目录号 | 产品详情 | 靶点 | |
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T8188 | Others Microtubule Associated | ||
Podophyllotoxone 是从八角莲根中分离得到的一种天然产物,能抑制微管蛋白聚合,具有抗癌活性。 | |||
T39994 | Microtubule Associated | ||
Sovilnesib 是一种有效kinesin-like protein KIF18A 抑制剂。它可用于癌症的研究。 | |||
T9595 | Microtubule Associated | ||
LP-261 是一种新型的微管蛋白靶向抗癌剂,可与微管蛋白上的秋水仙碱位点结合,诱导 G2/M 期阻滞,其EC50为 3.2 μM。它可抑制人非小细胞肺癌的生长,可用于癌症研究。 | |||
T21632 | Others Microtubule Associated | ||
Myoseverina 是多核肌管可逆分裂成单核片段的诱导剂,影响多种生长因子、免疫调节、细胞外基质重塑和应激反应基因的表达,与伤口愈合和组织再生相关通路的激活一致。 | |||
T10460 | Apoptosis Microtubule Associated | ||
Batabulin (T138067) 是一种抗肿瘤剂,可与 β-微管蛋白同种型的子集共价且选择性地结合,从而破坏微管聚合。它影响细胞形态并导致细胞周期停滞,最终诱导细胞凋亡。 | |||
T16129 | HDAC | ||
MPI_5a 是高效的 HDAC6选择性抑制剂,IC50=36 nM,对其他 HDAC 酶几乎无抑制作用。MPI_5a 抑制细胞内酰基微管蛋白积累, IC50为 210 nM。 | |||
T3S0209 | ERK p38 MAPK NF-κB Akt JNK mTOR | ||
Vincristine 与微管蛋白结合并抑制微管的形成,从而抑制癌细胞的有丝分裂。 Vincristine 可用作微管去稳定剂,用于研究治疗血液系统癌症,如白血病和淋巴瘤以及儿童肉瘤的相关研究。 | |||
T5699 | Apoptosis Microtubule Associated | ||
SSE15206 是一种克服多药耐药性的微管聚合抑制剂,其在 HCT116 细胞中的 GI50值为 197 nM。由于癌细胞中纺锤体形成不完整,导致 G2/M 停滞,有丝分裂异常。 | |||
T14965 | ATPase Hedgehog/Smoothened | ||
Ciliobrevin D 是细胞渗透性,可逆和特异性的 AAA + ATPase 运动细胞质动力蛋白抑制剂。它在体外抑制依赖于动力蛋白的微管滑动和 ATPase 活性。它抑制Hedgehog 信号和初级纤毛形成。 | |||
T1121 | Microtubule Associated Topoisomerase | ||
Podofilox ((+)-Shikonin) 是从八角莲中分离的一种木脂素,是微管组装和 DNA 拓扑异构酶 II 抑制剂。它对皮肤和粘膜有很强的刺激性,具有角质溶解作用,可用于治疗疣和角化病,具有潜在的抗肿瘤特性。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-03059 | Tubulin cofactor A Protein, Human, Recombinant | Human | E. coli | ||
Tubulin folding cofactor A belongs to the TBCA family. It is one of four proteins (cofactors A, D, E, and C) involved in the early step of the tubulin folding pathway. These proteins can fold intermediates and finally lead to correctly folded beta-tubulin. It is believed that tubulin folding cofactors A and D play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Tubulin folding cofactor E binds to the cofactor D/beta-tubulin complex; interaction with tubulin folding cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state.
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TMPJ-00773 | TUBB4A Protein, Human, Recombinant (His) | Human | E. coli | ||
Tubulin Beta-4A Chain (TUBB4A) is a cytoplasmic peptide containing 444 amino acids. TUBB4A is a member of the Tubulin family. Tubulin is the major constituent of microtubules. Tubulin is a dimer composed of one alpha and one beta tubulin molecule; there are many forms of beta tubulins, Beta II and Beta IV Tubulin are ubiquitously expressed. Beta-III Tubulin, also known as Tubulin Beta-4, is regarded as a neuron-specific marker. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
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TMPY-03392 | CKAP1/TBCB Protein, Human, Recombinant (His) | Human | E. coli | ||
Tubulin-folding cofactor B, also known as TBCB, belongs to the TBCB family. It contains 1 CAP-Gly domain and can be detected in most tissues. TBCB binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway. The cytoskeleton is composed of 3 structural elements: actin filaments, microtubules, and intermediate filaments. TBCB is involved in regulation of tubulin heterodimer dissociation. It may function as a negative regulator of axonal growth.
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TMPH-00383 | Tubulin beta-1 chain Protein, Chicken, Recombinant (His) | Chicken | E. coli | ||
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
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TMPY-04110 | TPPP2 Protein, Human, Recombinant (His) | Human | E. coli | ||
TPPP2 Protein, Human, Recombinant (His) is expressed in E. coli with His tag. The predicted molecular weight is 20.3 kDa. Accession number: AAH38970.1
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TMPY-03397 | TPPP3 Protein, Human, Recombinant (His) | Human | E. coli | ||
TPPP3, a member of the Tubulin polymerization-promoting protein family, is an intrinsically unstructured protein that induces tubulin polymerization. TPPP3 is a marker in the developing musculoskeletal system. In tendons, Tppp3 is expressed in cells at the circumference of the developing tendons, likely the progenitors of connective tissues that surround tendons: the tendon sheath, epitenon, and paratenon. Tppp3 is also expressed in forming synovial joints. The onset of Tppp3 expression in joints coincides with cavitation, representing a molecular marker that can be used to indicate this stage in joint transition in joint differentiation. In late embryonic stages, Tppp3 expression highlights other demarcation lines that surround differentiating tissues in the forelimb. Depletion of TPPP3 by microRNA-based RNA interference (RNAi) inhibits cell growth, arrests cell cycles, and causes mitotic abnormalities in HeLa cells. C57BL/6 mice that received subcutaneously injected LLC (Lewis lung carcinoma) cells in which TPPP3 was knocked down showed a pronounced reduction in tumor progression. The migration/invasion activity of TPPP3-knockdown LLC cells was significantly suppressed in a transwell chamber migration assay. When these cells were injected into the tail veins of C57BL/6 mice, they exhibited milder lung metastasis compared with control tumor cells. Taken together, these findings suggested that the TPPP3 gene played an important role in tumorigenesis and metastasis, and it could potentially become a novel target for cancer therapy.
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TMPY-01357 | S100A9 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A9, also known as S100 calciumbinding protein A9, S100A9, and CAGB, is a member of the S-100 family. S100A9 is expressed by macrophages in acutely inflammed tissues and in chronic inflammation. It is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a calcium-binding protein. It has anti-microbial activity towards bacteria and fungi. The anti-microbial and proapoptotic activity of S100A9 is inhibited by zinc ions. S100A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when unphosphorylated. It also promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A9 plays a role as a proinflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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TMPY-01203 | RP2 Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
XRP2, also known as Protein XRP2 and RP2, is a member of the TBCC (tubulin cofactor C) family and contains one C-CAP/cofactor C-like domain. This protein is encoded by the RP2 gene in humans. XRP2 stimulates the GTPase activity of tubulin, but does not enhance tubulin heterodimerization. XRP2 acts as guanine nucleotide dissociation inhibitor for ARL3. Defects in RP2 gene are the cause of retinitis pigmentosa type 2 (RP2), also known as X-linked retinitis pigmentosa 2 (XLRP-2). It leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
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TMPJ-00827 | Tau-D Protein, Human, Recombinant (His) | Human | E. coli | ||
Microtubule-Associated Protein TAU is abundantly expressed in neurons of the central nervous system and less commonly expressed elsewhere, but is also expressed at very low levels in CNS astrocytes and oligodendrocytes. Tau interacts with tubulin to stabilize microtubules and promotes tubulin assembly into microtubules. The C-terminus of TAU binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau acts as a linker protein. When tau is defective, and no longer stabilize microtubules properly, it can result in dementias such as Alzheimer's disease and other tauopathies.
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TMPH-02260 | TUBB Protein, Human, Recombinant (His) | Human | E. coli | ||
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
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TMPH-02261 | TUBB2A Protein, Human, Recombinant (His) | Human | Yeast | ||
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
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TMPH-02304 | Vasohibin-2/VASH2 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function. Critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning. Acts as an activator of angiogenesis: expressed in infiltrating mononuclear cells in the sprouting front to promote angiogenesis. Plays a role in axon formation.
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TMPY-03750 | CRIPT Protein, Human, Recombinant (His) | Human | E. coli | ||
CRIPT, also known as cysteine-rich PDZ-binding protein, belongs to the CRIPT family. It interacts with TUBB1. CRIPT also interacts strongly with the PDZ3 domain of members of the DLG4 family. It is involved in the cytoskeletal anchoring of DLG4 in excitatory synapses. CRIPT is highly conserved from mammals to plants and binds selectively to the third PDZ domain (PDZ3) of PSD-95 via its C terminus. n heterologous cells, CRIPT causes a redistribution of PSD-95 to microtubules. In brain, CRIPT colocalizes with PSD-95 in the postsynaptic density and can be coimmunoprecipitated with PSD-95 and tubulin. These findings suggest that CRIPT may regulate PSD-95 interaction with a tubulin-based cytoskeleton in excitatory synapses.
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TMPH-02262 | TUBB3 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TUBB3 plays a critical role in proper axon guidance and maintenance. Binding of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Plays a role in dorsal root ganglion axon projection towards the spinal cord.
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TMPH-02263 | VASH1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function. Critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning. Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis. This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts.
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TMPJ-01270 | ZMYND19 Protein, Human, Recombinant (His) | Human | E. coli | ||
Human Zinc Finger MYND Domain-Containing Protein 19 (ZMYND19) is a protein that contains 1 MYND-Type Zinc Finger. ZMYND19 can be expressed by the brain, testis, placenta, heart, liver, skeletal muscle, kidney, and stomach. ZMYND19 interacts with GPR24/MCH-R1. It binds to the C terminus of Melanin-Concentrating Hormone Receptor-1 and the N Termini of α-Tubulin. ZMYND19 may be involved as a regulatory molecule in GPR24/MCH-R1 signaling.
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TMPH-02183 | CCT2 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
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TMPJ-01387 | PACSIN2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Protein Kinase C and Casein Kinase Substrate in Neurons Protein 2 (PACSIN2) is a member of the PACSIN family. PACSIN2 is localized to the plasma membrane via its coiled-coil domain. PACSIN2 is widely expressed and contains one FCH domain and one SH3 domain. PACSIN2 forms homo- and hetero-aggregates with other PACSINs. PACSIN2 may play a role in vesicle formation and transport. In addition, PACSIN2 is involved in linking the actin cytoskeleton with vesicle formation by regulating tubulin polymerization.
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TMPY-03047 | Stathmin 1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Stathmin1 (STMN1) is a cytosolic phosphoprotein that regulates cellular microtubule dynamics and is known to have oncogenic activity. STMN1 is a possible biomarker for paclitaxel sensitivity and poor prognosis in GC and could be a novel therapeutic target in metastatic GC. STMN1 expression might serve as a biomarker for determining patient atypical meningioma prognosis. Stathmin1 (STMN1) is a cytosolic protein involved in microtubule dynamics through inhibition of tubulin polymerization and promotion of microtubule depolymerization, which has been implicated in carcinogenesis and aggressive behavior in multiple epithelial malignancies. Stathmin 1 (STMN1) suppression was reported to reduce cellular viability and migration potential. STMN1 may be a promising candidate for targeted therapies in PDAC.
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TMPY-03509 | TCTP/TPT1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Tumor protein, also known as TPT1, is a highly conserved protein among many eukaryotic organisms. Tumor protein is involved in a variety of cellular activities, including microtubule stabilization, calcium-binding activities, and apoptosis. The Mammalian translationally controlled tumour protein (TPT1) (or P23) is a protein that has been found to be preferentially synthesised in cells during the early growth phase of some types of tumour, but which is also expressed in normal cells. It was first identified as a histamine-releasing factor, acting in IgE +-dependent allergic reactions. In addition, TPT1 has been shown to bind to tubulin in the cytoskeleton, has a high affinity for calcium, is the binding target for the antimalarial compound artemisinin, and is induced in vitamin D-dependent apoptosis. TPT1 production is thought to be controlled at the translational as well as the transcriptional level.
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TMPH-01252 | DCTN1 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation.
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TMPY-01330 | S100A9 Protein, Human, Recombinant | Human | E. coli | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A9, also known as S100 calciumbinding protein A9, S100A9, and CAGB, is a member of the S-100 family. S100A9 is expressed by macrophages in acutely inflammed tissues and in chronic inflammation. It is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a calcium-binding protein. It has anti-microbial activity towards bacteria and fungi. The anti-microbial and proapoptotic activity of S100A9 is inhibited by zinc ions. S100A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when unphosphorylated. It also promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A9 plays a role as a proinflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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TMPY-02821 | S100A9 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A9, also known as S100 calciumbinding protein A9, S100A9, and CAGB, is a member of the S-100 family. S100A9 is expressed by macrophages in acutely inflammed tissues and in chronic inflammation. It is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a calcium-binding protein. It has anti-microbial activity towards bacteria and fungi. The anti-microbial and proapoptotic activity of S100A9 is inhibited by zinc ions. S100A9 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide (LPS). It promotes tubulin polymerization when unphosphorylated. It also promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A9 plays a role as a proinflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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TMPH-00297 | S100A9 Protein, Bovine, Recombinant (His & Myc & SUMO) | Bovine | E. coli | ||
S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, NXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif.
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