Recombinant Rat Osteocalcin (BGLAP) Protein (GST)

Name: Recombinant Rat Osteocalcin (BGLAP) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03078P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Rat Osteocalcin (BGLAP) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P04640
Target Symbol	BGLAP
Synonyms	Bglap; Bglap2; Osteocalcin; Bone Gla protein; BGP; Gamma-carboxyglutamic acid-containing protein
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	YLNNGLGAPAPYPDPLEPHREVCELNPNCDELADHIGFQDAYKRIYGTTV
Expression Range	50-99aa
Protein Length	Full Length of Mature Protein
Mol. Weight	32.6kDa
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	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: rno:25295 STRING: 10116.ENSRNOP00000026530 UniGene: PMID: 27291707 Uncarboxylated osteocalcin potentiates insulin secretion, inhibits Kv channels and increases [Ca(2+)]i. PMID: 27746193 This rat model of complete loss of osteocalcin provides a platform for further understanding the role of osteocalcin in disease. PMID: 27483347 gamma-Carboxylase inhibition prevents osteocalcin carboxylation and protects against diabetic cardiomyopathy, possibly through direct action on upregulated G protein-coupled receptor family C group 6 member A and indirectly via adiponectin. PMID: 27488359 Bone Gla Protein PMID: 25185647 In primary adipocytes, both carboxylated and uncarboxylated osteocalcin increased basal and insulin-stimulated glucose transport. PMID: 24554534 The physiological changes associated with estrous cycle stage were not sufficient to cause a detectable difference in carboxylated or undercarboxylated osteocalcin concentrations in this study. PMID: 23817840 Osteocalcin (OC)-containing neurons are distributed throughout the cerebellar nuclei; OC may play a role in modulating the neuroprotective function of osteopontin. PMID: 22552891 warfarin impaired the carboxylation of osteocalcin in rats. Factor Xa inhibitor edoxaban at or higher doses than needed for an antithrombotic effect sustained the circulating Gla-osteocalcin level. PMID: 22999414 results suggest that under some physiological conditions the oncoprotein MDM2 may cooperate with p53 to regulate the osteocalcin gene during osteoblastic differentiation. PMID: 22405968 These data are strongly in support of Sp1 as an essential transcription factor required for Osx recruitment and transactivation of the OCN promoter. PMID: 21820092 purified Bone Gla Protein (BGP) resulted in stabilization of hypoxia-inducible factor 1alpha (HIF-1alpha) in chondrocytes and vascular smooth muscle cells PMID: 21757657 The mechanism of high glucose induced calcification in vascular smooth muscle cells may be due to the increased expression of cbfalpha-1 and OC. PMID: 21302441 functional link between vitamin D-dependent bone tissue-specific transcription and histone acetylation at osteocalcin locus PMID: 11893738 the VDRE in the distal region of the OC gene promoter is refractory to binding of the VDR-RXR complex when organized in a nucleosomal context PMID: 11964167 deltaEF1 suppresses expression of the endogenous osteocalcin gene PMID: 12193549 acetylation of histones H3 and H4 is functionally coupled to the chromatin remodeling events that mediate the developmental induction of osteocalcin gene transcription in bone cells PMID: 12554783 Type I collagen promotes the activity of dentin formation by dental pulp cells by down-regulating Dmp-1 gene expression and up-regulating osteocalcin gene expression. PMID: 12647294 A human vitamin D receptor-glucocorticoid receptor DNA-binding domain chimera is functional on rat osteocalcin vitamin D-responsive element with only conservative change of lys-49 to arg, and of negatively charged glu-53 to basic amino acid (lys or arg). PMID: 12960019 Data show that in osteoblastic cells, the vitamin D receptor interacts directly with Runx2, and that this interaction contributes significantly to vitamin D3-dependent enhancement of the osteocalcin promoter. PMID: 15456860 Results describe gene regulation by Dlx3 in relation to that of Msx2 and Dlx5 during osteoblast differentiation. PMID: 15456894 Ocn is a Nurr1 target gene, which positions Nurr1 in the core of transcriptional factors regulating osteoblastic gene expression PMID: 15485875 OC-IR nerve fibers in the circumvallate papilla mainly originated from the petrosal ganglion. PMID: 15621021 Osteonectin (ON) and osteocalcin (OC) was used as osteoblast markersand assessed using an indirect immunoperoxidase. technique. PMID: 16443258 CEBP-beta-dependent recruitment of SWI/SNF activity is required for chromatin remodeling and transcriptional activity of the bone-specific osteocalcin gene PMID: 16772287 specific protein-DNA and protein-protein interactions that occur within the context of the OC gene promoter in osteoblastic cells stabilize the preferential association of the VDR-SRC-1 complex PMID: 17218095 These results support a model where VDR preferentially recruits SRC-1 to enhance bone-specific OC gene transcription. PMID: 17786964 These data suggest that long-term reduction in bone OC levels may induce the formation of immature bone, which is easily resorbed with changes in bone metabolism such as ovariectomy, and that OC may be one of the factors affecting bone turnover. PMID: 17968486 TFIIA gamma together with ATF4 and Runx2 stimulates osteocalcin promoter activity and endogenous mRNA expression. PMID: 18171674 Biomineralization followed secretion of osteocalcin, which may reflect early osteoblastic differentiation of cultured mesenchymal stem cells under osteoinductive conditions. PMID: 19191495 The Notch-responsive Hes-1 protein is capable of repressing osteocalcin gene transcription in osteoblastic cells through an E-box in the proximal promoter. PMID: 19670267

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.