Recombinant Mouse SERPINB10 Protein (His Tag)

Name: Recombinant Mouse SERPINB10 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4216
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Mouse
Accession	Q8K1K6
Synonym	9830131G07, BB233602, Serpinb10-ps
Background	Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have been identified. Mouse SerpinB1, also known as Peptidase inhibitor 1, PI-1, Bomapin and SERPINB1, is a nucleus and cytoplasm protein which belongs to theserpin family and Ov-serpin subfamily. SerpinB1 is expressed specifically in the bone marrow. SerpinB1 is a protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. SerpinB1 is a redox-sensitive nuclear serpin that augments proliferation or apoptosis of leukaemia cells, depending on growth factors availability. SerpinB1 may regulate protease activities in the cytoplasm and in the nucleus.
Description	A DNA sequence encoding the mouse SERPINB10 (Q8K1K6-1) (Met 1-Pro 397) was expressed, with a C-terminal His tag.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Met 1-Pro 397
Molecular Weight	The recombinant mouse SERPINB10 consists of 408 a.a. and has a calculated molecular mass of 46.5 kDa. It migrates as an approximately 44 kDa band in SDS-PAGE under reducing conditions.
Purity	>94% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0.
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.