5889 Results for: "Ligases"

Supplier: Prosci

Ubiquitin-Conjugating Enzyme E2 G2 (UBE2G2) is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation, which belong to the ubiquitin-conjugating enzyme family. It shares 60% and 100% sequence identity with S.cerevisiae Ubc7 and mouse respectively. The UBE2G2 enzyme and the GP78 E3 ligase are active components of endoplasmic reticulum-associated degradation pathway which is essential for the degradation of misfolded ER proteins. The mechanism of K48-linked poly-ubiquitination by UBE2G2/GP78 appears to involve the transfer of preassembled Ub chains from UBE2G2 to lysine residues in a substrate. The E2 and E3 enzymes form a large hetero-oligomer which brings multiple UBE2G2 molecules into close proximity which allows for Ub transfer between neighboring E2s.

Supplier: Genetex

Rabbit Polyclonal antibody to PJA2 (praja ring finger 2, E3 ubiquitin protein ligase)

Supplier: Bioss

The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. MARCH8 (membrane-associated ring finger (C3HC4) 8), also known as MIR or RNF178 (RING finger protein 178), is a 291 amino acid multi-pass membrane protein that localizes to vesicle membranes and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, including immature dendritic cells, MARCH8 functions as an E3 ubiquitin ligase that is thought to regulate immune responses by promoting the ubiquitination and subsequent degradation of target proteins, such as B7-2 and CD71.

Supplier: Rockland Immunochemical

Polycomb group (PcG) proteins are chromatin-associated proteins which are important for embryonic and adult stem cell self-renewal and maintenance. At least two distinct human PcG complexes have been identified. Polycomb repressive complex I (PRC1) contains CBX4/Pc2, HPH1 and RING domain-containing proteins (RING1, RING2 and BMI1). CBX4 (Chromobox protein homolog 4 or PC2), which functions as a transcriptional suppressor, is a candidate of KyoT2-binding proteins. It is a E3 SUMO-protein ligase which facilitates SUMO1 conjugation. Depletion of CBX4 results in decreased cellular resistance to ionizing radiation. CBX4 is directly involved in the cellular response to DNA damage.

Supplier: Rockland Immunochemical

The PIAS (protein inhibitor of activated STAT) proteins play a crucial role as transcriptional coregulators in various cellular pathways, including the STAT, p53 and the steroid hormone signaling pathway. The PIAS protein family includes at least five evolutionarily conserved genes, including PIAS3. The major function of the PIAS proteins is the control of gene transcription and can also act as small ubiquitin-like-modifier (SUMO) E3 ligases. PIAS3 binds specifically to STAT3 following the stimulation of STAT3. Increased expression of PIAS3 has been observed in several human cancers, including lung, breast, and brain tumors, but not in anaplastic lymphoma kinase-positive T/null-cell lymphomas, indicating that PIAS3 plays multiple roles in different tissue and cell types.

Supplier: Bioss

E3 ubiquitin ligase whose activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2.

Supplier: Bioss

The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. SH3RF2 (SH3 domain containing ring finger 2), also known as RNF158, is a 729 amino acid protein with one RING-type zinc finger domain and three SH3 domains. Via its RING-type zinc finger domain, SH3RF2 binds an E2 ubiquitin-conjugating enzyme. This suggests that SH3RF2 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. Due to alternative splicing events, SH3RF2 is expressed as two different isoforms.

Supplier: Prosci

E3 Ubiquitin-Protein Ligase CHIP is a cytoplasmic protein. CHIP is highly expressed in skeletal muscle, heart, pancreas, brain and placenta. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain; lead to in client substrate ubiquitylation and degradation by the proteasome. CHIP targets misfolded chaperone substrates towards proteasomal degradation. CHIP mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. CHIP plays a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. It also may regulate the receptor stability and activity through proteasomal degradation.

Supplier: Bioss

The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. MARCH8 (membrane-associated ring finger (C3HC4) 8), also known as MIR or RNF178 (RING finger protein 178), is a 291 amino acid multi-pass membrane protein that localizes to vesicle membranes and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, including immature dendritic cells, MARCH8 functions as an E3 ubiquitin ligase that is thought to regulate immune responses by promoting the ubiquitination and subsequent degradation of target proteins, such as B7-2 and CD71.

Supplier: Bioss

The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. SH3RF2 (SH3 domain containing ring finger 2), also known as RNF158, is a 729 amino acid protein with one RING-type zinc finger domain and three SH3 domains. Via its RING-type zinc finger domain, SH3RF2 binds an E2 ubiquitin-conjugating enzyme. This suggests that SH3RF2 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. Due to alternative splicing events, SH3RF2 is expressed as two different isoforms.

Supplier: Rockland Immunochemical

MDM2 is a nuclear phosphoprotein that binds and inhibits transactivation by p53, as part of an autoregulatory negative feedback loop (1). Overexpression of the MDM2 gene product can lead to excessive inactivation of p53 thereby diminishing its tumor suppressor function. The inactivation of p53 is mediated by the E3 ubiquitin ligase activity of MDM2 which targets p53 for proteasomal degradation. MDM2 also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5 (2). Amplification of MDM2 is frequently observed in human sarcomas and this is consistent with the hypothesis that MDM2 binds to p53 which then leads to escape from p53-regulated growth control. MDM2 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cell Cycle, and Cellular Stress research.

Supplier: Prosci

LIG1is DNA ligase I, with functions in DNA replication and the base excision repair process. Mutations in LIG1 that lead to DNA ligase I deficiency result in immunodeficiency and increased sensitivity to DNA-damaging agents.LIG1 encodes DNA ligase I, with functions in DNA replication and the base excision repair process. Mutations in LIG1 that lead to DNA ligase I deficiency result in immunodeficiency and increased sensitivity to DNA-damaging agents. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Rockland Immunochemical

The PIAS proteins (protein inhibitor of activated STAT) play a crucial role as transcriptional coregulators in various cellular pathways, including the STAT, p53 and the steroid hormone signaling pathway. The PIAS protein family includes at least five evolutionarily conserved genes, including PIAS1. The major function of the PIAS proteins is the control of gene transcription and can also act as small ubiquitin-like-modifier (SUMO) E3 ligases. PIAS1 binds specifically to STAT1, inhibiting STAT1-mediated gene activation and also binds to the Gu/RNA helicase II enzyme, leading to the proteolytic cleavage of Gu/RH-II. PIAS1 is a potent co-activator for CP2c-mediated alpha-globin expression in erythroid cells.

Supplier: Rockland Immunochemical

The PIAS (protein inhibitor of activated STAT) proteins play a crucial role as transcriptional coregulators in various cellular pathways, including the STAT, p53 and the steroid hormone signaling pathway. The PIAS protein family includes at least five evolutionarily conserved genes, including PIAS4. The major function of the PIAS proteins is the control of gene transcription and can also act as small ubiquitin-like-modifier (SUMO) E3 ligases. PIAS4 interacts with p53 and blocks its ability to induce Bax and p21 transcription. PIAS4 is also important in the control of the ubiquitin-dependent proteasomal degradation of the Ets-1 transcription factor. PIAS4 has been implicated in the DNA-damage response pathway and is thought to work in combination with PIAS1 for the productive association of 53BP1, BRCA1 and RNF168.

Supplier: Prosci

RNF43 is a HAP95 (AKAP8L) binding ubiquitin ligase that promotes cell growth and is upregulated in colon cancer.

Supplier: Prosci

E3 ubiquitin-protein ligase which promotes polyubiquitination and degradation by the proteasome pathway of ZIC2 (By similarity).

Supplier: Prosci

Probable E3 ubiquitin-protein ligase which plays an important role in blastocyst development (By similarity).

Supplier: Proteintech

The cullin family proteins are scaffold proteins for the Ring finger type E3 ligases. Humans express seven cullin proeins: CUL1–3, CUL4A, CUL4B, CUL5, and CUL7. Each cullin protein can form an E3 ligase similar to the prototype Ring-type E3 ligase Skp1-CUL1-F-box complex. The Cullin-RING-finger type E3 ligases are important regulators in early embryonic development, as highlighted by genetic studies demonstrating that knock-out of CUL1, CUL3, or CUL4A in mice results in early embryonic lethality.

Supplier: Prosci

MARCH7 is an E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.

Supplier: New England Biolabs (NEB)

New England Biolabs supplies a 5X reaction buffer for use with Quick T4 DNA Ligase

Supplier: Bioss

RNF43 is a probable E3 ubiquitin-protein ligase that promotes cell growth and is upregulated in colon cancer. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.

Supplier: Prosci

DCAF10 may function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.

Supplier: Proteintech

The UBE3C antibody from Proteintech is a rabbit polyclonal antibody to a recombinant protein of human UBE3C. This antibody recognizes human,mouse,rat antigen. The UBE3C antibody has been validated for the following applications: ELISA, WB analysis.

Supplier: Proteintech

Cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ligase are the largest family of ubiquitin ligases which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. One of seven cullin proteins serves as a scaffold protein for the assembly of the multisubunit ubiquitin ligase complex. CUL3 (Cullin-3) ubiquitin ligase complex targets multiple substrate for ubiquitination including cyclin E and of cyclin D1. Defects in CUL3 are the cause of Pseudohypoaldosteronism type 2E (PHA2E) characterized by severe hypertension, hyperkalemia, hyperchloremia, hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics.

Supplier: Bioss

Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.

Supplier: Bioss

Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.

Supplier: Bioss

Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.

Supplier: Genetex

Rabbit Polyclonal antibody to CHFR (checkpoint with forkhead and ring finger domains, E3 ubiquitin protein ligase)

Supplier: Genetex

DTX3L functions as an E3 ubiquitin ligase (Takeyama et al., 2003 [PubMed 12670957]).[supplied by OMIM]

Supplier: Bioss

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