catalog number :
MBS142454
products type :
Recombinant Protein
products full name :
Recombinant Human Cyclophilin-B
products short name :
Cyclophilin-B
products name syn :
Cyclophilin B Human; Cyclophilin-B Human Recombinant; Peptidylprolyl isomerase B; PPIase; Rotamase; S-cyclophilin; PPIB; cyclophilin-like protein; peptidyl-prolyl cis-trans isomerase B; Cyclophilin B; SCYLP; CYPB; CYP-S1; MGC2224; MGC14109; Cyclophilin B
other names :
peptidyl-prolyl cis-trans isomerase B; Peptidyl-prolyl cis-trans isomerase B; peptidyl-prolyl cis-trans isomerase B; PPIase B; S-cyclophilin; cyclophilin-like protein; epididymis secretory protein Li 39; rotamase B; peptidylprolyl isomerase B (cyclophilin B); CYP-S1; Cyclophilin B; Rotamase B; S-cyclophilin; SCYLP
other gene names :
PPIB; PPIB; OI9; CYPB; SCYLP; CYP-S1; HEL-S-39; CYPB; PPIase B; SCYLP
uniprot entry name :
PPIB_HUMAN
sequence :
MLLPGPSAAD EKKKGPKVTV KVYFDLRIGD EDVGRVIFGL FGKTVPKTVD NFVALATGEKGFGYKNSKFH RVIKDFMIQG GDFTRGDGTG GKSIYGERFP DENFKLKHYG PGWVSMANAGKDTNGSQFFI TTVKTAWLDG KHVVFGKVLE GMEVVRKVES TKTDSRDKPL KDVIIADCGK IEVEKPFAIA KE.
purity :
Greater than 95.0% as determined by SDS-PAGE.
form :
1 mg/ml solution containing 20mM Tris-HCl 8.0, 20mM NaCl, 0.5mM DTT and 10% glycerol. Sterile filtered colorless solution.
other info2 :
Biological Activity: Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.
products categories :
ENZYMES; Enzymes; Cyclophilin
products description :
Description: Cyclophilin-B Human Recombinant produced in E Coli is a single, non-glycosylated,polypeptide chain containing 192 amino acids (26-216) and having a molecular mass of 21.2 kDa. PPIB is purified by proprietary chromatographic techniques. Introduction: Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.
ncbi acc num :
NP_000933.1
ncbi gb acc num :
NM_000942.4
ncbi mol weight :
23,743 Da
ncbi pathways :
Collagen Biosynthesis And Modifying Enzymes Pathway (645289); Collagen Formation Pathway (645288); Extracellular Matrix Organization Pathway (576262); Prolactin Signaling Pathway (672462); Syndecan-1-mediated Signaling Events Pathway (138046)
ncbi summary :
The protein encoded by this gene is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression. Variants have been identified in this protein that give rise to recessive forms of osteogenesis imperfecta. [provided by RefSeq, Oct 2009]
uniprot summary :
PPIB: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Defects in PPIB are the cause of osteogenesis imperfecta type 9 (OI9). OI9 is a connective tissue disorder characterized by bone fragility, low bone mass and bowing of limbs due to multiple fractures. Short limb dwarfism and blue sclerae are observed in some but not all patients. Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. Protein type: RNA-binding; Secreted; Secreted, signal peptide; EC 5.2.1.8; Cyclophilin; Chaperone; Isomerase. Chromosomal Location of Human Ortholog: 15q21-q22. Cellular Component: focal adhesion; smooth endoplasmic reticulum; membrane; endoplasmic reticulum; perinuclear region of cytoplasm; endoplasmic reticulum lumen; melanosome; nucleus. Molecular Function: collagen binding; protein binding; peptidyl-prolyl cis-trans isomerase activity; unfolded protein binding; protein complex binding; peptide binding. Biological Process: extracellular matrix organization and biogenesis; protein peptidyl-prolyl isomerization; protein stabilization; positive regulation of multicellular organism growth. Disease: Osteogenesis Imperfecta, Type Ix