Cyclophilin B Antibody (Rabbit mAb) [F10F4]

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 - 1:10000

Application
WB

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
24 kDa 18 kDa, 24 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Cyclophilin B Antibody (Rabbit mAb) [F10F4] detects endogenous levels of total Cyclophilin B protein.

Clone
F10F4

Synonym(s)
CYPB, PPIB, Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP

Background
Cyclophilin B is a secretory pathway peptidyl‑prolyl cis‑trans isomerase of the cyclophilin family that functions as a molecular chaperone in the endoplasmic reticulum and participates in extracellular signaling after secretion. The protein carries an N‑terminal signal sequence that directs co‑translational translocation into the endoplasmic reticulum lumen, where it accumulates and assists protein folding by catalyzing cis‑trans isomerization of proline imidic peptide bonds in nascent and resident polypeptides, with cyclosporin A binding altering its trafficking through the secretory pathway. ER‑localized cyclophilin B shows a distribution between the endoplasmic reticulum and later secretory compartments, and cyclosporin A association leads to retention changes that affect its movement toward the Golgi and extracellular space, indicating that drug interaction modulates access of cyclophilin B to client proteins and secreted cargo. The secreted fraction engages cell surface receptors and matrix components; cyclophilin B acts as a ligand for the CD147 receptor and interacts with heparan sulfate proteoglycans on T lymphocytes, granulocytes and macrophages, which enables chemotaxis, adhesion of T cells to fibronectin and regulation of downstream events such as mitogen‑activated protein kinase activation, calcium transport and expression of the pro‑apoptotic protein Bim. This combination of ER chaperone activity and extracellular receptor binding places cyclophilin B in pathways that connect protein folding homeostasis with inflammatory signaling and cell migration, and its secretion in response to inflammatory stimuli and oxidative stress contributes to tissue or systemic inflammation without directly inducing pro‑inflammatory cytokine production on its own. Structural features include the conserved cyclophilin PPIase domain that provides the active site for proline isomerization, together with regions that support interaction with CD147 and heparan sulfate proteoglycans at the cell surface, allowing the same polypeptide to operate in folding and signaling environments. In adipogenesis and bone cell biology, cyclophilin B has been described as a molecular chaperone that promotes differentiation through modulation of signaling cascades such as AKT/mTOR or JAK2/STAT3, linking its PPIase activity and receptor interactions to transcriptional control of lineage‑specific genes in preadipocytes and osteoblast‑like cells. Serum and tissue levels of cyclophilin B increase under inflammatory and metabolic stress, including metabolic syndrome, where constitutive secretion correlates with prevalence and severity and supports a role in metabolic inflammation through its participation in cell–cell communication and leukocyte trafficking rather than direct cytokine induction. In viral infection, cyclophilin B functions as a host factor for hepatitis C virus replication by binding the viral RNA polymerase NS5B, stimulating its RNA binding activity and supporting efficient genome replication, and RNA interference‑mediated reduction of cyclophilin B or disruption of NS5B–cyclophilin B interaction lowers replication efficiency, establishing this PPIase as a regulator within the HCV replication machinery. Cyclophilin B expression is increased in several tumor types and inflammatory diseases such as rheumatoid arthritis and psoriasis, and its extracellular activity through CD147 and heparan sulfate proteoglycans contributes to chemotaxis, adhesion and signaling changes in immune cells, situating it at a junction of protein folding quality control, viral replication, metabolic and inflammatory signaling, and tumor progression that is accessible both to genetic manipulation and pharmacologic inhibition targeting cyclophilin–ligand interactions.

Background

Cyclophilin B is a secretory pathway peptidyl‑prolyl cis‑trans isomerase of the cyclophilin family that functions as a molecular chaperone in the endoplasmic reticulum and participates in extracellular signaling after secretion. The protein carries an N‑terminal signal sequence that directs co‑translational translocation into the endoplasmic reticulum lumen, where it accumulates and assists protein folding by catalyzing cis‑trans isomerization of proline imidic peptide bonds in nascent and resident polypeptides, with cyclosporin A binding altering its trafficking through the secretory pathway. ER‑localized cyclophilin B shows a distribution between the endoplasmic reticulum and later secretory compartments, and cyclosporin A association leads to retention changes that affect its movement toward the Golgi and extracellular space, indicating that drug interaction modulates access of cyclophilin B to client proteins and secreted cargo. The secreted fraction engages cell surface receptors and matrix components; cyclophilin B acts as a ligand for the CD147 receptor and interacts with heparan sulfate proteoglycans on T lymphocytes, granulocytes and macrophages, which enables chemotaxis, adhesion of T cells to fibronectin and regulation of downstream events such as mitogen‑activated protein kinase activation, calcium transport and expression of the pro‑apoptotic protein Bim. This combination of ER chaperone activity and extracellular receptor binding places cyclophilin B in pathways that connect protein folding homeostasis with inflammatory signaling and cell migration, and its secretion in response to inflammatory stimuli and oxidative stress contributes to tissue or systemic inflammation without directly inducing pro‑inflammatory cytokine production on its own. Structural features include the conserved cyclophilin PPIase domain that provides the active site for proline isomerization, together with regions that support interaction with CD147 and heparan sulfate proteoglycans at the cell surface, allowing the same polypeptide to operate in folding and signaling environments. In adipogenesis and bone cell biology, cyclophilin B has been described as a molecular chaperone that promotes differentiation through modulation of signaling cascades such as AKT/mTOR or JAK2/STAT3, linking its PPIase activity and receptor interactions to transcriptional control of lineage‑specific genes in preadipocytes and osteoblast‑like cells. Serum and tissue levels of cyclophilin B increase under inflammatory and metabolic stress, including metabolic syndrome, where constitutive secretion correlates with prevalence and severity and supports a role in metabolic inflammation through its participation in cell–cell communication and leukocyte trafficking rather than direct cytokine induction. In viral infection, cyclophilin B functions as a host factor for hepatitis C virus replication by binding the viral RNA polymerase NS5B, stimulating its RNA binding activity and supporting efficient genome replication, and RNA interference‑mediated reduction of cyclophilin B or disruption of NS5B–cyclophilin B interaction lowers replication efficiency, establishing this PPIase as a regulator within the HCV replication machinery. Cyclophilin B expression is increased in several tumor types and inflammatory diseases such as rheumatoid arthritis and psoriasis, and its extracellular activity through CD147 and heparan sulfate proteoglycans contributes to chemotaxis, adhesion and signaling changes in immune cells, situating it at a junction of protein folding quality control, viral replication, metabolic and inflammatory signaling, and tumor progression that is accessible both to genetic manipulation and pharmacologic inhibition targeting cyclophilin–ligand interactions.

References
https://pubmed.ncbi.nlm.nih.gov/7909608/ https://pubmed.ncbi.nlm.nih.gov/15989969/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%