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1000 results found for “Chitinase”
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Name :
HDAC8 HumanDescription:
Histone Deacetylase 8 Human Recombinant
Histone deacetylase 8, HD8, HDAC8, HDACL1, CDA07, RPD3.
Product # :
ENZ-210Price :
Quantity :
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Shipped with Ice Packs
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Description
HDAC8 Human Recombinant produced in Sf9 Baculovirus cells, glycosylated polypeptide chain containing 383 amino acids (1-377) and having a molecular mass of 42.6kDa. HDAC8 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The HDAC8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.
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Synonyms
Histone deacetylase 8, HD8, HDAC8, HDACL1, CDA07, RPD3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MEEPEEPADS GQSLVPVYIY SPEYVSMCDS LAKIPKRASM VHSLIEAYAL HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDDDH PDSIEYGLGY DCPATEGIFD YAAAIGGATI TAAQCLIDGM CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFE RILYVDLDLH HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDGIQDEKY YQICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWQLATLI LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH RIQQILNYIK GNLKHVVHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2L3 HumanDescription:
Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant
Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.
Product # :
ENZ-342Price :
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Description
Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids & having a molecular mass of 17.9 kDa.
Source
Escherichia Coli.
Formulation
The protein contains 50mM HEPES (pH-7.5) 150mM NaCl, 1mM DTT, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Human Ubquitin-conjugating enzyme 7 (UbcH7) is a ubiquitin-conjugating enzyme (E2) mediating c-fos degradation, transcription factor NF-B maturation, and human papilloma virus-mediated p53 and Myc protein degradation, in vitro. The ubiquitin-conjugating enzymes (E2s) are essential components of the post-translational protein ubiquitination pathway, mediating the transfer of activated ubiquitin to substrate proteins. The human UBE2L1-UBE2L4 gene could potentially encode different isoforms of the UbcH7. UBE2L3 gene, located at chromosome 22q11.2, is the only identical family member with introns and encodes a polypeptide sequence identical to that of UbcH7.
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Synonyms
Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2V2 HumanDescription:
Ubiquitin-Conjugating Enzyme E2 Variant 2 Human Recombinant
DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.
Product # :
ENZ-550Price :
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Description
UBE2V2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145 a.a.) and having a molecular mass of 18.5 kDa. The UBE2V2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2V2 Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
UBE2V2 comprises a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes however require the conserved cysteine residue that is vital for the catalytic activity of E2s. UBE2V2 shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. UBE2V2 participates in the differentiation of monocytes and enterocytes.
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Synonyms
DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ ELRRLMMSKE NMKLPQPPEG QTYNN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DAAO Human, ActiveDescription:
D-Amino Acid Oxidase Human Recombinant, BioActive
D-Amino Acid Oxidase 2, D-Amino-Acid Oxidase, EC 1.4.3.3, DAMOX, DAAO, EC 1.4.3, OXDA.
Product # :
ENZ-1142Price :
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Shipped with Ice Packs
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Description
DAAO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (1-347) and having a molecular mass of 41.6 kDa. DAAO Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DAAO Human protein (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 20% glycerol & 1mM DTT.
.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3.5unit/mg, in which one unit will oxidatively deaminate 1.0 umole of D-alanine to pyruvateper minute at pH 8.5 at 37C, in the presence of catalase.
More Info
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Introduction
D-amino-acid oxidase or DAAO is an enzyme that oxidizes D-amino acids to their imino acids form while using FAD (flavin adenine dinucleotide) as a co-factor, resulting in the formation of ammonia & hydrogen peroxide. the enzyme may take part in keeping the balance of acid base in the kidney tissue. Another role is to detoxifying molecules that abolish D-amino acids aggregated while the cell ages.
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Synonyms
D-Amino Acid Oxidase 2, D-Amino-Acid Oxidase, EC 1.4.3.3, DAMOX, DAAO, EC 1.4.3, OXDA.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UFC1 HumanDescription:
Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant
Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.
Product # :
ENZ-138Price :
Quantity :
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Shipped with Ice Packs
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Description
UFC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.6kDa.UFC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UFC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UFC1 is a member of the ubiquitin-conjugating enzyme family. UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1. UFM1 is activated by UBA5 (a novel E1-like enzyme) by forming a high-energy thioester bond. Activated UFM1 is subsequently transferred to its cognate E2-like enzyme, UFC1, in a similar thioester linkage.
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Synonyms
Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
UFC1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GLYAT HumanDescription:
Glycine-N-Acyltransferase Human Recombinant
Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.
Product # :
ENZ-148Price :
Quantity :
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Shipped with Ice Packs
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Description
GLYAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 36.0 kDa.The GLYAT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLYAT protein (0.5mg/ml) is supplied in 20mM Tris-HCl, pH-8, 1mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GLYAT is a mitochondrial acyltransferase that conjugates glycine with acyl-CoA substrates in the mitochondria. GLYAT is vital to the detoxification of endogenous and xenobiotic acyl-CoA's.
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Synonyms
Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.
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Physical Appearance
GLYAT is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMLPLQGAQM LQMLEKSLRK SLPASLKVYG TVFHINHGNP FNLKAVVDKW PDFNTVVVCP QEQDMTDDLD HYTNTYQIYS KDPQNCQEFL GSPELINWKQ HLQIQSSQPS LNEAIQNLAA IKSFKVKQTQ RILYMAAETA KELTPFLLKS KILSPSGGKP KAINQEMFKL SSMDVTHAHL VNKFWHFGGN ERSQRFIERC IQTFPTCCLL GPEGTPVCWD LMDQTGEMRM AGTLPEYRLH GLVTYVIYSH AQKLGKLGFP VYSHVDYSNE AMQKMSYTLQ HVPIPRSWNQ WNCVPL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2H HumanDescription:
Ubiquitin-Conjugating Enzyme E2H Human Recombinant
Ubiquitin-conjugating enzyme E2 H, UbcH2, Ubiquitin carrier protein H, Ubiquitin-conjugating enzyme E2-20K, Ubiquitin-protein ligase H, UBE2H, GID3, UBC8, UBCH.
Product # :
ENZ-603Price :
Quantity :
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Shipped with Ice Packs
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Description
UBE2H Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-183) and having a molecular mass of 23.1kDa.UBE2H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2H solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitin-conjugating enzyme E2 H (UBE2H) is a member of the ubiquitin-conjugating enzyme family. Protein modification with ubiquitin is a vital cellular apparatus for directing abnormal or short-lived proteins for degradation. Ubiquitination requires at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2H receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2H protein sequence is 100% identical to the mouse homolog and 98% identical to the frog and zebrafish homologs.
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Synonyms
Ubiquitin-conjugating enzyme E2 H, UbcH2, Ubiquitin carrier protein H, Ubiquitin-conjugating enzyme E2-20K, Ubiquitin-protein ligase H, UBE2H, GID3, UBC8, UBCH.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSPSPG KRRMDTDVVK LIESKHEVTI LGGLNEFVVK FYGPQGTPYE GGVWKVRVDL PDKYPFKSPS IGFMNKIFHP NIDEASGTVC LDVINQTWTA LYDLTNIFES FLPQLLAYPN PIDPLNGDAA AMYLHRPEEY KQKIKEYIQK YATEEALKEQ EEGTGDSSSE SSMSDFSEDE AQDMEL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MTHFS HumanDescription:
5,10-Methenyltetrahydrofolate Synthetase Human Recombinant
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
Product # :
ENZ-096Price :
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Shipped with Ice Packs
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Description
MTHFS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203a.a.) and having a molecular mass of 25.4 kDa. MTHFS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MTHFS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 5mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).
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Synonyms
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAAAVSSAK RSLRGELKQR LRAMSAEERL RQSRVLSQKV IAHSEYQKSK RISIFLSMQD EIETEEIIKD IFQRGKICFI PRYRFQSNHM DMVRIESPEE ISLLPKTSWN IPQPGEGDVR EEALSTGGLD LIFMPGLGFD KHGNRLGRGK GYYDAYLKRC LQHQEVKPYT LALAFKEQIC LQVPVNENDM KVDEVLYEDS STA
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CKMT3 HumanDescription:
Creatine Kinase Muscle Type-3 Human Recombinant
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.
Product # :
CKI-272Price :
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Shipped with Ice Packs
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Description
CKMT3 Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA.The CKMT3 is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Each mg of protein contains 20mM Tris pH-8, 1mM EDTA and 1mM DTT.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 500 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 2,000ng/ml.More Info
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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
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Synonyms
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PYGL HumanDescription:
Phosphorylase, Glycogen, Liver Human Recombinant
GSD6, Glycogen phosphorylase, liver form.
Product # :
ENZ-675Price :
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Shipped with Ice Packs
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Description
PYGL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 879 amino acids (1-847 a.a) and having a molecular mass of 100.7kDa.PYGL is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PYGL protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.
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Synonyms
GSD6, Glycogen phosphorylase, liver form.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFELRRQ ASMAKPLTDQ EKRRQISIRG IVGVENVAEL KKSFNRHLHF TLVKDRNVAT TRDYYFALAH TVRDHLVGRW IRTQQHYYDK CPKRVYYLSL EFYMGRTLQN TMINLGLQNA CDEAIYQLGL DIEELEEIEE DAGLGNGGLG RLAACFLDSM ATLGLAAYGY GIRYEYGIFN QKIRDGWQVE EADDWLRYGN PWEKSRPEFM LPVHFYGKVE HTNTGTKWID TQVVLALPYD TPVPGYMNNT VNTMRLWSAR APNDFNLRDF NVGDYIQAVL DRNLAENISR VLYPNDNFFE GKELRLKQEY FVVAATLQDI IRRFKASKFG STRGAGTVFD AFPDQVAIQL NDTHPALAIP ELMRIFVDIE KLPWSKAWEL TQKTFAYTNH TVLPEALERW PVDLVEKLLP RHLEIIYEIN QKHLDRIVAL FPKDVDRLRR MSLIEEEGSK RINMAHLCIV GSHAVNGVAK IHSDIVKTKV FKDFSELEPD KFQNKTNGIT PRRWLLLCNP GLAELIAEKI GEDYVKDLSQ LTKLHSFLGD DVFLRELAKV KQENKLKFSQ FLETEYKVKI NPSSMFDVQV KRIHEYKRQL LNCLHVITMY NRIKKDPKKL FVPRTVIIGG KAAPGYHMAK MIIKLITSVA DVVNNDPMVG SKLKVIFLEN YRVSLAEKVI PATDLSEQIS TAGTEASGTG NMKFMLNGAL TIGTMDGANV EMAEEAGEEN LFIFGMRIDD VAALDKKGYE AKEYYEALPE LKLVIDQIDN GFFSPKQPDL FKDIINMLFY HDRFKVFADY EAYVKCQDKV SQLYMNPKAW NTMVLKNIAA SGKFSSDRTI KEYAQNIWNV EPSDLKISLS NESNKVNGN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FTCD HumanDescription:
Formiminotransferase Cyclodeaminase Human Recombinant
Formiminotransferase-cyclodeaminase, FTCD, LCHC1, LC-1.
Product # :
ENZ-302Price :
Quantity :
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Shipped with Ice Packs
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Description
Formiminotransferase Cyclodeaminase Human Recombinant (also called liver cytosol type 1) produced in SF9, is a glycosylated, polypeptide chain having a molecular mass of 59,749 Dalton.The FTCD is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
FTCD is supplied in 16mM HEPES buffer pH-7.6, 240mM sodium chloride, and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Formiminotransferase cyclodeaminase is an enzyme which catalyzes the conversion of formiminoglutamateand tetrahydrofolateinto formiminotetrahydrofolateand glutamate.
Formiminotransferase cyclodeaminase, a bifunctional enzyme of tetrahydrofolate synthesis, is the target antigen of anti-LC1 (liver cytosol antigen type 1) autoantibodies. Presence of LC1 autoantibodies is a marker for type 2 autoimmune hepatitis (for which anti-LKM 1/cytochrome P450 2D6 autoantibodies are a further marker).
Serum LC1 autoantibody concentrations appear to fluctuate in parallel with aminotransferase levels, a particularly intriguing observation that suggests a possible role of LC1 autoreactivity in the pathogenic mechanism leading to hepatocyte injury. -
Synonyms
Formiminotransferase-cyclodeaminase, FTCD, LCHC1, LC-1.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°Cfor longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels, immuno-dot test).
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coating concentration
0.35-0.7 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2L3 Human HisDescription:
Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant, His Tag
Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.
Product # :
ENZ-344Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.coli is an 18.9 kDa protein containing 162 amino acids.The UBE2L3 protein contains 6xHis tag and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated (1 mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Human Ubquitin Conjugating Enzyme 7 (UbcH7) is a class I enzyme which functions in the stress response and the control of transcription factors. The enzyme is ubiquitously expressed with high levels of expression seen in adult muscle. UbcH7 mediates the selective degradation of short-lived and abnormal proteins and is highly homologous to UbcH5. It has been demonstrated to participate in the ubiquitinylation of p53, c-Fos and NF-?B. UbcH7 is one of two E2s (UbcH5 being the other) with which HECT domain proteins interact with UbcH7 being able to efficiently substitute for UbcH5 in E6-AP-dependent ubiquitinylation.
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Synonyms
Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized UBE2L3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2L3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized UBE2L3 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHHHHHHAMAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVP
DNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAEN
WKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFT
KKYGEKRPVD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MPI HumanDescription:
Mannose Phosphate Isomerase Human Recombinant
Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.
Product # :
ENZ-169Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MPI Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 382 amino acids (1-362) and having a molecular mass of 41.9 kDa.The MPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MPI solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MPI is a member of the mannose-6-phosphate isomerase type 1 family. Although MPI is expressed in all tissues, it can be found more abundantly in heart, brain and skeletal muscle. Localized to the cytoplasm, MPI exploits zinc as a cofactor and catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate. Mutations in the MPI gene are the cause of carbohydrate-deficient glycoprotein syndrome, type Ib.
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Synonyms
Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAPRVFPLS CAVQQYAWGK MGSNSEVARL LASSDPLAQI AEDKPYAELW MGTHPRGDAK ILDNRISQKT LSQWIAENQD SLGSKVKDTF NGNLPFLFKV LSVETPLSIQ AHPNKELAEK LHLQAPQHYP DANHKPEMAI ALTPFQGLCG FRPVEEIVTF LKTAAGNNME DIFGELLLQL HQQYPGDIGC FAIYFLNLLT LKPGEAMFLE ANVPHAYLKG DCVECMACSD NTVRAGLTPK FIDVPTLCEM LSYTPSSSKD RLFLPTRSQE DPYLSIYDPP VPDFTIMKTE VPGSVTEYKV LALDSASILL MVQGTVIAST PTTQTPIPLQ RGGVLFIGAN ESVSLKLTEP KDLLIFRACC LL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PAP HumanDescription:
Prostate Acid Phosphatase Human
Product # :
ENZ-1171Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Prostate Acid Phosphatase produced in Pooled human seminal fluid having a molecular mass of approximately 100kD.
Source
Pooled human seminal fluid.
Formulation
PAP Human is lyophilized (0.2 µm filtered) from 0.02M NH4HCO3.
Purity
Greater than 96.0% as determined by SDS-PAGE.
More Info
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Introduction
Prostatic acid phosphatase, also known as PAP, is an enzyme produced by the prostate. PAP may be found in increased amounts in men with prostate cancer.
PAP’s physiological function may be associated with the liquefaction process of semen.
The highest levels of PAP are found in metastasized prostate cancer. Diseases of the bone, such as Paget's disease or hyperparathyroidism, diseases of blood cells (sickle-cell disease) or multiple myeloma or lysosomal storage diseases (Gaucher's disease), will show moderately higher levels.
Certain medications can cause temporary changes in PAP levels. Manipulation of the prostate gland through rectal exam, biopsy or massage may increase the level. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
PAP Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized PAP Human in phosphate buffer containing 0.15M NaCl.
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Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, Hepatitis C antibodies and Syphilis.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PHPT1 Human, ActiveDescription:
Phosphohistidine Phosphatase 1 Human Recombinant, Active
PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.
Product # :
ENZ-1041Price :
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Shipped with Ice Packs
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Description
PHPT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-125a.a.) and having a molecular mass of 15.9kDa.PHPT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PHPT1 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >120 units/mg, and is defined as the amount of enzyme that hydrolyze 1nmol f p-nitrophenyl phosphate per minute at pH7.5 at 37°C.
More Info
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Introduction
PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.
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Synonyms
PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW ANDGY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KMT5A HumanDescription:
Lysine Methyltransferase 5A Human Recombinant
KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.
Product # :
ENZ-1080Price :
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Shipped with Ice Packs
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Description
KMT5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (195-352 a.a.) and having a molecular mass of 18.9kDa (Migrates at 18-28 kDa on SDS-PAGE under reducing conditions).KMT5A is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KMT5A protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 5mM DTT, 0.2M NaCl, 1mM EDTA and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Lysine Methyltransferase 5A (KMT5A) is an enzyme which catalyzes both histones and non-histone proteins. KMT5A contributes to the maintenance of proper higher-order structure of DNA during mitosis. KMT5A takes part in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. KMT5A plays a role as a barrier to prevent cellular senescence through chromatinmediated regulation of senescence-associated metabolic remodeling. KMT5A mediates monomethylation of p53/TP53 at 'Lys-382', which leads to repress p53/TP53-target genes. The loss of KMT5A simultaneously stimulate nucleolar function and retinoblastoma protein-mediated mitochondrial metabolism.
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Synonyms
KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MKAELQSEER KRIDELIESG KEEGMKIDLI DGKGRGVIAT KQFSRGDFVV EYHGDLIEIT DAKKREALYA QDPSTGCYMY YFQYLSKTYC VDATRETNRL GRLINHSKCG NCQTKLHDID GVPHLILIAS RDIAAGEELL YDYGDRSKAS IEAHPWLKHH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2Z HumanDescription:
Ubiquitin Conjugating Enzyme E2Z Human Recombinant
HOYS7, USE1, Ubiquitin-conjugating enzyme E2 Z, E2 ubiquitin-conjugating enzyme Z, Uba6-specific E2 conjugating enzyme 1, Ubiquitin carrier protein Z, Ubiquitin-protein ligase Z, UBE2Z.
Product # :
ENZ-804Price :
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Description
UBE2Z Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-246a.a) and having a molecular mass of 30.5kDa. UBE2Z is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2Z solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitin Conjugating Enzyme E2Z, also known as UBE2z, is a protein coding gene which is a part of the ubiquitin-conjugating enzyme family. UBE2z catalyzes the covalent attachment of ubiquitin to various proteins. UBE2z takes part in in apoptosis regulation and is also a specific substrate for UBA6, not charged with ubiquitin by UBE1.
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Synonyms
HOYS7, USE1, Ubiquitin-conjugating enzyme E2 Z, E2 ubiquitin-conjugating enzyme Z, Uba6-specific E2 conjugating enzyme 1, Ubiquitin carrier protein Z, Ubiquitin-protein ligase Z, UBE2Z.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSIYKEP PPGMFVVPDT VDMTKIHALI TGPFDTPYEG GFFLFVFRCP PDYPIHPPRV KLMTTGNNTV RFNPNFYRNG KVCLSILGTW TGPAWSPAQS ISSVLISIQS LMTENPYHNE PGFEQERHPG DSKNYNECIR HETIRVAVCD MMEGKCPCPE PLRGVMEKSF LEYYDFYEVA CKDRLHLQGQ TMQDPFGEKR GHFDYQSLLM RLGLIRQKVL ERLHNENAEM DSDSSSSGTE TDLHGSLRV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Luciferase FireflyDescription:
Luciferin 4-Monooxygenase Firefly Recombinant
Luciferase-like monooxygenase, LUC, EC 1.13.12.7.
Product # :
ENZ-553Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-550 a.a.) and having a molecular mass of 62.9kDa.Luciferase is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Luciferase protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.
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Synonyms
Luciferase-like monooxygenase, LUC, EC 1.13.12.7.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMEDAKNIKK GPAPFYPLED GTAGEQLHKA MKRYALVPGT IAFTDAHIEV DITYAEYFEM SVRLAEAMKR YGLNTNHRIV VCSENSLQFF MPVLGALFIG VAVAPANDIY NERELLNSMG ISQPTVVFVS KKGLQKILNV QKKLPIIQKI IIMDSKTDYQ GFQSMYTFVT SHLPPGFNEY DFVPESFDRD KTIALIMNSS GSTGLPKGVA LPHRTACVRF SHARDPIFGN QIIPDTAILS VVPFHHGFGM FTTLGYLICG FRVVLMYRFE EELFLRSLQD YKIQSALLVP TLFSFFAKST LIDKYDLSNL HEIASGGAPL SKEVGEAVAK RFHLPGIRQG YGLTETTSAI LITPEGDDKP GAVGKVVPFF EAKVVDLDTG KTLGVNQRGE LCVRGPMIMS GYVNNPEATN ALIDKDGWLH SGDIAYWDED EHFFIVDRLK SLIKYKGYQV APAELESILL QHPNIFDAGV AGLPDDDAGE LPAAVVVLEH GKTMTEKEIV DYVASQVTTA KKLRGGVVFV DEVPKGLTGK LDARKIREIL IKAKKGGKIA V.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LysostaphinDescription:
Lysostaphin Recombinant
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
Product # :
ENZ-269Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without any additives.
Purity
98% as determined by RP-HPLC.
Biological Activity
Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C. Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.
More Info
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Introduction
Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.
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Synonyms
Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.
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Protein content
Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.
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Specific Activity
Determined to be 3,540 units/mg.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ACPP MouseDescription:
Acid Phosphatase Prostate Mouse Recombinant
acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.
Product # :
ENZ-1157Price :
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Shipped with Ice Packs
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Description
ACPP Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (32-381 aa) and having a molecular mass of 41.3kDa.ACPP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The ACPP solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >80,000 unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.
More Info
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Introduction
Prostatic Acid Phosphatase or ACPP is part of a family of proteins called histidine acid phosphatase. ACPP enhances the hydrolyzation of many phosphate monoesters and proteins that are phosphorylated. In order to function best, ACPP needs a range of range of 4-6 pH, furthermore, L(+)-tartrate inhibits ACPP’s catalyzation. This enzyme can act as a lipid phosphatase as well and can inhibit lysophosphatidic acid in seminal plasma.
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Synonyms
acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
KELKFVTLVF RHGDRGPIET FPTDPITESS WPQGFGQLTQ WGMEQHYELG SYIRKRYGRF LNDTYKHDQI YIRSTDVDRT LMSAMTNLAA LFPPEGISIW NPRLLWQPIP VHTVSLSEDR LLYLPFRDCP RFEELKSETL ESEEFLKRLH PYKSFLDTLS SLSGFDDQDL FGIWSKVYDP LFCESVHNFT LPSWATEDAM IKLKELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILKNMK LATQPQKYKK LVMYSAHDTT VSGLQMALDV YNGVLPPYAS CHMMELYHDK GGHFVEMYYR NETQNEPYPL TLPGCTHSCP LEKFAELLDP VISQDWATEC MATSSHQGRN HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2W HumanDescription:
Ubiquitin Conjugating Enzyme E2W Human Recombinant
Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.
Product # :
ENZ-117Price :
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Shipped with Ice Packs
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Description
UBE2W produced in E.Coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (1-151 a.a.) and having a molecular mass of 19.5kDa.UBE2W is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2W solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
UBE2W receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2W catalyzes monoubiquitination and 'Lys-11'-linked polyubiquitination. UBE2W is broadly expressed, particularly at highest levels in the testis.
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Synonyms
Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
UBE2W Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DIMT1 HumanDescription:
DIM1 Dimethyladenosine Transferase 1 Human Recombinant
Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.
Product # :
ENZ-628Price :
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Shipped with Ice Packs
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Description
DIMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-313) and having a molecular mass of 37.5kDa.DIMT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DIMT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 30% glycerol, 2mM DTT, 200mM NaCl and 2mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.
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Synonyms
Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMPKVKSGAI GRRRGRQEQR RELKSAGGLM FNTGIGQHIL KNPLIINSII DKAALRPTDV VLEVGPGTGN MTVKLLEKAK KVVACELDPR LVAELHKRVQ GTPVASKLQV LVGDVLKTDL PFFDTCVANL PYQISSPFVF KLLLHRPFFR CAILMFQREF ALRLVAKPGD KLYCRLSINT QLLARVDHLM KVGKNNFRPP PKVESSVVRI EPKNPPPPIN FQEWDGLVRI TFVRKNKTLS AAFKSSAVQQ LLEKNYRIHC SVHNIIIPED FSIADKIQQI LTSTGFSDKR ARSMDIDDFI RLLHGFNAEG IHFS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2S HumanDescription:
Ubiquitin Conjugating Enzyme E2S Human Recombinant
Ubiquitin-conjugating enzyme E2 S, Ubiquitin-protein ligase S, Ubiquitin carrier protein S, Ubiquitin-conjugating enzyme E2-24 kDa, E2-EPF5, E2-EPF, UBE2S, E2EPF, EPF5.
Product # :
ENZ-444Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
UBE2S Human Recombinant fused with a 36 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 258 amino acids (1-222 a.a.) and having a molecular mass of 27.9kDa.The UBE2S is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2S solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitin-conjugating enzyme E2S (UBE2S) belongs to the ubiquitin-conjugating enzyme family. UBE2S is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme-dependent manner, a typical property of ubiquitin carrier proteins. UBE2S catalyzes the covalent attachment of ubiquitin to other proteins. UBE2S acts as a crucial factor of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by purposely elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, augmenting the degradation of APC/C substrates by the proteasome and promoting mitotic exit. UBE2S also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is nevertheless uncertain whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and consequent degradation of VHL, resulting in an accumulation of HIF1A.
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Synonyms
Ubiquitin-conjugating enzyme E2 S, Ubiquitin-protein ligase S, Ubiquitin carrier protein S, Ubiquitin-conjugating enzyme E2-24 kDa, E2-EPF5, E2-EPF, UBE2S, E2EPF, EPF5.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNSN VENLPPHIIR LVYKEVTTLT ADPPDGIKVF PNEEDLTDLQ VTIEGPEGTP YAGGLFRMKL LLGKDFPASP PKGYFLTKIF HPNVGANGEI CVNVLKRDWT AELGIRHVLL TIKCLLIHPN PESALNEEAG RLLLENYEEY AARARLLTEI HGGAGGPSGR AEAGRALASG TEASSTDPGA PGGPGGAEGP MAKKHAGERD KKLAAKKKTD KKRALRRL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DECR2 HumanDescription:
2,4-Dienoyl CoA Reductase 2 Human Recombinant
Peroxisomal 2,4-dienoyl-CoA reductase, pDCR, 2,4-dienoyl-CoA reductase 2, DECR2, PDCR, SDR17C1.
Product # :
ENZ-211Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
- purity
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Description
DECR2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 33.2kDa.DECR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DECR2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Peroxisomal 2,4-dienoyl-CoA reductase (DECR2) is an supporting enzyme of beta-oxidation. DECR2 partakes in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. DECR2 catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
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Synonyms
Peroxisomal 2,4-dienoyl-CoA reductase, pDCR, 2,4-dienoyl-CoA reductase 2, DECR2, PDCR, SDR17C1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQPPPD VEGDDCLPAY RHLFCPDLLR DKVAFITGGG SGIGFRIAEI FMRHGCHTVI ASRSLPRVLT AARKLAGATG RRCLPLSMDV RAPPAVMAAV DQALKEFGRI DILINCAAGN FLCPAGALSF NAFKTVMDID TSGTFNVSRV LYEKFFRDHG GVIVNITATL GNRGQALQVH AGSAKAAVDA MTRHLAVEWG PQNIRVNSLA PGPISGTEGL RRLGGPQASL STKVTASPLQ RLGNKTEIAH SVLYLASPLA SYVTGAVLVA DGGAWLTFPN GVKGLPDFAS FSAKL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.