Cyclophilin B Antibody (YA7601)
(Synonyms: CYPB, PPIB, Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP)Cyclophilin B Antibody (YA7601) is a Rabbit-derived and non-conjugated IgG, Kappa monoclonal antibody, targeting to Cyclophilin B.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF, ELISA
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH7.4) containing 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|---|
| Dilution Ratio | 1:200-1:1000 | 1:2000-1:10000 | 1:200-1:1000 | 1:5000-1:20000 |
Product Details
Cyclophilin B Antibody (YA7601) is a Rabbit-derived and non-conjugated IgG, Kappa monoclonal antibody, targeting to Cyclophilin B.
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Host Rabbit
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Clonality Monoclonal,Recombinant
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 20 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 24 kDa
The exact sequence is proprietary to MCE.
Endogenous
Protein A affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH7.4) containing 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Cyclophilin B (CyPB), encoded by PPIB, is an endoplasmic reticulum (ER) -resident peptidyl-prolyl cis-trans isomerase that catalyzes proline isomerization and supports protein folding within the secretory pathway[1][2]. Mechanistically, CyPB functions as a major folding catalyst for type I collagen by accelerating the rate-limiting cis-trans conversion of proline residues required for triple-helix formation[3][4][5]. CyPB also operates within the P3H1/CRTAP/PPIB complex, which is essential for procollagen folding and prolyl 3-hydroxylation in the ER, linking its enzymatic activity to collagen biosynthesis and extracellular matrix assembly[6][7]. In disease models, PPIB deficiency disrupts collagen post-translational modification, delays procollagen folding, alters collagen cross-linking, and causes recessive osteogenesis imperfecta with defective connective tissue formation[8][9][10][2]. Compared with other rough ER-resident peptidyl-prolyl isomerases, CyPB has a particularly prominent role in collagen maturation because collagen molecules contain abundant proline residues that require efficient isomerization during biosynthesis[5][11]. Structural and biochemical studies further demonstrate that CyPB interacts with calnexin-associated folding machinery and collagen-processing complexes, highlighting its specialized ER chaperone function rather than a generalized folding role[2][6]. For experimental applications, cyclosporin A binds the active site of CyPB and inhibits its isomerase activity, providing a widely used pharmacological tool for investigating collagen folding, ER protein maturation, and connective tissue biology[2][4].
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Subcellular Localization
Virion,Endoplasmic reticulum lumen,Melanosome
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Isoforms & Post-Translational Modification
P23284: 216 amino acids, molecular weight 23743 Da.
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Subunit
Interacts with DYM
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SwissProt ID
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Synonyms
CYPB, PPIB, Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP
Documentation
References
[1]. Cyclophilin B gene information from NCBI.
[2]. Lee MJ, et al. Time to HIV rebound after infusion of long-acting broadly neutralising antibodies 3BNC117-LS and 10-1074-LS and analytical treatment interruption (the RIO trial): a double-blind, randomised, placebo-controlled trial. Lancet HIV. 2026 May 27:S2352-3018(26)00059-7. [Content Brief]
[3]. Li W, et al. The structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex. Nat Commun. 2024 Sep 8;15(1):7844. [Content Brief]
[4]. Ishikawa Y, et al. Ziploc-ing the structure: Triple helix formation is coordinated by rough endoplasmic reticulum resident PPIases. Biochim Biophys Acta. 2015 Oct;1850(10):1983-93. [Content Brief]
[5]. Cabral WA, et al. Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta. PLoS Genet. 2014 Jun 26;10(6):e1004465. [Content Brief]
[6]. Wu J, et al. Characterization of PPIB interaction in the P3H1 ternary complex and implications for its pathological mutations. Cell Mol Life Sci. 2019 Oct;76(19):3899-3914. [Content Brief]
[7]. Kiros M, et al. Trends in HIV-1 pretreatment drug resistance and HIV-1 variant dynamics among antiretroviral therapy-naive Ethiopians from 2003 to 2018: a pooled sequence analysis. Virol J. 2023 Oct 25;20(1):243. [Content Brief]
[8]. Okada Y, et al. Genome-wide association study for C-reactive protein levels identified pleiotropic associations in the IL6 locus. Hum Mol Genet. 2011 Mar 15;20(6):1224-31. [Content Brief]
[9]. Barnes AM, et al. Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding. N Engl J Med. 2010 Feb 11;362(6):521-8. [Content Brief]
[10]. Rabezanahary H, et al. Live virus neutralizing antibodies against pre and post Omicron strains in food and retail workers in Québec, Canada. Heliyon. 2024 May 21;10(10):e31026. [Content Brief]
[11]. Koag MC, et al. Structural basis for the inefficient nucleotide incorporation opposite cisplatin-DNA lesion by human DNA polymerase β. J Biol Chem. 2014 Nov 7;289(45):31341-8. [Content Brief]
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