Recombinant Human DCUN1D1 Protein

Name: Recombinant Human DCUN1D1 Protein
Brand: Beta LifeScience
SKU: BL-3050PS
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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	DCN1, defective in cullin neddylation 1-domain containing 1 (S. cerevisiae), RP42, DCUN1L1, SCCRO, SCRO, Tes3, Defective in cullin neddylation protein 1-like protein 1, Squamous cell carcinoma-related oncogene, DCUN1 domain-containing protein 1, DCN1-like protein 1, RP42 homolog.
Background	DCUN1D1 takes part in the malignant transformation of squamous cell lineage. DCUN1D1 protein regulates Gli1, a main regulator of the hedgehog (HH) pathway which takes a vital role in development, maintenance, and regeneration of practically all adult tissues.
Description	DCUN1D1 expressed in E.Coli is a single, non-glycosylated polypeptide chain containing 279a.a. (1-259a.a.) and having a molecular weight of 32.2kDa. DCUN1D1 is fused to a 20a.a. His-tag at N-terminus and purified by unique purification methods.
Source	E.coli
AA Sequence	MGSSHHHHHH SSGLVPRGSH MNKLKSSQKD KVRQFMIFTQ SSEKTAVSCL SQNDWKLDVA TDNFFQNPEL YIRESVKGSL DRKKLEQLYN RYKDPQDENK IGIDGIQQFC DDLALDPASI SVLIIAWKFR AATQCEFSKQ EFMDGMTELG CDSIEKLKAQ IPKMEQELKE PGRFKDFYQF TFNFAKNPGQ KGLDLEMAIA YWNLVLNGRF KFLDLWNKFL LEHHKRSIPK DTWNLLLDFS TMIADDMSNY DEEGAWPVLI DDFVEFARPQ IAGTKSTTV
Purity	>90% as determined by SDS-PAGE.
Endotoxin	<1.0 EU per μg by the LAL method.
Formulation	The DCUN1D1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 10% glycerol.
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.Please avoid 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.