc6a to induce GLP-1 release from the gut; the stimulatory effect of uncarboxylated osteocalcin on insulin secretion is largely mediated by GLP-1. PMID: 23437377
  • These results indicate that PP2A Calpha and its activity play a negative role in osteoblast differentiation and Osterix is a key factor responsible for regulating the expressions of Bsp and OCN during PP2A Calpha-mediated osteoblast differentiation. PMID: 23042641
  • alphaNAC interacts with histone deacetylase corepressors to control Myogenin and Osteocalcin gene expression. PMID: 23092676
  • Data from TR4 (steroid/thyroid hormone receptor 4) knockout mice suggest that TR4 binds to promoter region of osteocalcin gene and induces osteocalcin expression; this interaction maintains osteoblast activity during bone development/remodeling. PMID: 22676849
  • Alterations of responses in knockout mice that suggest participation of osteocalcin in transmission of information about those sensory stimuli. PMID: 22350212
  • BMP2 induces osteoblast differentiation through Runx2-dependent ATF6 expression, which directly regulates Oc transcription. PMID: 22102412
  • Data show that Mkp1 KO mice displayed delayed differentiation and reduced expressions of osteocalcin (OCN) and Runx2 genes associated with osteoblast maturation and function. PMID: 21852324
  • Both BGP overexpression and treatment with purified Bone Gla Protein (BGP) resulted in stabilization of hypoxia-inducible factor 1alpha (HIF-1alpha) in chondrocytes and vascular smooth muscle cells PMID: 21757657
  • Foxo1 is a novel negative regulator of osteoblast-specific transcription factor Runx2 and modulates IGF1/insulin-dependent regulation of osteocalcin expression in osteoblasts. PMID: 21471200
  • Data show that osteocalcin synthesis was significantly reduced in the stable HSP27-transfected MC3T3-E1 cells and normal human osteoblasts. PMID: 21427224
  • Findings expand the biological importance of osteocalcin, begin to unravel its molecular mode of action, and provide the first evidence that the skeleton is an endocrine regulator of fertility. PMID: 21333348
  • the activation of PPARgamma inhibits osteocalcin expression both by suppressing the expression of Runx2 and by interfering with the transactivation ability of Runx2 PMID: 12704187
  • 1,25-(OH)(2)D(3)and T3 upregulated osteocalcin, depending on the stage of cell differentiation. PMID: 12798773
  • osteocalcin fibroblast growth factor response element activation is enhanced by MINT, the Msx2 interacting nuclear matrix target PMID: 15131132
  • Nell-1 reduced osterix-producing cells and increased bone sialoprotein, osteocalcin, and BMP-7 expression. PMID: 16936265
  • Expression of the osteoblast-specific gene OC was examined in marrow stromal cell cultures at various time points. PMID: 17705049
  • during osteoblast differentiation, early on, when Runx2 protein and DNA-binding are maximal, Runx2 is nearly absent from the OC promoter. Later, Runx2 is recruited to the OC promoter as Runx2 mRNA, protein, and in vitro DNA binding progressively decrease. PMID: 18821584
  • Results show that induction of alkaline phosphatase, type I collagen, osteocalcin, CD44, CD47 and CD51 by mevinolin is responsible for the osteoblastic differentiation of D1 cells. PMID: 19162043

    • 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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