Recombinant Human c-jun Protein (His Tag)

Name: Recombinant Human c-jun Protein (His Tag)
Brand: Beta LifeScience
SKU: BL-103PC
Availability: InStock

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.

Product Overview

Tag	His
Host Species	Human
Synonym	AP-1; AP1; c-Jun and Homo sapiens jun oncogene (JUN).
Background	The transcription factor AP-1 (activator protein-1) is involved in cellular proliferation, transformation and death. AP-1 and nuclear factor B (NF-kB) can be specifically targeted to prevent cancer induction in mouse models. AP-1 can be produced by 18 different dimeric combinations of proteins from the Jun (c-Jun, JunB and JunD) and Fos (c-Fos, FosB, Fra-1 and Fra-2) families, including Jun homodimers and Jun-Fos heterodimers (1-4). The Jun and Fos proteins contain a basic-region leucine zipper (bZIP) domain, and are capable of binding to other bZIP proteins including those from the ATF, MAF, CNC and C/EBP (CCAAT/enhancer-binding protein) subfamilies (5]) Jun-Jun and Jun-Fos dimers bind with highest affinity to the 12-O-tetradecanoylphorbol-13-acetate (TPA) response element (TRE) [TGA(C/G)TCA] (6), although many other `AP-1-like sites` have been reported. Binding to any of these sites can be tissue-specific, or affected by neighboring sequences, and dependent upon interactions with other transcription factors or cofactors. Jun and Fos proteins can also dimerize with other bZIP proteins, allowing them to target other DNA binding sites, such as the cAMP response element (CRE), the antioxidant response elements (ARE), and half-sites composed of half of a TRE site and half of a MAF- or CNC-binding site. In addition, AP-1 proteins can interact with other proteins, including the p65 subunit of NF-kB, CBP (CRE-binding-protein-binding protein) (p300), SMAD-3 and -4, and the retinoblastoma protein (see 5 for a more complete list), further increasing the combinatorial potential of Jun and Fos proteins. AP-1 regulates a variety of cellular processes, including proliferation, differentiation and apoptosis, and contributes to both basal and stimulus-activated gene expression. It is activated by growth factors, hormones, stress, cytokines, ROS and ultraviolet radiation Activation occurs both transcriptionally and post-translationally, and is signaled predominantly through the mitogen-activated protein kinase (MAPK) cascade (7). The combinatorial diversity of AP-1 proteins and other interacting factors appears to influence how specific cell types respond to a stimulus. The growth-promoting activity of c-Jun is mediated by repression of tumor suppressors, as well as up-regulation of positive cell cycle regulators. Mostly, c-Jun is a positive regulator of cell proliferation, whereas JunB has the converse effect (8).
Description	Recombinant Human c-jun Protein was expressed in Baculovirus-insect cell. This protein is fused with a His tag and purified using our unique purification methods.
Source	Baculovirus-insect cell
AA Sequence	MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP PLSPIDMESQ ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F
Molecular Weight	37.5 kDa.
Purity	>90% purity by SDS-PAGE
Endotoxin	<0.1 ng/µg (1 EU/µg) as determined by LAL test.
Bioactivity	1 unit equals 1 nanogram of purified protein.
Formulation	The Human c-jun protein is supplied in 20mM Tris-HCl pH7.9,100mM NaCl, 0.2mM EDTA, 1mM DTT and 20% glycerol.
Usage	For Research Use Only
Storage	Stored the protein at -70°C before use. 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.