Human TRIM21 - Recombinant Protein | Custom Made-To-Order

Name: Human TRIM21 (E3 Ubiquitin-Protein Ligase Trim21) - Recombinant Protein
Brand: Beta LifeScience
SKU: BLT-07371P
Price: 445.0 USD
Availability: InStock

SDS-PAGE analysis of Human TRIM21 (E3 Ubiquitin-Protein Ligase Trim21) - Recombinant Protein, CAT# BLT-07371P, showing >90% purity under 15% SDS-PAGE (Reduced)

Price Save $150

Size

100ug

Quantity

Quantity Pricing

Pack Size	Price (USD)
500 µg	$1,030 (Fall Promotion)
1 mg	$1,870 (Fall Promotion)

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Product Overview

Product Name	Recombinant Human Sjogren Syndrome Antigen A1(SSA1/TRIM21) Protein
Product Overview	This recombinant human Sjogren Syndrome Antigen A1(SSA1/TRIM21) protein includes amino acids 268-465aa of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in PBSprior to lyophilization.
Target Uniprot Id	P19474
Recommended Name	E3 ubiquitin-protein ligase TRIM21
Gene Name	TRIM21
Synonyms	RO52; RNF81; RO52; TRIM21; 52kDa,Ribonucleoprotein Autoantigen SS-A/Ro; Tripartite Motif-Containing
Species	Human
Predicted Molecular Mass	27 kDa
Expression System	E.coli
Expression Range	268-465aa
Tag	N-6His
Purity	>90%
Formulation	Lyophilized
Buffer	PBS
Storage Condition	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Reconstitution Instruction	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Applications	Positive Control; Immunogen; SDS-PAGE; WB
Research Area	Epigenetics And Nuclear Signaling
Target Function	E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of IRF3, hence attenuating type I interferon (IFN)-dependent immune responses. Represses the innate antiviral response by facilitating the formation of the NMI-IFI35 complex through 'Lys-63'-linked ubiquitination of NMI.
Subcellular Location	Cytoplasm. Cytoplasmic vesicle, autophagosome. Nucleus. Cytoplasm, P-body. Note=Enters the nucleus upon exposure to nitric oxide. Localizes to small dot- or rod-like structures in the cytoplasm, called processing bodies (P-bodies) that are located underneath the plasma membrane and also diffusely in the cytoplasm. They are located along the microtubules and are highly motile in cells. Colocalizes with DCP2 in P-bodies.
Protein Family	TRIM/RBCC family
Tissue Specificity	Isoform 1 and isoform 2 are expressed in fetal and adult heart and fetal lung.

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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.