Osteocalcin Antibodies

Osteocalcin (BGLAP)

Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.

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Gene Information

Human
Gene Name:	BGLAP
Uniprot:	P02818
Entrez:	632

Family

Belongs to:
osteocalcin/matrix Gla protein family

Alternative Names

BGLAP; BGP; bone gamma-carboxyglutamate (gla) protein (osteocalcin); bone gamma-carboxyglutamate (gla) protein; Bone Gla protein; Gamma-carboxyglutamic acid-containing protein; OC; OCN; Osteocalcin

Molecular Weight

Mass (kDA):
10.963 kDA

Genomic Context

Human
Location:	1q22
Sequence:	1; NC_000001.11 (156242184..156243317)

Subcellular Localizations

Secreted.

Diseases

• Fracture
• Osteoporosis
• Diabetes Mellitus
• Malignant Neoplasms
• Headache
• Diabetes Mellitus, Non-insulin-dependent
• Growth Arrest
• Insulin Resistance
• Osteopenia
• Acute Lymphocytic Leukemia
• Insulin Sensitivity
• Leukemia

• Autoimmunity
• Malnutrition
• Maple Syrup Urine Disease
• Hypoxia
• Diabetic Neuropathies
• Neoplasm Invasiveness
• Dental Fluorosis, Acquired

Pathways

• Osteoblast Differentiation
• Bone Resorption
• Cell Proliferation
• Regeneration
• Bone Development
• Ossification
• Chondrocyte Differentiation
• Cell Differentiation
• Senescence
• Methylation
• Secretion
• Transport
• Osteoclast Differentiation

• Gene Silencing
• Stem Cell Differentiation
• Cellular Senescence
• Dna Demethylation
• Cell Fate Determination
• Virulence
• Mesenchymal Cell Differentiation

PTMs

• Methylation

• Demethylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/BGLAP

Best Uses Of The BGLAP Marker By Boster Bio

If you want to determine the BGLAP protein expression in cancer cells it is possible to use antibodies that specifically target the protein produced by Boster Bio. Boster's antibodies have been validated using both positive and negative samples to ensure high specificity and high affinity. Boster offers product credits to reward early reviewers. This program is open for all scientists from around the world.

Antibody Picoband(tm)

The BGLAP Marker is a cis-acting molecule found on the promoter of osteoblast-specific genes. The expression of the BGLAP gene is tightly controlled by a transcriptional factor known as runx2. Runx2 and factors downstream of it are overexpressed during pancreatic cancer. These factors could be the reason for the increased growth of pancreatic cancerous cells. Runx2 is a significant factor with a decreased expression of bone sialoprotein in pancreatic cancer cells, as well as a less expression of the protein in pancreatic cancer cells.

A study that was conducted on human pancreatic cancer cell lines proved that BGLAP is expressed only in the acinar cells. The immunocytochemistry study confirmed the localization of BGLAP in pancreatic cancer cells through staining a specific antibody against the protein. Negative control was performed with normal mouse IgG. The results are summarized in Table 1 and in the Supplementary Materials.

Medical research has many applications for the BGLAP marker. It has been implicated with various malign tumors. It is a biochemical indicator of bone regeneration in multiple myeloma and the levels in serum of BGLAP are decreased in patients suffering from osteolytic bone lesions. BGLAP has been shown to be linked with bone complications, disease progression, and tumor growth. BGLAP has also been shown to be expressed in prostate cancer cells which can improve adhesion, proliferation, as well as survival of cancer cells.

Down-regulation of BGLAP levels has also been shown to inhibit pancreatic cancer cells invasion and growth. Other indications of BGLAP inhibition include osteosarcoma, prostate cancer and breast cancer. Similar to many cancer-related proteins, BGLAP silencing is highly efficient. It is crucial to have a positive effect on tumor cells. This is a good way to determine the effectiveness of BGLAP-targeting drugs.

Immunocytochemistry

The BGLAP marker is a monoclonal antibody that was created to detect pancreatic cancer cells. Numerous studies have proven that BGLAP staining detects 15/20 pancreatic cancer cell lines. As an unintended control, Control IgG was used. These results are in support of the use of BGLAP for immunocytochemistry research. We also discuss the application of BGLAP immunohistochemistry in the study of pancreatic cancer.

The BGLAP mRNA level BGLAP is not significantly different from that of normal pancreatic tissues. However, BGLAP expression is increased in malignant tissues, such as osteosarcoma or prostate cancer. BGLAP expression is associated with skeletal complications, disease progression and growth of tumors. BGLAP expression is also found in pancreatic cancer cells which enhances adhesion and proliferation and survival.

After the antigens were identified tissues were removed and deparaffinized. Then it was added ethanol to rehydrate the tissues. A microwave oven was used to deparaffinize the tissue sections. The tissues were then boiled in 10 mM citrate buffer to remove the antigens. After quenching the endogenous peroxidase activity the slides were rinsed three times with washing buffer. The slides were then incubated with a monoclonal antibody to BGLAP, diluted in universal blocking reagent. The antibodies were then counterstained with Mayer's Hematoxylin.

This antibody is used to detect BGLAP protein in cells. For 20 minutes, the primary antibody was Wnt-11 (1.100, Invitrogen Carlsbad, CA USA). Horseradish peroxidase labeled streptomyces roundbumin was the secondary antibody. The immunohistochemistry was conducted using this antibody.

In pancreatic cancer cells, down-regulations of BGLAP led to significant growth and invasion decreases. Similar results have been observed in osteosarcoma cells. Boster Bio's BGLAP antibody immunocytochemistry is a unique immunoassay to BGLAP. But, this antibody is still in its infancy. Researchers hope to validate their findings by conducting clinical trials.

Two independent studies using WJ-MSC were conducted to evaluate the efficacy of this antibody. The cells were stained using mouse anti-human antibody conjugated to fluorophores, phycoerythrin, and PerCP-Cy(tm). The samples were examined using the BD Stemflow hMSC immunocytochemistry analysis kit. The results were consistent, reproducible.

Immunofluorescence

The company's BGLAP marker for immunofluoroscopy was created in response to various clinical studies. One study revealed that the antibody could detect osteoblast-induced cells. The antibodies were used to label cells, and another antibody (IgG) was added to the sample. Santa Cruz Biotechnology, Sigma St. Louis, Abcam and Abcam sold the primary antibodies that have a binding affinity to BGLAP. The secondary antibodies, that have HRP labeling, were obtained from Wuhan Boster Biological Technology Co., Ltd.

Enzyme immunoassay

There are many advantages to using a Boster Bio enzyme immunoassay. For one, it's an simple to use and efficient method of detecting proteins in tissues and cells. IHC utilizes a procedure in which antibodies connect to the protein target. Secondary antibodies identify protein localization, and produce crisp staining of tissue structures. Nearly every immunoassay procedure begins with sample preparation. Nearly every type of sample requires special treatment.

The ELISA kit contains all of the reagents you need to conduct the test. It utilizes a plate-based method to detect molecules in samples. To measure the results enzymes are linked to antibodies. Different types of ELISA have different antigen-antibody interactions. Boster's ELISA kit has high affinity antibodies against native proteins. Each of these ELISA kits has been validated against a range of immunogenic proteins and superfamilies.

A carboxylic feature added to NVP derivatives made from synthetics connects NVP with KLH and AChE. EIA showed very good antibody titers following the second booster injection. The tracer NVP-AChE was used to improve the antiserum. It is available for horseradish phosphatase as well as alkaline phosphatase and human serum albumin. The LOD of the enzyme immunoassay was approximately 100 pg 1 (7 fmol/well).

The method could be further developed by modifying the original ELISA method to detect colistin. The development of the enzyme immunoassay enables accurate detection of colistin in actual samples. Optimizing the components of the extraction solution for samples has increased the detection limit of this test. The new method has a quick detection time of only 15 minutes. The high accuracy allows researchers to identify colistin on a cell level in real-time.