Recombinant Human PSMB9 Protein

Beta LifeScience SKU/CAT #: BL-1652PS

Recombinant Human PSMB9 Protein

Beta LifeScience SKU/CAT #: BL-1652PS
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Tag N/A
Host Species Human
Synonym Proteasome subunit beta type-9, Low molecular mass protein 2, Macropain chain 7, Multicatalytic endopeptidase complex chain 7, Proteasome chain 7, Proteasome subunit beta-1i, Really interesting new gene 12 protein, PSMB9, LMP2, PSMB6i, RING12, beta1i, MGC70470.
Background Proteasome subunit beta type-9 (PSMB9) belongs to the proteasome B-type family which is a 20S core beta subunit. PSMB9 is positioned in the class II region of the MHC (major histocompatibility complex). Expression of the PSMB9 protein is induced byINFGand this gene product replaces catalytic subunit 1 (proteasome beta 6 subunit) in the immunoproteasome.
Description PSMB9 expressed in E.Coli is a single, non-glycosylated polypeptide chain containing 220a.a. (21-219 a.a.) and having a molecular weight of 23.5kDa.PSMB9 is fused to a 21a.a. His-tag at N-terminus and purified by unique purification methods.
Source E.coli
AA Sequence MGSSHHHHHH SSGLVPRGSH MTTIMAVEFD GGVVMGSDSR VSAGEAVVNR VFDKLSPLHE RIYCALSGS AADAQAVADMA AYQLELHGIE LEEPPLVLAA ANVVRNISYK YREDLSAHLM VAGWDQREGG QVYGTLGGML TRQPFAIGGS GSTFIYGYVD AAYKPGMSPE ECRRFTTDAI ALAMSRDGSS GGVIYLVTIT AAGVDHRVIL GNELPKFYDE.
Purity >90.0% as determined by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Formulation PSMB9 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 50mM NaCl.
Stability Recombinant protein is stable for 12 months at -70°C
Usage For Research Use Only
Storage Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple 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.

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