Bisphosphoglycerate Mutase (BPGM) is a member of the Phosphoglycerate Mutase family and BPG-Dependent PGAM subfamily. BPGM is a multifunctional enzyme. BPGM catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. It also has phosphoglycerate phosphomutase activity. BPGM plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Deficiency of BPGM increases the affinity of cells for oxygen and result in hemolytic anemia.
BPHL is a member of the serine protease family. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol. It catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. BPHL also activates valacyclovir to acyclovir. It may play a role in detoxification processes.
Bactericidal permeability-increasing protein(BPI for short), is a secreted protein which belongs to the BPI/LBP/Plunc superfamily, BPI/LBP family. It exists as a monomer or a disulfide-linked homodimer. The cytotoxic action of BPI is limited to many species of Gram-negative bacteria. This specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. BPI has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, and this activity is inhibited by LPS from P.aeruginosa.
BPIFB1, also known as LPLUNC1, belongs to the BPI/LBP/Plunc superfamily, plunc family. BPIFB1 may be involved in the innate immune response to bacterial exposure in the mouth, nasal cavities, and lungs. BPIFB1 is expressed in the upper respiratory tract and oral cavity, which may function in host defence. The expression of BPIF proteins is associated with CF lung disease in humans and mice. It is unclear if this elevation of protein production, which results from phenotypic alteration of the cells within the diseased epithelium, plays a role in the pathogenesis of the disease. BPIFB1 is an abundant, secreted product of goblet cells and minor mucosal glands of the respiratory tract and oral cavity and suggest that the protein functions in the complex milieu that protects the mucosal surfaces in these locations.
Brain-type Natriuretic Peptide (BNP) is a nonglycosylated peptide that is produced predominantly by ventricular myocytes and belongs to the natriuretic peptide family. Proteolytic cleavage of the 12 kDa BNP precursor gives rise to N-terminal Pro BNP (NT-proBNP) and mature BNP. N-terminal proB-type natriuretic peptide (NT-proBNP); a useful marker of heart failure (HF); is considered to be secreted mainly from the ventricle; increased serum NT-proBNP levels are also encountered in conditions such as atrial fibrillation (AF) and atrial septal defect in patients without HF.
RCA1,also named as RNF53,plays a central role in DNA repair by facilitating cellular response to DNA repair. It is required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair,ubiquitination and transcriptional regulation to maintain genomic stability. BRCA1 acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. It is involved in transcriptional regulation of P21 in response to DNA damage. BRCA1 is required for FANCD2 targeting to sites of DNA damage. It may function as a transcriptional regulator. BRCA1 inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. The antibody is specific to BRCA1. BRCA1 appears to produce multiple splice variants. BRCA1 is a nuclear protein with a molecular mass of 220 kDa. The present study describes the isolation and expression of two cDNAs of BRCA1,including a splice variant designated BRCA1D672-4095. BRCA1D672-4095 is generated by exclusion of exon 11 by in-frame splicing and produces a 97 kDa protein. In contrast to BRCA1,BRCA1D672-4095 localizes to the cytoplasm.
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