Recombinant human PPIH protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
M A V A N S S P V N P V V F F D V S I G G Q E V G R M K I E L F A D V V P K T A E N F R Q F C T G E F R K D G V P I G Y K G S T F H R V I K D F M I Q G G D F V N G D G T G V A S I Y R G P F A D E N F K L R H S A P G L L S M A N S G P S T N G C Q F F I T C S K C D W L D G K H V V F G K I I D G L L V M R K I E N V P T G P N N K P K L P V V I S Q C G E M
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone.
CYP20, CYPH, PPIH, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, Small nuclear ribonucleoprotein particle-specific cyclophilin H, U-snRNP-associated cyclophilin SnuCyp-20, CypH, USA-CYP
Recombinant human PPIH protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
pH: 7.4
Constituents: PBS, 10% Glycerol (glycerin, glycerine)
ab78874 is purified using conventional chromatography techniques.
PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone.
Belongs to the cyclophilin-type PPIase family. PPIase H subfamily.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
The peptidyl-prolyl cis-trans isomerase H (PPIH) also known as cyclophilin H is involved in protein folding and assembly. PPIH has a molecular weight of approximately 18 kDa. This protein expresses widely in human tissues with a notable presence in the nucleus. As an isomerase PPIH accelerates the cis-trans isomerization of prolyl bonds an important step in protein folding influencing protein conformation and function.
PPIH plays a significant role in pre-mRNA splicing. It acts as a component of the spliceosome a critical molecular machinery for removing introns from pre-mRNA. Through its action within the spliceosome PPIH helps regulate the maturation of mRNA and by extension protein synthesis. Its interactions ensure the stability and functional configuration of the spliceosomal complex.
PPIH participates in mRNA processing and splicing pathways. It engages in the spliceosomal pathway aligning closely with proteins like SMN1 and the rest of the spliceosome complex which are involved in RNA processing and gene expression regulation. The interplay of PPIH in these pathways highlights its essential role in gene expression and cellular growth functions.
Research connects PPIH with certain neurodegenerative disorders and cancer. Abnormalities in PPIH function or expression might influence diseases like spinal muscular atrophy due to its relationship with SMN1. Additionally dysregulation of PPIH-connected pathways could contribute to oncogenesis supporting its significance in cancer research. Scientists continue exploring PPIH to develop targeted therapies for these conditions.
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15% SDS-PAGE showing ab78874 at approximately 19kDa (3μg).
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