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TMPH-02079
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SPTLC2 Protein, Human, Recombinant (His & SUMO)
Long chain base biosynthesis protein 2a,Long chain ...
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Human
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E. coli
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Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate. Plays an important role in de novo sphyngolipid biosynthesis which is crucial for adipogenesis. SPTLC2 Protein, Human, Recomb... |
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TMPY-02279
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Nucleoside phosphorylase/PNP Protein, Human, Recombinant (His)
PUNP,PRO1837,purine nucleoside phosphorylase,NP
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Human
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E. coli
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Purine nucleoside phosphorylase (PNP) is a purine-metabolizing enzyme that catalyzes the reversible phosphorolysis of 6-oxypurine (deoxy)nucleosides to their respective bases and (deoxy)ribose-1-phosphate. It is a key enzyme in the purine salvage pathway of mammalian cells. Purine nucleoside phosphorylase is a transferase that catalyzes the addition of phosphate and removal of a purine base from guanosine and similar nucleosides.PNP defects result in metabolic abnormalities and fatal T cell immu... |
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TMPH-01238
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POLQ Protein, Human, Recombinant (His)
DNA polymerase eta,POLQ,DNA polymerase theta
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Human
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Baculovirus Insect Cells
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DNA polymerase that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA. MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions, some of them leading to cellular transformation. POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumul... |
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TMPY-02798
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NEIL1 Protein, Human, Recombinant (His)
NEI1,nei endonuclease VIII-like 1 (E. coli),FPG1,hFPG1
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Human
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E. coli
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NEIL1 is a member of DNA glycosylases. DNA glycosylases are a family homologous to the bacterial Fpg/Nei family. They play a role in base excision repair which is the mechanism by which damaged bases in DNA are removed and replaced. The first step of this process is catalyzed by DNA glycosylases. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. NEIL1 functions in base excision r... |
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TMPH-01237
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POLQ Protein, Human, Recombinant (E. coli, His)
DNA polymerase eta,POLQ,DNA polymerase theta
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Human
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E. coli
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DNA polymerase that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA. MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions, some of them leading to cellular transformation. POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumul... |
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TMPH-00522
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Recombinase cre Protein, Enterobacteria phage P1, Recombinant (His & Myc)
cre,Recombinase cre
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Escherichia phage P1
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E. coli
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Catalyzes site-specific recombination between two 34-base-pair LOXP sites. Its role is to maintain the phage genome as a monomeric unit-copy plasmid in the lysogenic state. |
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TMPJ-00792
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DNA PolymeraseBeta Protein, Human, Recombinant (His)
DNA Polymeraseβ,POLB,DNA Polymerase Beta,DNA Polymerase β
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Human
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E. coli
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Human DNA polymerase β is constitutively expressed in cells. It fills in gaps in DNA that are formed following base excision repair. Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. It conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a proce... |
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TMPH-02463
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HMf-2 Protein, Methanothermus fervidus, Recombinant (His)
Archaeal histone B,hmfB,DNA-binding protein HMf-2
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Methanothermus fervidus
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E. coli
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Binds and compacts DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation in vitro. HMf-2 Protein, Methanothermus fervidus, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 11.7 kDa and the accession number is P19267. |
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TMPH-02462
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HMf-1 Protein, Methanothermus fervidus, Recombinant (His & Myc)
Archaeal histone A,hmfA,DNA-binding protein HMf-1
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Methanothermus fervidus
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E. coli
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Binds and compacts DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation. HMf-1 Protein, Methanothermus fervidus, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 14.9 kDa and the accession number is P48781. |
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TMPK-00516
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BST1 Protein, Cynomolgus, Recombinant (His)
Bp-3,CD157,Bst1,BST-1,Ly65,Bp3,Antigen BP3
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Cynomolgus
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HEK293 Cells
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BST1 overexpression conferred resistance to sphingosine in yeast. BST1 deletion produced sensitivity to exogenous D-erythro-sphingosine and phytosphingosine and intracellular accumulation of sphingosine 1-phosphate upon exposure to exogenous sphingosine. sphingoid base metabolism is similar in all eukaryotes and suggests that yeast genetics may be useful in the isolation and identification of other genes involved in sphingolipid signaling and metabolism. |
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TMPH-01008
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PNKP Protein, Human, Recombinant (His & SUMO)
Polynucleotide kinase-3'-phosphatase,PNKP,DNA 5'-kinase/3'-p...
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Human
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E. coli
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Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. PNKP Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The ... |
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TMPJ-00464
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APE Protein, Human, Recombinant
APEX,Apurinic-Apyrimidinic Endonuclease 1,APEN,DNA-(Apurinic...
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Human
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E. coli
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Apurinic-Apyrimidinic Endonuclease 1 (APE1) is required for efficient DNA base excision repair. When the DNA glycosylase remove the damaged bases, APE1 cleaves the AP site to allow resynthesis and ligation to complete repair. APE1 stimulates the DNA binding activity of many transcription factors, which participate in cancer promotion and progression. APE1 regulates the redox state of multiple transcription factors, such as c-Jun, c-Fos, NF-kB, p53. APEN is also involved in calcium-dependent down... |
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TMPJ-00731
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Carbonic Anhydrase 1 Protein, Human, Recombinant (His)
Carbonic Anhydrase B,Carbonate Dehydratase I,CA-I,Carbonic A...
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Human
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E. coli
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Carbonic Anhydrase 1 (CA1) is a cytosolic enzyme, belonging to the alpha-carbonic anhydrase family. It is highly expressed in erythrocytes and acts as an early marker for erythroid differentiation. Carbonic anhydrase 1 plays a improtant role in many biological processes such as calcification, cellular respiration, bone resorption, acid-base balance. It is activated by imidazole, histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. At the same time, It is inhibited by sulfonam... |
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TMPJ-00701
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Carbonic Anhydrase 11 Protein, Human, Recombinant (His)
Carbonic Anhydrase-Related Protein 2,CARP XI,CA11,CARP-2,Car...
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Human
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HEK293 Cells
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Carbonic Anhydrase-Related Protein 11 (CA11) is a secreted protein member of the α-carbonic anhydrase family. Carbonic Anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA11 is expressed abundantly in the brain with moder... |
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TMPJ-01386
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STUB1 Protein, Human, Recombinant
Carboxy Terminus of Hsp70-Interacting Protein,STIP1 Homology...
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Human
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E. coli
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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.... |
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TMPY-03811
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KCT2 Protein, Human, Recombinant (His)
chromosome 5 open reading frame 15,KCT2,HTGN29
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Human
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HEK293 Cells
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C5orf15 (Chromosome 5 Open Reading Frame 15, also known as KCT2) is a Protein Coding gene. KCT2 gene maps to human chromosome 5q31.1 and is conserved in human, chimpanzee, cow, rat, and chicken. KCT2 is a 265 amino acid single-pass type I membrane protein that is widely expressed in the thyroid, kidney, and other tissues. Chromosome 5 is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. ... |
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TMPY-01877
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CA5A Protein, Human, Recombinant (His)
CA5,GS1-21A4.1,CA5AD,carbonic anhydrase VA, mitochondrial,CA...
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Human
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E. coli
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Carbonic anhydrase 5A, mitochondrial, also known as Carbonate dehydratase VA, Carbonic anhydrase VA, CA-VA and CA5A, is a member of thealpha-carbonic anhydrase family. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospi... |
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TMPY-02277
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Carbonic Anhydrase 7 Protein, Human, Recombinant (His)
CAVII,carbonic anhydrase VII
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Human
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E. coli
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Carbonic anhydrase 7, also known as carbonate dehydratase VII, carbonic anhydrase VII, CA-VII and CA7, is a cytoplasm protein which belongs to thealpha-carbonic anhydrase family. Carbonic anhydrases are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, ... |
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TMPY-01761
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Carbonic Anhydrase 3 Protein, Human, Recombinant (His)
carbonic anhydrase III,CAIII,Car3
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Human
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E. coli
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Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. Carbonic anhydrases (CAs) form a family of enzymes that catalyze the rapid conversion of carbon dioxide and water to bicarbonate an... |
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TMPY-04267
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MSH2 Protein, Human, Recombinant (His & GST)
FCC1,COCA1,HNPCC1,HNPCC,LCFS2,mutS homolog 2
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Human
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Baculovirus Insect Cells
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MSH2 is a key DNA mismatch repair protein, which plays an important role in genomic stability. In addition to its DNA repair function, MSH2 serves as a sensor for DNA base analogs-provoked DNA replication errors and binds to various DNA damage-induced adducts to trigger cell cycle arrest or apoptosis. Loss or depletion of MSH2 from cells renders resistance to certain DNA-damaging agents. Therefore, the level of MSH2 determines the DNA damage response.MSH2 is a central component of the mismatch r... |
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TMPY-01734
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CA13 Protein, Human, Recombinant (His)
carbonic anhydrase XIII,FLJ37995,CAXIII,MGC59868
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Human
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E. coli
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The carbonic anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The carbonic anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. The CAXIII is a member of th... |
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TMPY-02000
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UNG Protein, Human, Recombinant (GST)
uracil-DNA glycosylase,HIGM4,UNG15,UNG1,DGU,UNG2,HIGM5,UDG
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Human
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E. coli
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Isoform 1 is widely expressed with the highest expression in skeletal muscle, heart and testicles. Isoform 2 has the highest expression levels in tissues containing proliferating cells. Uracil-DNA glycosylase exists in two forms: mitochondrial uracil-DNA glycosylase 1 (UNG1) and nuclear uracil-DNA glycosylase 2 (UNG2). uracil-DNA glycosylase. This gene encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil... |
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TMPY-03610
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PSME2 Protein, Human, Recombinant (His)
REGβ,proteasome (prosome, macropain) activator subunit 2 (PA...
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Human
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E. coli
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PSME2, also known as PA28b, is a subunit of proteasome. The 26S proteasome multicatalytic proteinase complex has a highly ordered structure composed of 2 complexes, a 2S core and a 19S regulator. The 2S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 1 non-ATPase subunit... |
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TMPY-03612
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PSME1 Protein, Human, Recombinant (His)
proteasome (prosome, macropain) activator subunit 1 (PA28 al...
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Human
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E. coli
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PA28A, also known as PSME1, is a subunit of proteasome. The 26S proteasome multicatalytic proteinase complex has a highly ordered structure composed of 2 complexes, a 2S core and a 19S regulator. The 2S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 1 non-ATPase subunit... |
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TMPY-03614
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PSME3 Protein, Human, Recombinant (His)
PA28G,PA28-gamma,HEL-S-283,REG-GAMMA,proteasome (prosome, ma...
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Human
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E. coli
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PSME3, also known as PA28-gamma, is a subunit of proteasome. The 26S proteasome multicatalytic proteinase complex has a highly ordered structure composed of 2 complexes, a 2S core and a 19S regulator. The 2S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 1 non-ATPase su... |
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TMPY-01480
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LTC4S Protein, Human, Recombinant (His)
LTC4S,MGC33147,leukotriene C4 synthase
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Human
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Baculovirus Insect Cells
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Leukotriene C4 synthase, also known as LTC4 synthase, Leukotriene-C(4) synthase, and LTC4S, is a multi-pass membrane protein that belongs to the MAPEG family. LTC4S is detected in the lung, platelets, and the myelogenous leukemia cell line KG-1 (at protein level). LTC4S activity is present in eosinophils, basophils, mast cells, certain phagocytic mononuclear cells, endothelial cells, vascular smooth muscle cells, and platelets. LTC4S is essential for the production of cysteinyl leukotrienes (Cys... |
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TMPY-02133
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Carbonic Anhydrase VB Protein, Human, Recombinant (His)
carbonic anhydrase VB, mitochondrial,CA-VB,MGC39962
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Human
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E. coli
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Carbonic anhydrase 5B, also known as carbonate dehydratase VB, carbonic anhydrase VB, CA-VB and CA5B, is amember of the alpha-carbonic anhydrase family. The strongest expression of CA5B / CA-VB is in heart, pancreas, kidney, placenta, lung, and skeletal muscle. It is not expressed in liver. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological process... |
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