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Recombinant Human E3 ubiquitin-protein ligase TRIM21(TRIM21)

SKU : BHP10502518

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CUSABIO TECHONOLOGY LLC

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Mfr.No.	CSB-YP024457HU
Alternative Names	52 kDa Ro protein52 kDa ribonucleoprotein autoantigen Ro/SS-ARING finger protein 81Ro(SS-A)Sjoegren syndrome type A antigen ,SS-ATripartite motif-containing protein 21, 52 kDa Ro protein52 kDa ribonucleoprotein autoantigen Ro/SS-ARING finger protein 81Ro(SS-A)Sjoegren syndrome type A antigen ; SS-ATripartite motif-containing protein 21
Antigen	TRIM21
Tag	N-terminal 6xHis-tagged
Regulatory	RUO
Relevance	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
Source	Yeast
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Protein Name	Recommended name: E3 ubiquitin-protein ligase TRIM21; EC= 6.3.2.-; Alternative name(s): 52 kDa Ro protein; 52 kDa ribonucleoprotein autoantigen Ro/SS-A; RING finger protein 81; Ro(SS-A); Sjoegren syndrome type A antigen; Short
Expression Region	1-475aa
Mol Weight	56.2kDa
Nature	recombinant
Protein Description	Full Length

Subcellular Location	Cytoplasm, Cytoplasmic vesicle, autophagosome, Nucleus, Cytoplasm, P-body
Uniprot	P19474, P19474
Database Links	HGNC:11312 OMIM:109092 KEGG:hsa:6737 STRING:9606.ENSP00000254436 UniGene:Hs.532357
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
Protein Families	TRIM/RBCC family
Research Area	Epigenetics and Nuclear Signaling
Tissue Specificity	Isoform 1 and isoform 2 are expressed in fetal and adult heart and fetal lung.
Weight	56.17kDa

Stotage Note	Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Buffer	Tris-based buffer，50% glycerol
Purity	Greater than 90% as determined by SDS-PAGE.
Storage	The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Storage Buffer	Tris-based buffer,50% glycerol

Immunogen Species	Homo Sapiens (Human)

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SKU	Supplier No.	Size	Your price	Quantity
BHP10502518	CSB-YP024457HU	500ug	$1298		Add to Cart
BHP10502518	CSB-YP024457HU	100ug	$470		Add to Cart
BHP10502518	CSB-YP024457HU	20ug	$250		Add to Cart

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