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Search results

1000 results found for “Trypsin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Y.Enterocolitica (O:9) YopH

    Description:

    Yersinia Enterocolitica (O:9) YopH Recombinant

    Product # :

    PRO-2275

    Price :

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    Description

    Recombinant Yersinia Enterocolitica (O:9) YopH produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 52,311 Dalton. Y.Enterocolitica (O:9) YopH is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Y.Enterocolitica (O:9) YopH is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.

    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.

    Yenterocolitica O 9 Yoph
  • View Data Sheet

    Name :

    C.Albicans Enolase

    Description:

    Candida Albicans Enolase Recombinant

    Product # :

    PRO-2297

    Price :

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    Description

    Recombinant Candida Albicans Enolase produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. C.Albicans Enolase is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    C.Albicans Enolase is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Candida albicans is a diploid fungus, which grows both as yeast and filamentous cells and a contributory agent of opportunistic oral and genital infections in humans, and candidal onychomycosis (an infection of the nail plate). Systemic fungal infections (fungemias) including those by C. albicans are regarded as key causes of morbidity and mortality in immunocompromised patients (e.g., AIDS, cancer chemotherapy, organ or bone marrow transplantation). C. albicans biofilms may develop on the surface of implantable medical devices. C. albicans is commensal and a constituent of the normal gut flora containing microorganisms which live in the human mouth and gastrointestinal tract. Overgrowth of the fungus leads to in candidiasis (candidosis). Candidiasis is frequently detected in immunocompromised persons, including HIV-infected patients. To infect host tissue, the habitual unicellular yeast-like form of C. albicans reacts to environmental signals and changes into an invasive, multicellular filamentous form, a phenomenon which is known as dimorphism.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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. Avoid multiple 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.

    Calbicans Enolase
  • View Data Sheet

    Name :

    Gly m 4.0101

    Description:

    Stress-Induced Protein SAM22 Recombinant

    Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    Product # :

    PRO-2278

    Price :

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    Description

    Recombinant Stress-Induced Protein SAM22 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 19,484 Dalton. Gly m 4.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Gly m 4.0101 is supplied in in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.

    • Synonyms

      Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Gly M 40101
  • View Data Sheet

    Name :

    BPNT1 Human

    Description:

    3(2) 5-Bisphosphate Nucleotidase 1 Human Recombinant

    3'(2'), 5'-bisphosphate nucleotidase 1, Bisphosphate 3'-nucleotidase 1, PAP-inositol-1,4-phosphatase, PIP, EC 3.1.3.7, BPntase.

    Product # :

    ENZ-061

    Price :

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    Description

    BPNT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-308a.a.) and having a molecular mass of 37.5kDa.BPNT1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BPNT1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 5mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      BPNT1 belongs to the magnesium-dependent, lithium-sensitive phosphomono-esterase superfamily. BPNT1 catalyzes the conversion of PAPS (adenosine 3'-phosphate 5' phosphosulfate) to APS (adenosine 5'-phosphosulfate) and the conversion of PAP (3'(2')-phosphoadenosine 5' phosphate) to AMP (adenosine 5'-phosphate) using magnesium as a cofactor. BPNT1 is expressed everywhere but at maximum levels in brain and kidney. BPNT1 is potently inhibited by lithium, a drug used for the treatment of manic depression and bipolar affective disorder, which suggests that BPNT1 has a possible role in the etiology of mood disorders.

    • Synonyms

      3'(2'), 5'-bisphosphate nucleotidase 1, Bisphosphate 3'-nucleotidase 1, PAP-inositol-1,4-phosphatase, PIP, EC 3.1.3.7, BPntase.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS NTVLMRLVAS AYSIAQKAGM IVRRVIAEGD LGIVEKTCAT DLQTKADRLA QMSICSSLAR KFPKLTIIGE EDLPSEEVDQ ELIEDSQWEE ILKQPCPSQY SAIKEEDLVV WVDPLDGTKE YTEGLLDNVT VLIGIAYEGK AIAGVINQPY YNYEAGPDAV LGRTIWGVLG LGAFGFQLKE VPAGKHIITT TRSHSNKLVT DCVAAMNPDA VLRVGGAGNK IIQLIEGKAS AYVFASPGCK KWDTCAPEVI LHAVGGKLTD IHGNVLQYHK DVKHMNSAGV LATLRNYDYY ASRVPESIKN ALVP

    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.

    Bpnt1 Human
  • View Data Sheet

    Name :

    ABHD10 Human

    Description:

    Abhydrolase Domain Containing 10 Human Recombinant

    Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.

    Product # :

    ENZ-612

    Price :

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    Description

    ABHD10 Human Recombinant produced in E. coli is a single polypeptide chain containing 279 amino acids (53-306) and having a molecular mass of 30.9kDa.ABHD10 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ABHD10 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Abhydrolase domain-containing protein 10 (ABHD10) is a member of the AB hydrolase superfamily.

    • Synonyms

      Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMTSLSF LNRPDLPNLA YKKLKGKSPG IIFIPGYLSY MNGTKALAIE EFCKSLGHAC IRFDYSGVGS SDGNSEESTL GKWRKDVLSI IDDLADGPQI LVGSSLGGWL MLHAAIARPE KVVALIGVAT AADTLVTKFN QLPVELKKEV EMKGVWSMPS KYSEEGVYNV QYSFIKEAEH HCLLHSPIPV NCPIRLLHGM KDDIVPWHTS MQVADRVLST DVDVILRKHS DHRMREKADI QLLVYTIDDL IDKLSTIVN

    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.

    Abhd10 Human
  • View Data Sheet

    Name :

    SERPINC1 Human, Sf9

    Description:

    Serpin Peptidase Inhibitor, Clade C Member 1 Human Recombinant, Sf9

    SERPINC1, AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1.

    Product # :

    PRO-2541

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    Description

    SERPINC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (33-464a.a.) and having a molecular mass of 50.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). SERPINC is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SERPINC protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serpin Peptidase Inhibitor, Clade C Member 1 (SERPINC1), which is a part of the serpin superfamily, is a plasma protease inhibitor. SERPINC1 inhibits thrombin and other activated serine proteases of the coagulation system, and regulates the blood coagulation cascade. SERPINC1 also inhibits Thrombin and Factors IXa, Xa and XIa. Deficiencies in SERPINC1 can cause ATIII deficiency, an autosomal dominant disease which might lead to a hereditary thrombophilia.

    • Synonyms

      SERPINC1, AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      ADPHGSPVDI CTAKPRDIPM NPMCIYRSPE KKATEDEGSE QKIPEATNRR VWELSKANSR FATTFYQHLA DSKNDNDNIF LSPLSISTAF AMTKLGACND TLQQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SKLVSANRLF GDKSLTFNET YQDISELVYG AKLQPLDFKE NAEQSRAAIN KWVSNKTEGR ITDVIPSEAI NELTVLVLVN TIYFKGLWKS KFSPENTRKE LFYKADGESC SASMMYQEGK FRYRRVAEGT QVLELPFKGD DITMVLILPK PEKSLAKVEK ELTPEVLQEW LDELEEMMLV VHMPRFRIED GFSLKEQLQD MGLVDLFSPE KSKLPGIVAE GRDDLYVSDA FHKAFLEVNE EGSEAAASTA VVIAGRSLNP NRVTFKANRP FLVFIREVPL NTIIFMGRVA NPCVKHHHHH H.

    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.

    Serpinc1 Protein 2
  • View Data Sheet

    Name :

    BLVRB Mouse

    Description:

    Biliverdin Reductase B Mouse Recombinant

    Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.

    Product # :

    ENZ-1074

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    Description

    BLVRB Mouse Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-206 a.a) and having a molecular mass of 24.6kDa.BLVRB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BLVRB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.

    • Synonyms

      Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.

    • Physical Appearance

      Sterile filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTVKKIA IFGATGRTGL TTLAQAVQAG YEVTVLVRDS SRLPSEGPQP AHVVVGDVRQ AADVDKTVAG QEAVIVLLGT GNDLSPTTVM SEGTRNIVTA MKAHGVDKVV ACTSAFLLWD PTKVPPRLQD VTDDHIRMHK ILQESGLKYV AVMPPHIGDQ PLTGAYTVTL DGRGPSRVIS KHDLGHFMLR CLTTNEYDGH TTYPSHQYD.

    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.

    Blvrb Mouse
  • View Data Sheet

    Name :

    TPM2 Human

    Description:

    Tropomyosin-2 Human Recombinant

    Tropomyosin 2 (beta), DA1, TMSB, DA2B, AMCD1, NEM4, Arthrogryposis Multiplex Congenital Distal-Type 1, beta-Tropomyosin.

    Product # :

    PRO-069

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    Description

    TPM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-284a.a.) and having a molecular mass of 35.1kDa(molecular weight on SDS-PAGE will appear higher).TPM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPM2 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tropomyosin beta chain isoform 2 is affiliate to the actin filament binding protein family which primarily expressed in slow, type 1 muscle fibers. Mutations in TPM2 can change the expression of other sarcomeric tropomyosin proteins, and cause cap disease, nemaline myopathy and distal arthrogryposis syndromes.

    • Synonyms

      Tropomyosin 2 (beta), DA1, TMSB, DA2B, AMCD1, NEM4, Arthrogryposis Multiplex Congenital Distal-Type 1, beta-Tropomyosin.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL KGTEDEVEKY SESVKEAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAMKDEEK MELQEMQLKE AKHIAEDSDR KYEEVARKLV ILEGELERSE ERAEVAESRA RQLEEELRTM DQALKSLMAS EEEYSTKEDK YEEEIKLLEE KLKEAETRAE FAERSVAKLE KTIDDLEETL ASAKEENVEI HQTLDQTLLE LNNL.

    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.

    Tpm2 Human
  • View Data Sheet

    Name :

    CBR3 Human

    Description:

    Carbonyl Reductase-3 Human Recombinant

    Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.

    Product # :

    ENZ-428

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    Description

    Recombinant Human CBR3 fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-277 a.a) and having a molecular mass of 33kDa. CBR3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CBR3 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy.
      CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis.

    • Synonyms

      Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP MPFDIKAEMT LKTNFFATRN MCNELLPIMK PHGRVVNISS LQCLRAFENC SEDLQERFHS ETLTEGDLVD LMKKFVEDTK NEVHEREGWP NSPYGVSKLG VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS IRTVEEGAET PVYLALLPPD ATEPQGQLVH DKVVQNW.

    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.

    Cbr3 Human
  • View Data Sheet

    Name :

    UBE2N Human

    Description:

    Ubiquitin Conjugating Enzyme E2N Human Recombinant

    Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU, MGC8489, UbcH-ben, MGC131857.

    Product # :

    ENZ-104

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    Description

    UBE2N produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-152a.a.) and having a molecular mass of 19.3kDa.UBE2N is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2N solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2N belongs to the E2 ubiquitin-conjugating enzyme family. UBE2N catalyzes the ATP-dependent synthesis of non-canonical polyubiquitin chains, a process which doesn’t set in motion proteasomal degradation. UBE2N mediates the transcription of some target genes and is believed to have a role in cell cycle progression; cellular differentiation and DNA repair mechanisms which ensure cell survival after DNA damage.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU, MGC8489, UbcH-ben, MGC131857.

    • Physical Appearance

      Sterile filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI.

    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.

    Ube2N Human
  • View Data Sheet

    Name :

    TNNI3 Human

    Description:

    Cardiac Troponin I Human Recombinant

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    Product # :

    PRO-324

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    Description

    Recombinant Human TNNI3 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 210 amino acids having an additional methionine residue at N-terminus
    The TNNI3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human TNNI3 was lyophilized in 0.01M HCl.

    Purity

    Greater than 95.0% as determined by both SDS-PAGE.

    More Info

    • Introduction

      Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI is acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and is exclusively expressed in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNNI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cardiac Troponin I 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.

    • Solubility

      It is recommended to reconstitute the lyophilized TNNI3 with urea /Tris buffer (20mM Tris, pH 7.5, 5 mM EDTA, 7 M urea and 15 mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQ
      IAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEE
      RYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKE
      SLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES.

    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.

    Tnni3 Human
  • View Data Sheet

    Name :

    Treponema Mosaic

    Description:

    Treponema pallidum Mosaic Recombinant

    Product # :

    TRP-276

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    Description

    Recombinant Treponema pallidum Mosaic contains TP15, TP17 & TP47 epitopes containing 382 a.a. produced in E.Coli and fused to a 6xHis tag at C-terminus. The total Mw is 38kDa and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Treponema Mosaic protein solution contains 1x PBS & 25mM K2CO3.

    Purity

    Treponema Mosaic is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      Treponema Mosaic protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Immunoassay.

    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.

    Treponema Mosaic
  • View Data Sheet

    Name :

    Treponema TP0453

    Description:

    Outer Membrane Protein Treponema pallidum Recombinant

    Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453

    Product # :

    TRP-255

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    Description

    Recombinant Treponema pallidum Outer Membrane Protein TP0453 has a Mw of 26kDa, and was purified from E. coli.The Recombinant Treponema pallidum Outer Membrane Protein TP0453 is fused to 6 amino acid His tag at its C terminal and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Treponema TP0453 solution contains 25mM K2CO3 with PBS.

    Purity

    Protein is >95% pure as determined by SDS-PAGE (coomassie staining).

    More Info

    • Introduction

      Tp0453 is a carrier of lipids and glycolipids during outer membrane. Tp045 is hypothesized to be a new type of bacterial outer membrane protein, which reduces T.pallidum outer membrane permeability to nutrients while remaining inaccessible to antibodies. Tp0453 exhibited 100% specificity and sensitivity in reaction with syphilis patients’ sera, giving negative result with Lyme disease, relapsing-fever or leptospirosis patients’ sera.

    • Synonyms

      Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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.

    • Applications

      Rapid test, Immunoassay.

    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.

    Tp0453 Treponema
  • View Data Sheet

    Name :

    Gliadin Alpha Wheat

    Description:

    Gliadin Alpha Wheat Recombinant

    Product # :

    PRO-2147

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    Description

    Recombinant Wheat Gliadin Alpha protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 34557.64 Dalton, pI 7.70. Purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Gliadin Alpha protein solution in 10mM Tris-HCl pH 7.2.

    Purity

    Protein is >90% pure.

    More Info

    • Introduction

      Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Gliadin Alpha although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MVRVPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQPFPPQQPYPQPQPFPSQQPYLQ
      LQPFPQPQLPYPQPQLPYPQPQLPYPQPQPFRPQQPYPQSQPQYSQPQQPISQQQQQQQQ
      QQQQKQQQQQQQQILQQILQQQLIPCRDVVLQQHSIAYGSSQVLQQSTYQLVQQLCCQQL
      WQIPEQSRCQAIHNVVHAIILHQQQQQQQQQQQQPLSQVSFQQPQQQYPSGQGSFQPSQ
      QNPQAQGSVQPQQLPQFEEIRNLALETLPAMCNVYIPPYCTIAPVGIFGTNYRHHHHHH.

    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.

    Gliadin Alpha Wheat
  • View Data Sheet

    Name :

    TnT Human

    Description:

    Cardiac Troponin T Human

    Troponin T cardiac muscle, TnTc, Cardiac muscle troponin T, cTnT, TNNT2, CMH2, CMPD2, MGC3889.

    Product # :

    PRO-342

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    Description

    Human Cardiac Troponin T produced from Human Cardiac Tissue, having a molecular weight of approximately 35 kDa.
    The Cardiac troponin-T is Immunogen for troponin biochemical, antibody production and immunochemical studies.

    Source

    Human skeletal muscle.

    Formulation

    Human Cardiac Troponin was lyophilized in 0.01 M HCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.


    More Info

    • Introduction

      Troponin-T is one of three subunits that form the troponin complex of the thin filaments of striated muscle, it regulates muscle contraction in response to alterations in intracellular calcium ion concentration. TnTc is expressed only in the heart and has proved to be a specific biomarker for heart disease.
      Mutations in TNNT2 are associated with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy.
      Alternative splicing results in many tissue-specific isoforms.

    • Synonyms

      Troponin T cardiac muscle, TnTc, Cardiac muscle troponin T, cTnT, TNNT2, CMH2, CMPD2, MGC3889.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TnT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cardiac Troponin T 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.

    • Solubility

      It is recommended to reconstitute the lyophilized TnT with urea /Tris buffer (20mM Tris, pH 7.5, 5 mM EDTA, 7 M urea and 15 mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      Blood sample from the tissue donor was tested and found negative for HBsAg, HIV-1 and HIV-2 antibodies, HCV, 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.

    Troponin T Human
  • View Data Sheet

    Name :

    GST-HRP Antibody

    Description:

    Glutathione-S-Transferase, Mouse Antibody Peroxidase Conjugated

    Product # :

    ANT-220

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    Description

    Monoclonal antibodies are produced by immunizing mouse with GST protein.

    Formulation

    1×PBS & 50% glycerol.

    More Info

    • Introduction

      GST family of enzymes comprises a long list of cytosolic, mitochondrial, and microsomal proteins that are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenous and xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called 'GST gene fusion system'. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's multiple cloning sites results in expression of a fusion protein - the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. Fusion proteins offer an important biological assay for direct protein-to-protein interactions. The GST tag has the size of 220 amino acids, which, compared to other tags like the myc- or the FLAG-tag, is quite big. It is fused to the N-terminus of a protein. However, many commercially-available sources of GST-tagged plasmids include a thrombin domain for cleavage of the GST tag during protein purification. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.

    • Ig Subclass

      Mouse IgG2b.

    • Clone

      PGSTHRPSHG.

    • Applications

      Western Blot.

    • Titer

      Western Blotting: 1:1000.

    • Type

      Mouse Antibody Monoclonal.

    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.

    Gst Hrp Antibody
  • View Data Sheet

    Name :

    T.pallidum p15 (Partial), His

    Description:

    Treponema pallidum p15 (Partial) Recombinant, His Tag

    Product # :

    TRP-247

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    • sds-page

    Description

    The E.Coli derived recombinant 6xHis tag fusion protein is a multimer having a molecular mass of 15kDa and contains the Trp. Pallidum p15 immunodominant regions and six histidines fused at the C- terminus.

    Source

    Escherichia Coli.

    Formulation

    70mM Tris-HCl pH 8.0, 50mM NaCl, 50% Glycerol, 1.5 M Urea.

    Purity

    Treponema Pallidum protein is >95% pure as determined by SDS- PAGE.

    sds-page

    T.pallidum p15 (Partial), His sds-page - Product image 1

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Stability

      Treponema Pallidum protein should be stored at 2-8°C. Do NOT freeze.

    • Specificity

      Immunoreactive with sera of Trp. Pallidum infected individuals.

    • Purification Method

      Treponema Pallidum protein was purified by proprietary chromatographic technique.

    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.

    Tpallidum P15 His
  • View Data Sheet

    Name :

    Avidin Recombinant

    Description:

    Avidin Recombinant

    Avidin, AVD, AVID.

    Product # :

    PRO-2597

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    Description

    Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.

    Source

    Corn (Zea Mays).

    Purity

    Greater than 90% as visualized by SDS-PAGE.

    Biological Activity

    13.5 units/mg protein, 1 unit binds 1µg biotin.

    More Info

    • Introduction

      Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

    • Synonyms

      Avidin, AVD, AVID.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Recombinant Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant Avidin 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.

    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.

    Avidin Recombinant
  • View Data Sheet

    Name :

    ODC1 Human

    Description:

    Ornithine Decarboxylase 1 Human Recombinant

    ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

    Product # :

    ENZ-181

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    Description

    ODC1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 484 amino acids (1-461) and having a molecular mass of 53.5 kDa.ODC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ODC1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ornithine decarboxylase is the preliminary and rate-limiting enzyme in the biosynthetic pathway of polyamines and it takes part in the alteration of ornithine to putrescine. ODC1 is a key member of various biological processes, such as cell growth, transformation, differentiation and apoptosis. Overexpression of the ODC1 gene has a vital part in cell proliferation and the progress of cancer.

    • Synonyms

      ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMNNFGNE EFDCHFLDEG FTAKDILDQK INEVSSSDDK DAFYVADLGD ILKKHLRWLK ALPRVTPFYA VKCNDSKAIV KTLAATGTGF DCASKTEIQL VQSLGVPPER IIYANPCKQV SQIKYAANNG VQMMTFDSEV ELMKVARAHP KAKLVLRIAT DDSKAVCRLS VKFGATLRTS RLLLERAKEL NIDVVGVSFH VGSGCTDPET FVQAISDARC VFDMGAEVGF SMYLLDIGGG FPGSEDVKLK FEEITGVINP ALDKYFPSDS GVRIIAEPGR YYVASAFTLA VNIIAKKIVL KEQTGSDDED ESSEQTFMYY VNDGVYGSFN CILYDHAHVK PLLQKRPKPD EKYYSSSIWG PTCDGLDRIV ERCDLPEMHV GDWMLFENMG AYTVAAASTF NGFQRPTIYY VMSGPAWQLM QQFQNPDFPP EVEEQDASTL PVSCAWESGM KRHRAACASA SINV

    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.

    Odc1 Human
  • View Data Sheet

    Name :

    EOGT Mouse

    Description:

    EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase Mouse Recombinant

    EGF domain-specific O-linked N-acetylglucosamine transferase, Extracellular O-linked N-acetylglucosamine transferase.

    Product # :

    ENZ-946

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    Description

    EOGT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 516 amino acids (20-527 a.a.) and having a molecular mass of 60.4kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). EOGT is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EOGT protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase (EOGT) takes part in the regulation of Notch receptor. EOGT catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine/ threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). EOGT mainly glycosylates the Thr residue positioned between the fifth and sixth conserved cysteines of folded EGF-like domains.

    • Synonyms

      EGF domain-specific O-linked N-acetylglucosamine transferase, Extracellular O-linked N-acetylglucosamine transferase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      DKAHSEADDA PGKALYDYSS LRLPAEHIPF FLHNNRHVAS VCREDSHCPY KKHLENLNYC WGYEKSCAPE FRFGSPVCSY VDLGWTDTLE SAQDMFWRQA DFGYARERLG EIRTICQPER ASDSSLVCSR YLQYCRATGL YLDLRNIKRN HDRFKEDFLQ GGEIGGYCKL DSHALVSEGQ RKSPLQSWFA ELQGYTQLNF RPIEDAKCDI VVEKPTYFMK LDAGINMYHH FCDFLNLYLT QHVNNSFSTD VYIVMWDTST YGYGDLFSDT WKAFTDYDVI HLKTYDSKKV CFKEAVFSLL PRMRYGLFYN TPLISGCQNT GLFRAFSQHV LHRLNITQEG PKDGKVRVTI LARSTEYRKI LNQDELVNAL KTVSTFEVRV VDYKYRELGF LDQLRITHNT DIFIGMHGAG LTHLLFLPDW AAVFELYNCE DERCYLDLAR LRGIHYITWR KPSKVFPQDK GHHPTLGEHP KFTNYSFDVE EFMYLVLQAA EHVLQHPQWP FKKKHDELLE 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.

    Eogt Mouse
  • View Data Sheet

    Name :

    EPHX1 Human

    Description:

    Epoxide Hydrolase 1 Microsomal Human Recombinant

    Epoxide hydrolase 1, microsomal (xenobiotic), MEH, EPHX, EPOX, Epoxide hydratase, Microsomal epoxide hydrolase.

    Product # :

    ENZ-773

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    Description

    EPHX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 451 amino acids (21-455a.a) and having a molecular mass of 52.2kDa. EPHX1 is fused to a 16 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EPHX1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.

    • Synonyms

      Epoxide hydrolase 1, microsomal (xenobiotic), MEH, EPHX, EPOX, Epoxide hydratase, Microsomal epoxide hydrolase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • 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.

    • Amino Acid Sequence

      MASMTGGQQM GRGSHMRDKE ETLPLEDGWW GPGTRSAARE DDSIRPFKVE TSDEEIHDLH QRIDKFRFTP PLEDSCFHYG FNSNYLKKVI SYWRNEFDWK KQVEILNRYP HFKTKIEGLD IHFIHVKPPQ LPAGHTPKPL LMVHGWPGSF YEFYKIIPLL TDPKNHGLSD EHVFEVICPS IPGYGFSEAS SKKGFNSVAT ARIFYKLMLR LGFQEFYIQG GDWGSLICTN MAQLVPSHVK GLHLNMALVL SNFSTLTLLL GQRFGRFLGL TERDVELLYP VKEKVFYSLM RESGYMHIQC TKPDTVGSAL NDSPVGLAAY ILEKFSTWTN TEFRYLEDGG LERKFSLDDL LTNVMLYWTT GTIISSQRFY KENLGQGWMT QKHERMKVYV PTGFSAFPFE LLHTPEKWVR FKYPKLISYS YMVRGGHFAA FEEPELLAQD IRKFLSVLER Q.

    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.

    Ephx1 Human
  • View Data Sheet

    Name :

    PAPP-A Human

    Description:

    Pregnancy-Associated Plasma Protein-1 Human Recombinant

    Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.

    Product # :

    ENZ-441

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    Description

    PAPP-A Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 191 amino acids fragment (81-271) corresponding to the PAPP-A “Jelly-Roll” domain fragment, having a total molecular mass of 25.75kDa and fused with an amino-terminal hexahistidine tag. The PAPP-A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PAPP-A protein is supplied in 20mM Tris Hcl PH 8.0, 4M Urea and 50% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PAPPA is a large zinc binding protein, which acts as a metalloprotease and specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. PAPP-A can also act as a regulator of IGF bioactivity in a number of biological systems, including the human ovary and cardiovascular systems. It was shown that PAPP A levels are elevated in patients with unstable angina or acute myocardial infarction. Furthermore, PAPPA is believed to be involved in local proliferative processes such as wound healing and bone remodeling. Moreover, PAPP-A is produced in high concentrations during pregnancy and is released into the maternal circulation. In placenta, PAPP A is expressed in X cells in septa and anchoring villi, and in syncytiotrophoblasts in the chorionic villi.
      Lower levels of PAPPA are found in an array of other tissues including kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow, colon, fibroblasts and osteoblasts. PAPP-A is present in serum and placenta during pregnancy; with levels increasing throughout pregnancy. Low levels of PAPP A are associated with a number of foetal chromosomal abnormalities, as well as pre-eclampsia and stillbirth.
      PAPPA levels may be a potentially highly specific marker for heart disease.
      PAPP-A proteolytic activity is inhibited by targeting substrate exosite binding.

    • Synonyms

      Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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. Please avoid 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.

    Papp A Human
  • View Data Sheet

    Name :

    CA1 Human, Active

    Description:

    Carbonic Anhydrase-1 Human Recombinant, BioActive

    CA1, CA-I, CAB.

    Product # :

    ENZ-1137

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    Description

    CA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261) and having a molecular mass of 31.0 kDa. CA1 Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA1 Human protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 8.0 at 37C.

    More Info

    • Introduction

      CA, also known as carbonic anhydrase is an enzyme. Its main function revolves around the CO2 + H2O HCO3- + H+ (conversion of carbon dioxide to bicarbonate & protons). CA has a zinc ion in its active site. The main function of CA is to keep acid-base balance in the blood stream and various tissues. This enzyme also assists Carbonic Anhydrase I to move CO2 to and from tissues.

    • Synonyms

      CA1, CA-I, CAB.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.

    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.

    Ca1 Enzyme
  • View Data Sheet

    Name :

    TPO Human

    Description:

    Thyroid Peroxidase Human Recombinant

    Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    Product # :

    ENZ-285

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    Description

    Thyroid Peroxidase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing 834 amino acids and having a molecular mass of 92,872 Dalton (excluding glycosylation), 101 kDa total mass.The TPO is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TPO is supplied in 16mM HEPES pH-7.6, 160mM NaCl, 0.08mM Kl and 20% glycerol.

    Purity

    Greater than 95% as determined by Densitometric Analysis

    More Info

    • Introduction

      Thyroid Peroxidase (TPO) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. Its identity with the formerly so-called `microsomal antigen` has been shown several years ago. As an integral membrane glycoprotein it is restricted to the apical plasma membrane of the follicular epithelial cells and comprises two identical subunits of approx. 100 kDa molecular weight. The hemoprotein TPO plays a key role in the thyroid hormone biosynthesis by catalysing both the iodination of tyrosyl residues and the coupling of iodotyrosyl residues in thyroglobulin (TG) to form precursors of the thyroid hormones T4 and T3.

    • Synonyms

      Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    • 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. Avoid multiple freeze-thaw cycles.

    • coating concentration

      0.15-0.375 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.

    Thyroid Peroxidase Human
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