Recombinant Mouse gp130 Protein (His & Fc Tag)

Name: Recombinant Mouse gp130 Protein (His & Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-2302
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His&Fc
Host Species	Mouse
Accession	NP_034690.3
Synonym	5133400A03Rik, AA389424, BB405851, CD130, D13Ertd699e, gp130
Background	Glycoprotein 13 (also known as gp13, IL6ST, IL6-beta or CD13) is a transmembrane protein which is the founding member of the class of all cytokine receptors. CD13/gp13 is a signal transducer shared by many cytokines, including interleukin 6 (IL6), ciliary neurotrophic factor (CNTF), leukemia inhibitory factor (LIF), and Oncostatin M (OSM). CD13/gp13 functions as a part of the cytokine receptor complex. The activation of this protein is dependent upon the binding of cytokines to their receptors. CD13/gp13 plays a critical role in regulating myocyte apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been described. A related pseudogene has been identified on chromosome 17. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp13 for initiating signal transmission. CD13/gp13 binds to IL6/IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduces the signal. CD13/gp13 may have a role in embryonic development. The type I OSM receptor is capable of transducing OSM-specific signaling events.
Description	A DNA sequence encoding the mouse gp130 (NP_034690.3) extracellular domain (Met 1-Glu 617) was fused with the C-terminal His-tagged Fc region of human IgG1 at the C-terminus.
Source	CHO Cells
Predicted N Terminal	Glu 19
AA Sequence	Met 1-Glu 617
Molecular Weight	The recombinant mouse gp130/Fc chimera is a disulfide-linked homodimer. The reduced monomer consists of 843 a.a. and has a predicted molecular mass of 94.7 kDa. As a result of glycosylation, the apparent molecular mass of rm gp130/Fc monomer is approximately 120-130 kDa in SDS-PAGE under reducing conditions.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by its ability to inhibit the IL6 Ralpha enhancement of IL6 activity on M1 mouse myeloid leukemia cells. The ED50 for this effect is typically 0.03-0.15 ug/ml in the presence of 10 ng/ml recombinant human IL6sR and 20 ng/ml recombinant human IL6.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.