Recombinant Rat F11 protein, His & GST-tagged
Cat.No. : | F11-1862R |
Product Overview : | Recombinant Rat F11 aa. (Ile275~Gly516) fused with N-terminal His & GST tag was produced in E. coli cells. |
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Source : | E. coli |
Species : | Rat |
Tag : | His & GST |
Form : | Freeze-dried powder |
Molecular Mass : | 57kDa as determined by SDS-PAGE reducing conditions. |
Protein length : | Ile275~Gly516 |
Endotoxin : | <1.0EU per 1ug (determined by the LAL method) |
Purity : | >98% |
Characteristic : | The isoelectric point is 6.5. |
Applications : | SDS-PAGE; WB; ELISA; IP; CoIP; Purification; Amine Reactive Labeling. |
Stability : | The thermal stability is described by the loss rate of the target protein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. (Referring from China Biological Products Standard, which was calculated by the Arrhenius equation.) The loss of this protein is less than 5% within the expiration date under appropriate storage condition. |
Storage : | Avoid repeated freeze/thaw cycles. Store at 2-8°C for one month. Aliquot and store at -80°C for 12 months. |
Concentration : | 200μg/mL |
Storage Buffer : | 20mM Tris, 150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT, 0.01% sarcosyl, 5% Trehalose and Proclin300. |
Reconstitution : | Reconstitute in 20mM Tris, 150mM NaCl (pH8.0) to a concentration of 0.1-1.0mg/mL. Do not vortex. |
Gene Name : | F11 coagulation factor XI [ Rattus norvegicus (Norway rat) ] |
Official Symbol : | F11 |
Synonyms : | CYP1A1; cytochrome P450 family 1 subfamily A member 1; AHH; AHRR; CP11; CYP1; CYPIA1; P1-450; P450-C; P450DX; cytochrome P450 1A1; aryl hydrocarbon hydroxylase; cytochrome P1-450, dioxin-inducible; cytochrome P450 form 6; cytochrome P450, family 1, subfamily A, polypeptide 1; cytochrome P450, subfamily I (aromatic compound-inducible), polypeptide 1; cytochrome P450-C; cytochrome P450-P1; flavoprotein-linked monooxygenase; xenobiotic monooxygenase |
Gene ID : | 290757 |
mRNA Refseq : | NM_001047848.1 |
Protein Refseq : | NP_001041313.1 |
UniProt ID : | Q6TUF8 |
Products Types
◆ Recombinant Protein | ||
F11-900M | Recombinant Mouse F11 Protein, His-tagged | +Inquiry |
F11-957H | Recombinant Human F11 Protein, MYC/DDK-tagged | +Inquiry |
F11-2914M | Recombinant Mouse F11 Protein, His (Fc)-Avi-tagged | +Inquiry |
F11-439M | Recombinant Mouse F11 Protein, MYC/DDK-tagged | +Inquiry |
F11-2004H | Recombinant Human F11 Protein (19-387 aa), His-tagged | +Inquiry |
◆ Native Protein | ||
F11-2466H | Native Human Coagulation Factor XI | +Inquiry |
◆ Lysates | ||
F11-2681HCL | Recombinant Human F11 cell lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (6)
Ask a questionF11 plays an important role in diabetes, and abnormal levels may lead to insulin resistance and lipid metabolism disorders, which can lead to diabetes.
The mutation types of F11 include point mutations, insertions/deletions, duplications, etc., which may cause structural and functional abnormalities of the protein.
Studying the regulatory mechanism of F11 requires the comprehensive use of various experimental methods and techniques, such as gene knockout, transcriptome analysis, protein interaction, etc.
Abnormal F11 levels may indicate some diseases related to lipid metabolism, such as diabetes, obesity, hyperlipidemia, etc.
There are no drugs that directly regulate F11 levels, but they can be affected by lifestyle adjustments such as diet and exercise.
F11 has a complex relationship with other genes or proteins, and can interact with other genes or proteins and participate in a variety of biochemical reactions.
Customer Reviews (3)
Write a reviewThe structure of the recombinant protein was analyzed by nuclear magnetic resonance (NMR), X-ray crystallography or electron microscopy, and the results showed that the protein was stable.
In the process of purification, the removal of impurities is good.
There are no structural or functional defects.
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