Code | CSB-MP743558HU |
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Size | $228 |
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A DNA fragment encoding the extracellular domain (1-118aa) of the human SIGIRR was fused with a C-terminal 6xHis-tag and expressed in mammalian cells. The resulting product is the recombinant human single Ig IL-1-related receptor (SIGIRR) protein. The purity of the recombinant human SIGIRR protein was determined to be greater than 95% using SDS-PAGE and SEC-HPLC analyses. This recombinant human SIGIRR protein can be used in immunology-related research, including studies on IL-1 signaling, TLR signaling, and the NF-κB pathway. The SIGIRR protein acts as a negative regulator of immune responses and inflammation, providing a mechanism to fine-tune and balance the immune system. Its function is to inhibit IL-1 signaling, attenuate TLR signaling, and regulate the NF-κB pathway, thereby maintaining immune homeostasis and preventing inflammatory disorders.
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What validations or detections have you performed for this protein SIGIRR?
Normally, we provide molecular weight, electrophoretic results (SDS-PAGE), concentration, purity, etc. For this protein, we have also done HPLC verification. If you have special demand, we can also provide electrophoretic parameters, activity evaluation, sequence identification, tag removal service, endotoxin removal service, WB and MS validations. You can learn more from this link: https://www.cusabio.com/QC_protein.html.
What is the impact of the tag on any potential biological activity of the SIGIRR protein?
Theoretically small tags generally have very small influence on protein activity. However, the specific impact on protein activity can't be concluded (There is no impact on some proteins, small impact on some proteins, and relatively great impact on some proteins).
Can you remove the endotoxin?
Not all endotoxin can be removed. Please contact us in advance if you need to remove endotoxin, which takes 2-3 business days. We could offer endotoxin removal service free of charge using PMB affinity chromatography, use LAL reagent to semi-quantitatively detect the content of endotoxin and guarantee endotoxin level within 0.1 ng/μg (1 EU/μg).
Why is the actual band size different from the predicted one?
a. Post-translational modification. Phosphorylation, glycosylation, etc which increases the size of the protein.
b. Post-translational cleavage. Many proteins are synthesized as pro-proteins, and then cleaved to give the active form.
c. Splice variants. Alternative splicing may create different sized proteins from the same gene.
d. Relative charge. The composition of amino acids have different relative charge which will affect the electrophoretic mobility.
e. Multimers such as dimerization of a protein. This is usually prevented in reducing conditions, although strong interactions can result in the appearance of higher bands.
f. Protein structure such as disulfide bond, protein secondary structure, or protein 3D structure formation.
g. Hydrophobic proteins, such as transmembrane proteins, may have difficulties in migrating into the gel and thus resulting in different multi-banded patterns.
Can this protein be used in ELISA/WB experiments?
ELISA/WB is mainly aimed at protein immunoreactivity. In theory, this protein is applicable to ELISA/WB experiments, but it is necessary to confirm whether your antibody-antigen information matches, including sequence, expression system, etc., mainly to determine whether the sequence information of the protein (antigen) is consistent with the immunogenic sequence information of the antibody.
Is this SIGIRR protein cell-component-free?
The protein expressed in the body, regardless of the system, is expressed by cell, and the cell expression can be divided into intracellular expression and secretory expression.
The E. coli system only has intracellular expression and needs to be broken, so the cell components are relatively more secreted than other systems.
Yeast, Baculovirus, and Mammalian cell systems can be expressed both in the cell and in the secretory expression, and the secreted expression of the protein component remains relatively less intracellular.
In vitro expression means that cell-free, and the E. coli cell extract is also added, so that the cell component remains.
Therefore, no matter which expression system and which way the protein is expressed, there will be residual cell components, but we finally use affinity chromatography to purify. In theory, the residual of the cell components will be very small, but 100% of no residue cannot be guaranteed. (Nor does any company dare to guarantee).
How long can I get the products after I place an order?
We have enough quantity of this protein in stock and can be shipped out in 3-7 business days once passing our Quality Control process. Each of our proteins will undergo a strict QC process before being delivered.