FKBP12 Antibody
Rabbit mAb
- 产品详情
- 实验流程
Application ![]()
| WB, IF, ICC |
---|---|
Primary Accession | P62942 |
Reactivity | Rat, Human, Mouse |
Clonality | Monoclonal |
Other Names | FKBP 12; FKBP 1A; FKBP1; FKBP12 Exip3; FKBP12C; fkbp1a; Immunophilin FKBP12; PKC12; PPIase FKBP1A; Rotamase; |
Isotype | Rabbit IgG |
Host | Rabbit |
Calculated MW | 11951 Da |
Dilution | WB 1:1000~1:5000 ICC/IF 1:50~1:200 |
---|---|
Purification | Affinity-chromatography |
Immunogen | A synthesized peptide derived from human FKBP12 |
Description | May play a role in modulation of ryanodine receptor isoform-1 (RYR-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. There are four molecules of FKBP12 per skeletal muscle RYR. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
Storage Condition and Buffer | Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle. |
Name | FKBP1A |
---|---|
Synonyms | FKBP1, FKBP12 |
Function | Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
Cellular Location | Cytoplasm, cytosol. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P62943}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62943}; Cytoplasmic side {ECO:0000250|UniProtKB:P62943} |
Research Areas
For Research Use Only. Not For Use In Diagnostic Procedures.
Application Protocols
Provided below are standard protocols that you may find useful for product applications.

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