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Search results

1000 results found for “Endonuclease”

Name

Description

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  • View Data Sheet

    Name :

    SENP8 Human

    Description:

    Sentrin Specific Peptidase Family Member 8 Human Recombinant

    SUMO/sentrin specific peptidase family member 8, DEN1, NEDP1, Protease cysteine 2 (NEDD8 specific), PRSC2, NEDD8-specific protease 1, HsT17512, Deneddylase-1, NEDD8 specific-protease cysteine 2, Sentrin/SUMO-specific protease SENP8.

    Product # :

    ENZ-146

    Price :

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    Description

    SENP8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.2 kDa.The SENP8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SENP8 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SENP8 is a cysteine protease which belongs to the sentrin-specific protease family. SENP8 takes part in processing and deconjugation of the ubiquitin-like protein labeled, neural precursor cell expressed developmentally downregulated 8(NEDD8).

    • Synonyms

      SUMO/sentrin specific peptidase family member 8, DEN1, NEDP1, Protease cysteine 2
      (NEDD8 specific), PRSC2, NEDD8-specific protease 1, HsT17512, Deneddylase-1, NEDD8 specific-protease cysteine 2, Sentrin/SUMO-specific protease SENP8.

    • Physical Appearance

      SENP8 is supplied as a 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 MDPVVLSYMD SLLRQSDVSL LDPPSWLNDH IIGFAFEYFA NSQFHDCSDH VSFISPEVTQ FIKCTSNPAE IAMFLEPLDL PNKRVVFLAI NDNSNQAAGG THWSLLVYLQ DKNSFFHYDS HSRSNSVHAK QVAEKLEAFL GRKGDKLAFV EEKAPAQQNS YDCGMYVICN TEALCQNFFR QQTESLLQLL TPAYITKKRG EWKDLITTLA KK

    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.

    Senp8 Human
  • View Data Sheet

    Name :

    ECHDC1 Human

    Description:

    Enoyl CoA Hydratase Domain Containing 1 Human Recombinant

    Ethylmalonyl-CoA decarboxylase, Enoyl-CoA hydratase domain-containing protein 1, Methylmalonyl-CoA decarboxylase, MMCD, ECHDC1, dJ351K20.2.

    Product # :

    ENZ-573

    Price :

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    Description

    SNAP25 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-206 a.a.) and having a molecular mass of 25.4 kDa. SNAP25 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    E.coli.

    Formulation

    The ECHDC1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Enoyl CoA hydratase domain containing 1 (ECHDC1) is a member of the enoyl-CoA hydratase/isomerase family. ECHDC1 is an enzyme which hydrates the double bond between the second and third carbons on acyl-CoA. The ECHDC1 enzyme is crucial to metabolizing fatty acids to supply both acetyl CoA and energy.

    • Synonyms

      Ethylmalonyl-CoA decarboxylase, Enoyl-CoA hydratase domain-containing protein 1, Methylmalonyl-CoA decarboxylase, MMCD, ECHDC1, dJ351K20.2.

    • 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 MALKQEMAKS LLKTASLSGR TKLLHQTGLS LYSTSHGFYE EEVKKTLQQF PGGSIDLQKE DNGIGILTLN NPSRMNAFSG VMMLQLLEKV IELENWTEGK GLIVRGAKNT FSSGSDLNAV KSLGTPEDGM AVCMFMQNTL TRFMRLPLIS VALVQGWALG
      GGAEFTTACD FRLMTPESKI RFVHKEMGII PSWGGTTRLV EIIGSRQALK VLSGALKLDS KNALNIGMVE EVLQSSDETK SLEEAQEWLK QFIQGPPEVI RALKKSVCSG RELYLEEALQ NERDLLGTVW GGPANLEAIA KKGKFNK.

    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.

    Echdc1 Human
  • View Data Sheet

    Name :

    ENPP1 Mouse

    Description:

    Ectonucleotide Pyrophosphatase Mouse Recombinant

    Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Membrane component chromosome 6 surface marker 1, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, ENPP1, M6S1, NPPS, PC1, PDNP1, NPP1, PC-1, PCA1, ARHR2, COLED.

    Product # :

    ENZ-1193

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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    • More Info

    Description

    ENPP1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 828 amino acids (Lys85-Glu906) and having a molecular mass of 95.2kDa. ENPP1 Mouse is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    The filtered (0.4µm) concentrated protein solution was lyophilized with PBS, PH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Membrane component chromosome 6 surface marker 1, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, ENPP1, M6S1, NPPS, PC1, PDNP1, NPP1, PC-1, PCA1, ARHR2, COLED.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      KEVKSCKGRC FERTFSNCRC DAACVSLGNC CLDFQETCVE PTHIWTCNKF RCGEKRLSRF VCSCADDCKT HNDCCINYSS VCQDKKSWVE ETCESIDTPE CPAEFESPPT LLFSLDGFRA EYLHTWGGLL PVISKLKNCG TYTKNMRPMY PTKTFPNHYS IVTGLYPESH GIIDNKMYDP KMNASFSLKS KEKFNPLWYK GQPIWVTANH QEVKSGTYFW PGSDVEIDGI LPDIYKVYNG SVPFEERILA VLEWLQLPSH ERPHFYTLYL EEPDSSGHSH GPVSSEVIKA LQKVDRLVGM LMDGLKDLGL DKCLNLILIS DHGMEQGSCK KYVYLNKYLG DVNNVKVVYG PAARLRPTDV PETYYSFNYE ALAKNLSCRE PNQHFRPYLK PFLPKRLHFA KSDRIEPLTF YLDPQWQLAL NPSERKYCGS GFHGSDNLFS NMQALFIGYG PAFKHGAEVD SFENIEVYNL MCDLLGLIPA PNNGSHGSLN HLLKKPIYNP SHPKEEGFLS QCPIKSTSND LGCTCDPWIV PIKDFEKQLN LTTEDVDDIY HMTVPYGRPR ILLKQHHVCL LQQQQFLTGY SLDLLMPLWA SYTFLRNDQF SRDDFSNCLY QDLRIPLSPV HKCSYYKSNS KLSYGFLTPP RLNRVSNHIY SEALLTSNIV PMYQSFQVIW HYLHDTLLQR YAHERNGINV VSGPVFDFDY DGRYDSLEIL KQNSRVIRSQ EILIPTHFFI VLTSCKQLSE TPLECSALES SAYILPHRPD NIESCTHGKR ESSWVEELLT LHRARVTDVE LITGLSFYQD RQESVSELLR LKTHLPIFSQ EDHHHHHH.

    • Background

      Ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1) is an enzyme with multifaceted roles in cellular metabolism, bone mineralization, and insulin signaling. Research utilizing mouse models has been pivotal in elucidating the complex biology of ENPP1 and its implications for various physiological processes and disease states. This study aims to provide a comprehensive exploration of ENPP1 in mouse physiology, shedding light on its diverse functions and potential applications in understanding metabolic health and disease mechanisms.

      The primary objective of this research is to elucidate the impact of ENPP1 in mouse models on metabolic health. In vivo experiments using genetically modified mice with altered ENPP1 expression or activity will be conducted to investigate how ENPP1 influences glucose homeostasis, insulin sensitivity, and lipid metabolism. Understanding these mechanisms is fundamental for deciphering the role of ENPP1 in metabolic diseases such as diabetes and obesity.

      The second objective is to assess the clinical relevance of ENPP1 in mouse models of bone health. Mouse models of skeletal disorders will be employed to explore how ENPP1 affects bone mineralization, density, and remodeling. These investigations may provide valuable insights into potential therapeutic strategies targeting ENPP1 in bone-related diseases.

      The third objective is to explore the broader implications of ENPP1 in mouse physiology, including its effects on vascular health, inflammation, and tissue repair. Research will investigate its roles in vascular calcification, inflammation resolution, and tissue regeneration. Understanding the multifaceted properties of ENPP1 in mouse models may open new avenues for therapeutic interventions in various metabolic and chronic disease contexts.

      By delving into the diverse functions of ENPP1 in mouse physiology, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for metabolic diseases, bone disorders, and other conditions influenced by ENPP1.

    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.

    Enpp1 Mouse
  • View Data Sheet

    Name :

    FUCA2 Human

    Description:

    Fucosidase Alpha-L- 2 Plasma Human Recombinant

    Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

    Product # :

    ENZ-840

    Price :

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    Description

    FUCA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (29-467 a.a) and having a molecular mass of 53.3kDa.FUCA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FUCA2 protein solution (1mg/ml) containing 20mM phosphate (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fucosidase Alpha-L- 2 Plasma (FUCA2) is a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. FUCA2 protein belongs to the glycosyl hydrolase 29 family, and catalyzes the hydrolysis of the alpha-1,6-linked fucose fused to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA2 is crucial for Helicobacter pylori adhesion to human gastric cancer cells.

    • Synonyms

      Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

    • 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 MGSHSATRFD PTWESLDARQ LPAWFDQAKF GIFIHWGVFS VPSFGSEWFW WYWQKEKIPK YVEFMKDNYP PSFKYEDFGP LFTAKFFNAN QWADIFQASG AKYIVLTSKH HEGFTLWGSE YSWNWNAIDE GPKRDIVKEL EVAIRNRTDL RFGLYYSLFE WFHPLFLEDE SSSFHKRQFP VSKTLPELYE LVNNYQPEVL WSDGDGGAPD QYWNSTGFLA WLYNESPVRG TVVTNDRWGA GSICKHGGFY TCSDRYNPGH LLPHKWENCM TIDKLSWGYR REAGISDYLT IEELVKQLVE TVSCGGNLLM NIGPTLDGTI SVVFEERLRQ MGSWLKVNGE AIYETHTWRS QNDTVTPDVW YTSKPKEKLV YAIFLKWPTS GQLFLGHPKA ILGATEVKLL GHGQPLNWIS LEQNGIMVEL PQLTIHQMPC KWGWALALTN VI.

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    Fuca2 Human
  • View Data Sheet

    Name :

    XPNPEP1 Human

    Description:

    X-Prolyl Aminopeptidase-1 Human Recombinant

    X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.

    Product # :

    ENZ-880

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    Description

    XPNPEP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 655 amino acids (1-623 a.a) and having a molecular mass of 73.4kDa. XPNPEP1 is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    XPNPEP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      X-Prolyl Aminopeptidase-1, also known as XPNPEP1 is a member of the peptidase M24B family. XPNPEP1 encodes the cytosolic form of a metalloaminopeptidase which catalyzes the cleavage of the N-terminal amino acid adjacent to a proline residue. Furthermore, XPNPEP1 plays a role in degradation as well as maturation of tachykinins, neuropeptides and peptide hormones.

    • Synonyms

      X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.

    • 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 MGSEFELRRQ ASMPPKVTSE LLRQLRQAMR NSEYVTEPIQ AYIIPSGDAH QSEYIAPCDC RRAFVSGFDG SAGTAIITEE HAAMWTDGRY FLQAAKQMDS NWTLMKMGLK DTPTQEDWLV SVLPEGSRVG VDPLIIPTDY WKKMAKVLRS AGHHLIPVKE NLVDKIWTDR PERPCKPLLT LGLDYTGISW KDKVADLRLK MAERNVMWFV VTALDEIAWL FNLRGSDVEH NPVFFSYAII GLETIMLFID GDRIDAPSVK EHLLLDLGLE AEYRIQVHPY KSILSELKAL CADLSPREKV WVSDKASYAV SETIPKDHRC CMPYTPICIA KAVKNSAESE GMRRAHIKDA VALCELFNWL EKEVPKGGVT EISAADKAEE FRRQQADFVD LSFPTISSTG PNGAIIHYAP VPETNRTLSL DEVYLIDSGA QYKDGTTDVT RTMHFGTPTA YEKECFTYVL KGHIAVSAAV FPTGTKGHLL DSFARSALWD SGLDYLHGTG HGVGSFLNVH EGPCGISYKT FSDEPLEAGM IVTDEPGYYE DGAFGIRIEN VVLVVPVKTK YNFNNRGSLT FEPLTLVPIQ TKMIDVDSLT DKECDWLNNY HLTCRDVIGK ELQKQGRQEA LEWLIRETQP ISKQH.

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    Xpnpep1 Human
  • View Data Sheet

    Name :

    NARS Human

    Description:

    Asparaginyl-TRNA Synthetase Human Recombinant

    NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    Product # :

    ENZ-915

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    Description

    NARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-548 a.a) and having a molecular mass of 65.3kDa. NARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    NARS protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

    • Synonyms

      NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    • 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

      GSSHHHHHH SSGLVPRGSH MGSMVLAELY VSDREGSDAT GDGTKEKPFK TGLKALMTVG KEPFPTIYVD SQKENERWNV ISKSQLKNIK KMWHREQMKS ESREKKEAED SLRREKNLEE AKKITIKNDP SLPEPKCVKI GALEGYRGQR VKVFGWVHRL RRQGKNLMFL VLRDGTGYLQ CVLADELCQC YNGVLLSTES SVAVYGMLNL TPKGKQAPGG HELSCDFWEL IGLAPAGGAD NLINEESDVD VQLNNRHMMI RGENMSKILK ARSMVTRCFR DHFFDRGYYE VTPPTLVQTQ VEGGATLFKL DYFGEEAFLT QSSQLYLETC LPALGDVFCI AQSYRAEQSR TRRHLAEYTH VEAECPFLTF DDLLNRLEDL VCDVVDRILK SPAGSIVHEL NPNFQPPKRP FKRMNYSDAI VWLKEHDVKK EDGTFYEFGE DIPEAPERLM TDTINEPILL CRFPVEIKSF YMQRCPEDSR LTESVDVLMP NVGEIVGGSM RIFDSEEILA GYKREGIDPT PYYWYTDQRK YGTCPHGGYG LGLERFLTWI LNRYHIRDVC LYPRFVQRCT P.

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    Human Nars
  • View Data Sheet

    Name :

    UMOD Porcine

    Description:

    Uromodulin Porcine

    Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    Product # :

    ENZ-733

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    Description

    Porcine Uromodulin is a 97kDa glycoprotein which is produced in the thick ascending limb of Henle´s loop and early distal convoluted tubules of the nephron.

    Source

    Porcine Urine.

    Formulation

    The UMOD protein was lyophilized from 0.4µm filtered solution at a concentration of 0.5mg/ml containing deionized water.

    More Info

    • Introduction

      Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

    • Synonyms

      Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    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.

    Umod Porcine
  • View Data Sheet

    Name :

    UBE2B Human

    Description:

    Ubiquitin Conjugating Enzyme E2B Human Recombinant

    Ubiquitin-conjugating enzyme E2 B, EC 6.3.2.19, Ubiquitin-protein ligase B, Ubiquitin carrier protein B, HR6B, hHR6B, E2-17 kDa UBC2, HHR6B, RAD6B, E2-17kDa, UBE2B.

    Product # :

    ENZ-340

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    Description

    Ubiquitin Conjugating Enzyme E2B Human Recombinant produced in E.coli is a 19 kDa protein containing 166 amino acids.The UE2B 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

    • Introduction

      This E2 enzyme encodes for the human homolog of the yeast DNA repair gene RAD6, which is induced by DNA damaging agents. UBE2B can conjugate ubiquitin to histone H2A in an E3- independent manner in vitro, and is essential for the multi-ubiquitination and degradation of N-end rule substrates. Additionally, UBE2B may have a role in sepsis-induced muscle protein proteolysis and cancer-induced cachexia.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 B, EC 6.3.2.19, Ubiquitin-protein ligase B, Ubiquitin carrier protein B, HR6B, hHR6B, E2-17 kDa UBC2, HHR6B, RAD6B, E2-17kDa, UBE2B.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized UBE2B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2B 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 UBE2B in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAMGQLRSMSTPARRRLMRDFKRLQEDPPVGVSGAPSENN
      IMQWNAVIFGPEGTPFEDGTFKLVIEFSEEYPNKPPTVRFLSKMFHPNVY
      ADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQE
      NKREYEKRVSAIVEQSWNDS.

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    Ube2B Human
  • View Data Sheet

    Name :

    RNPA E.Coli

    Description:

    Ribonuclease P protein component E.Coli Recombinant

    ECK3696, Rnase P protein, RnaseP protein, b3704, JW3681, Ribonuclease P protein component, EC 3.1.26.5, Protein C5.

    Product # :

    ENZ-1169

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    Description

    RNPA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (1-119a.a) and having a molecular mass of 13.7kDa.RNPA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNPA protein solution (0.25mg/ml) in Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rnase P protein, AKA rnpA, is an important enzyme consisting of the C5 protein (which encoded by rnpA) and the catalytic M1 RNA (encoded by rnpB) subunits. rnpA is ribonucleoprotein that catalyzes the removal of the 50- leader elements of precursor tRNAs and generates the mature 50-end of tRNAs. This step is critical for theformation of functional tRNA molecules in bacteria, archaea and eukarya. More importantly, it has lately been established that RNase P is essential for the endonucleolytic separation of certain polycistronic tRNA transcripts such as valV valW, leuQ leuP leuV and secG leuU. Therefore, it was hypothesized that the essential function of RNase P might be related to the complete absence of a particular tRNAthat was dependent on the enzyme for initial separation from polycistronic transcripts.

    • Synonyms

      ECK3696, Rnase P protein, RnaseP protein, b3704, JW3681, Ribonuclease P protein component, EC 3.1.26.5, Protein C5.

    • 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

      MVKLAFPREL RLLTPSQFTF VFQQPQRAGT PQITILGRLN SLGHPRIGLT VAKKNVRRAH ERNRIKRLTR ESFRLRQHEL PAMDFVVVAK KGVADLDNRA LSEALEKLWR RHCRLARGS

    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.

    Rnpa Ribonuclease P 2
  • View Data Sheet

    Name :

    MMP2 Human

    Description:

    Matrix Metalloproteinase-2 Human Recombinant

    kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    Product # :

    ENZ-769

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    Description

    MMP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 576 amino acids (110-660a.a) and having a molecular mass of 64.7kDa. MMP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Matrix metalloproteinase-2 (MMP-2) is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).

    • Synonyms

      kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    • 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 MGSEFYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARAFQVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGKEY NSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NAEGQPCKFP FRFQGTSYDS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRSDGKMW CATTANYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS QDDIKGIQEL YGASPDIDLG TGPTPTLGPV TPEICKQDIV FDGIAQIRGE IFFFKDRFIW RTVTPRDKPM GPLLVATFWP ELPEKIDAVY EAPQEEKAVF FAGNEYWIYS ASTLERGYPK PLTSLGLPPD VQRVDAAFNW SKNKKTYIFA GDKFWRYNEV KKKMDPGFPK LIADAWNAIP DNLDAVVDLQ GGGHSYFFKG AYYLKLENQS LKSVKFGSIK SDWLGC.

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    Mmp2 Human
  • View Data Sheet

    Name :

    Pfu DNA Polymerase

    Description:

    Pfu-DNA Polymerase Recombinant

    DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

    Product # :

    ENZ-265

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    Description

    Pfu DNA Polymerase is a thermo-stable enzyme having a Mw of about 90kDa. Pfu DNA Polymerase is derived from E. coli that and cloned from Pyrococcus furiosus strain Vc1 DSM3638. Pfu DNA Polymerase replicates DNA at 75°C, catalyzing the polymerization of nucleotides into duplex DNA in the 5´ to 3´ direction in the existence of magnesium. Pfu DNA Polymerase possesses 3´ to 5´ exonuclease (proofreading) activity. Base misinsertions that take place during polymerization are swiftly removed by the proofreading activity of the polymerase. Therefore, Pfu DNA Polymerase is suggested for use in PCR and primer extension reactions that require high-fidelity synthesis. Pfu DNA Polymerase-generated PCR fragments are blunt-ended.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris-HCl, pH 8.2, 1mM DTT, 0.1mM EDTA, 0.05% CHAPS and 50% glycerol.

    More Info

    • Introduction

      Pfu DNA polymeraseenzyme is found in the hyperthermophilic archaeonPyrococcus furiosus, where it functions in vivoto replicate the organism's DNA. In vitro, Pfu is used to swiftly amplify DNAin the Polymerase Chain Reaction, where the enzyme serves the central function of copying a new strand of DNA during each extension step. Pfu DNA polymerase has superior thermostability and 'proofreading' properties compared to other thermostable polymerases. Unlike Taq DNA polymerase, Pfu DNA polymerase possesses 3' to 5' exonuclease proof reading activity, meaning that it works its way along the DNA from the 5' endto the 3' endand corrects nucleotidemisin corporation errors. Pfu DNA polymerase-generated PCRfragments will have fewer errors than Taq-generated PCR inserts. As a result, Pfu is more commonly used for molecular cloning of PCR fragments than the historically popular Taq. Pfu DNA polymerase is superior for techniques that require high-fidelity DNA synthesis, but can also be used in conjunction with Taq polymerase to obtain the fidelity of Pfu with the speed of Taq polymerase activity.

    • Synonyms

      DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

      Pfu DNA Polymerase although stable at 10°C for 5 days, should be stored below -18°C.Please prevent freeze-thaw cycles.

    • Applications

      1. Ideal for high-fidelity amplification.
      2. 3'-5' exonuclease activity provides a low error rate.
      3. One of the most thermostable DNA polymerases known.
      4. Lack of extendase activity means no unwanted 3’ overhangs.
      5. Optimal for blunt-end PCR cloning.
      6. Optimum temperature near 75°C.
      7. 95% active after 1-hour incubation at 98°C.

    • PCR Protocol

      Add the following components to amplify 1kb DNA template: 0.2µl Pfu-DNA Polymerase.4µl 2.5mM dNTPs.5µl 10x buffer with MgSO4. 1µl Primers mix (10µM each).1µl Template.38µl ddH2O. Amplify using the following cycling parameters: Heat Soak: 1 cycle at 94°C/4 min.Denaturation: 30 cycles at 94°C/30 sec.Annealing: 30 cycles at 55°C /30 sec.Extension: 30 cycles at 72°C /90 sec. Final: 1 cycle at 72°C /5 min.

    • Unit Definition

      1U of enzyme catalyzes the incorporation of 10nmol of dNTP into acid-insoluble product in 30 minutes at 75°C.

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    Pfu Dna Polymerase
  • View Data Sheet

    Name :

    NIT2 Human

    Description:

    Nitrilase Family Member 2 Human Recombinant

    Nitrilase homolog 2, Nitrilase family member 2, omega-amidase NIT2, MGC111199, Nit protein 2, EC 3.5.1.3.

    Product # :

    ENZ-039

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    Description

    NIT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276a.a.) and having a molecular mass of 33kDa.NIT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NIT2 protein solution (1mg/1ml) is formulated in 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

      NIT2 is a member of the nitrilase superfamily. NIT2 protein has an omega-amidase activity which removes potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. In addition, Nit2 is widely distributed in nature and is thought to be a tumor suppressor protein.

    • Synonyms

      Nitrilase homolog 2, Nitrilase family member 2, omega-amidase NIT2, MGC111199, Nit protein 2, EC 3.5.1.3.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTSFRLA LIQLQISSIK SDNVTRACSF IREAATQGAK IVSLPECFNS PYGAKYFPEY AEKIPGESTQ KLSEVAKECS IYLIGGSIPE EDAGKLYNTC AVFGPDGTLL AKYRKIHLFD IDVPGKITFQ ESKTLSPGDS FSTFDTPYCR VGLGICYDMR FAELAQIYAQ RGCQLLVYPG AFNLTTGPAH WELLQRSRAV DNQVYVATAS PARDDKASYV AWGHSTVVNP WGEVLAKAGT EEAIVYSDID LKKLAEIRQQ IPVFRQKRSD LYAVEMKKP

    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.

    Nit2 Human
  • View Data Sheet

    Name :

    PYCRL Human

    Description:

    Pyrroline-5-Carboxylate Reductase Like Human Recombinant

    Pyrroline-5-carboxylate reductase 3, P5C reductase 3, P5CR 3, Pyrroline-5-carboxylate reductase-like protein, PYCRL.

    Product # :

    ENZ-678

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    Description

    PYCRL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-274) and having a molecular mass of 31kDa.PYCRL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PYCRL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pyrroline-5-Carboxylate Reductase Like (PYCRL) is a member of the pyrroline-5-carboxylate reductase family and acts as a homodecamer. PYCRL plays a key role in proline bio-synthesis. Proline serves as a non-enzymatic antioxidant to reduce damage caused by reactive oxygen species (ROS) in microorganisms, animals and plants. In the final stage of proline biosynthesis, PYCRL catalyzes the reduction of aldehyde dehydrogenase 4A1 (ALDH4A1) to proline with NAD(P)H as the cofactor.

    • Synonyms

      Pyrroline-5-carboxylate reductase 3, P5C reductase 3, P5CR 3, Pyrroline-5-carboxylate reductase-like protein, PYCRL.

    • 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 MGSMAAAEPS PRRVGFVGAG RMAGAIAQGL IRAGKVEAQH ILASAPTDRN LCHFQALGCR TTHSNQEVLQ SCLLVIFATK PHVLPAVLAE VAPVVTTEHI LVSVAAGVSL STLEELLPPN TRVLRVLPNL PCVVQEGAIV MARGRHVGSS ETNLLQHLLE ACGRCEEVPE AYVDIHTGLS GSGVAFVCAF SEALAEGAVK MGMPSSLAHR IAAQTLLGTA KMLLHEGQHP AQLRSDVCTP GGTTIYGLHA LEQGGLRAAT MSAVEAATCR AKELSRK.

    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.

    Pycrl Human
  • View Data Sheet

    Name :

    Urease

    Description:

    Urease Recombinant

    Product # :

    ENZ-277

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    Description

    The mutant Urease from microorganism source, showing shifted substrate affinity to urea. It was designed wildtype coding gene from microorganism. The subunit structure is very similar to well known microbial urease. Please refer to published literature such as JBC 262, 5963-67 (1987). It is composed of multi-subunits and shows a bit complex protein structure (alpha 2 Beta 4 Gamma 4) as compared to plant urease rUrease is genetically designed unique mutant having shifted high Km to urea, which is suited material to kinetic urea assay with wide measurable range. The enzyme comprises of three different subunits to make complete fully active form, 60.3 kD a subunit, 11.7 kD b subunit and 11.1 kD g subunit respectively.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 370µg Potassium Phosphate and 30µg EDTA Na2.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity was found to be 120U/mg powder.

    More Info

    • Physical Appearance

      Sterile Lyophilized Powder.

    • Stability

      Urease although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Urease in sterile 18MΩ-cm H2O.

    • Unit Definition

      One Unit oxidizes one micromole of NADH per minute at 25°C, at pH 7.6.

    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.

    Urease
  • View Data Sheet

    Name :

    HERC5 Human

    Description:

    HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant

    HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.

    Product # :

    ENZ-797

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    Description

    HERC5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (681-1024 a.a.) and having a molecular mass of 43kDa. HERC5 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    HERC5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 (HERC5) is a member of the HERC family of ubiquitin ligases, found in a cluster of HERC family genes on chromosome 4. HERC5 is a protein with a HECT domain and 5 RCC1 repeats. The HERC5 protein localizes to the cytoplasm and perinuclear region and serves as an INF-induced E3 protein ligase that mediates ISGylation of protein targets. HERC5 exhibits antiviral activity towards HIV-1, influenza A virus and human papillomavirus. HERC5 is a major E3 ligase for ISG15 conjugation. HERC5 also serves as a positive regulator of innate antiviral response in cells induced by INF. Pro-inflammatory cytokines upregulate HERC5 in endothelial cells. HERC5 is physically connected with polyribosomes, broadly modifies recently synthesized proteins in a cotranslational fashion.

    • Synonyms

      HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.

    • 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 MGSFDLTVRR NHLIEDVLNQ LSQFENEDLR KELWVSFSGE IGYDLGGVKK EFFYCLFAEM IQPEYGMFMY PEGASCMWFP VKPKFEKKRY FFFGVLCGLS LFNCNVANLP FPLALFKKLL DQMPSLEDLK ELSPDLGKNL QTLLDDEGDN FEEVFYIHFN VHWDRNDTNL IPNGSSITVN QTNKRDYVSK YINYIFNDSV KAVYEEFRRG FYKMCDEDII KLFHPEELKD VIVGNTDYDW KTFEKNARYE PGYNSSHPTI VMFWKAFHKL TLEEKKKFLV FLTGTDRLQM KDLNNMKITF CCPESWNERD PIRALTCFSV LFLPKYSTME TVEEALQEAI NNNRGFG.

    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.

    Herc5 Human
  • View Data Sheet

    Name :

    PRSS7 Human

    Description:

    Protease Serine 7 Human Recombinant

    PRSS7,ENTK,Protease, Serine, 7 (Enterokinase), Transmembrane Protease, Serine 15, Serine Protease 7, Enteropeptidase, EC 3.4.21.9, Transmembrane Protease Serine 15,Enterokinase Catalytic Subunit, Proenterokinase, Enterokinase, EC 3.4.21.

    Product # :

    ENZ-850

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    Description

    PRSS7 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 237 amino acids (785-1019 a.a.) and having a molecular mass of 26.4kDa. The PRSS7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRSS7 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protease Serine 7, also known as PRSS7, is in charge of initiating the activation of pancreatic proteolytic proenzymes such as trypsin, chymotrypsin and carboxypeptidase A. PRSS7 catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, as well as proelastases.

    • Synonyms

      PRSS7,ENTK,Protease, Serine, 7 (Enterokinase), Transmembrane Protease, Serine 15, Serine Protease 7, Enteropeptidase, EC 3.4.21.9, Transmembrane Protease Serine 15,Enterokinase Catalytic Subunit, Proenterokinase, Enterokinase, EC 3.4.21.

    • 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

      MAIVGGSNAK EGAWPWVVGL YYGGRLLCGA SLVSSDWLVS AAHCVYGRNL EPSKWTAILG LHMKSNLTSP QTVPRLIDEI VINPHYNRRR KDNDIAMMHL EFKVNYTDYI QPICLPEENQ VFPPGRNCSI AGWGTVVYQG TTANILQEAD VPLLSNERCQ QQMPEYNITE NMICAGYEEG GIDSCQGDSG GPLMCQENNR WFLAGVTSFG YKCALPNRPG VYARVSRFTE WIQSFLH

    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.

    Prss7 Human
  • View Data Sheet

    Name :

    T7 RNAP

    Description:

    T7 RNA Polymerase Recombinant

    T7 RNAP.

    Product # :

    ENZ-1180

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    Description

    T7 RNA polymerase Recombinant protein is produced by bacteriophage T7 DNA which is expressed in recombinant E. coli bacterial system T7 RNA Polymerase is a DNA-dependent 5'→ 3' RNA polymerase which specifically recognizes T7 promoter sequences.

    Source

    T7 Bacteriophage RNA Polymerase gene

    Formulation

    Transcription Buffer 40mM Tris-HCl (25°C, pH-8), 20mM MgCl2, 2.5mM TCEP & 2mM spermidine.

    Purity

    Greater than 95% as visualized by SDS-PAGE

    More Info

    • Introduction

      T7 RNA polymerase active enzyme synthesizes RNA at an increasing degree of that of E. coli RNA polymerase and it terminates transcription often. T7 RNA polymerase is very selective for initiation at its own promoter sequences and is resistant to antibiotics that inhibit E. coli RNA polymerase. In-vitro transcription of mRNA is achieved via bacteriophage T7 RNA polymerase using its ability to produce full-length RNA transcripts with high reliability, thoughT7 RNAP can manufacture as well immunostimulatory by products for example dsRNA which affect protein expression.

    • Synonyms

      T7 RNAP.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Two years when stored at -20°C, 2 weeks at 4°C. DO NOT STORE AT -70C.

    • Applications

      Synthesis of :

      • ssRNAs.
      • Labeled or unlabeled highly specific RNA probes.
      • Capped mRNA using cap analogues.
    • Unit Definition

      1U is defined as the amount of enzyme required to incorporate 1nmol of [3H] ATP into acid-insoluble precipitates within 1 hour at 37℃, pH-8.

    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.

    T7 Rnap
  • View Data Sheet

    Name :

    MGMT Human

    Description:

    O-6-Methylguanine-DNA Methyltransferase Human Recombinant

    Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, MGMT.

    Product # :

    ENZ-389

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    Description

    MGMT Human Recombinant fused to a 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 227 amino acids (1-207) and having a molecular mass of 23.8 kDa. The MGMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MGMT solution contains 20mM Tris-HCl pH-7.5, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MGMT is an enzyme that repairs O-6-methylguanine, a mutagenic DNA base damaged by endogenous and environmental alkylating agents and takes part in the cellular defense against the biological effects of O-6-methylguanine in DNA. MGMT repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. abnormal MGMT expression correlates with the prognosis in human solid cancers. MGMT decrease of expression is correlated with methylation. The human MGMT is a negative regulator of estrogen receptor-mediated transcription upon alkylation DNA damage. MGMT promoter hypermethylation plays an important role in the early steps of colorectal carcinogenesis. Abnormal promoter hypermethylation of MGMT gene is associated with oral squamous cell carcinomas.

    • Synonyms

      Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, MGMT.

    • Physical Appearance

      Sterile Filtered clear 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 MDKDCEMKRT TLDSPLGKLE LSGCEQGLHE IKLLGKGTSA ADAVEVPAPA AVLGGPEPLM QCTAWLNAYF HQPEAIEEFP VPAFHHPVFQ QESFTRQVLW KLLKVVKFGE VISYQQLAAL AGNPKAARAV GGAMRGNPVP ILIPCHRVVC SSGAVGNYSG GLAVKEWLLA HEGHRLGKPG LGGSSGLAGA WLKGAGATSG SPPAGRN.

    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.

    Product Image
  • View Data Sheet

    Name :

    GDA Human, Active

    Description:

    Guanine Deaminase Human Recombinant, Active

    Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.

    Product # :

    ENZ-982

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    Description

    GDA Human Recombinant produced in E. coli is a single polypeptide chain containing 477 amino acids (1-454) and having a molecular mass of 53kDa.GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol, 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,000 pmol/min/ug, and is defined as the amount of enzyme that convert guanine to xanthine per minute at pH 8.0 at 37C.

    More Info

    • Introduction

      GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

    • Synonyms

      Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.

    • 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 MGSMCAAQMP PLAHIFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE ASQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHASQ YSFAGSSIDL PLLEWLTKYT FPAEHRFQNI DFAEEVYTRV VRRTLKNGTT TACYFATIHT DSSLLLADIT DKFGQRAFVG KVCMDLNDTF PEYKETTEES IKETERFVSE MLQKNYSRVK PIVTPRFSLS CSETLMGELG NIAKTRDLHI QSHISENRDE VEAVKNLYPS YKNYTSVYDK NNLLTNKTVM AHGCYLSAEE LNVFHERGAS IAHCPNSNLS LSSGFLNVLE VLKHEVKIGL GTDVAGGYSY SMLDAIRRAV MVSNILLINK VNEKSLTLKE VFRLATLGGS QALGLDGEIG NFEVGKEFDA ILINPKASDS PIDLFYGDFF GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.

    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.

    Gda Human Active
  • View Data Sheet

    Name :

    HaeIII

    Description:

    HaeIII Recombinant

    site-specific DNA-methyltransferase, HaeIVRM.

    Product # :

    ENZ-1203

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    Description

    HaeIII is a prokaryotic DNA that protects organisms from an unknown DNA. HaeIII’s recognition site is the GGCC nucleotide sequence which means it cleaves DNA at the site 5′-GG/CC-3.

    Source

    E. coli that carries the HaeIII gene from Haemophilus aegypticus

    Purity

    Great than 95 % as estimated by SDS-PAGE analyses.

    More Info

    • Synonyms

      site-specific DNA-methyltransferase, HaeIVRM.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      HaeIII although stable at 15°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Background

      HaeIII cleaves the DNA at the positions where the GGCC sequence is found. The cleavage happens between the 2nd and the third nucleotides -G and C. The resulting DNA fragments are known as restriction fragments. HaeIII cuts both strands of DNA in the same location, creating restriction fragments with blunt ends.

    • Storage Buffer

      10mM Tris-HCl (pH 7.4), 1 mM DTT, 50% (v/v) glycerol, 0.1mM EDTA, 50 mM KCl and 200µg/ml BSA.

    • Unit Definition

      1 unit is defined as the amount of HaeIII required to digest 1 µg of lambda DNA in 1 hour at 37°C in 50 µL of recommended reaction buffer.

    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.

    Haeiii Enzyme
  • View Data Sheet

    Name :

    MMLV RT

    Description:

    Moloney Murine Leukemia Virus Reverse Trancscriptase Recombinant

    Product # :

    ENZ-310

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    Description

    MMLV (Moloney Murine Leukemia Virus) Reverse Transcriptase is a DNA polymerase that synthesizes a complementary DNA strands from single-stranded RNA, DNA, or an RNA-DNA hybrid as a template. This recombinant enzyme was purified from E.coli, which carried a modified MMLV-RT gene. Compared to AMV Reverse Transcriptase, this enzyme has a much weaker 5' - 3' ribonuclease H activity, which allows the syntesis of longer cDNAs (>7kb).

    Source

    Recombinant E. coli strain.

    Formulation

    50mM Tris-HCl, 0.1M NaCl, 0.1% Triton X-100, 2mM DTT, 0.1mM EDTA and 50% glycerol.

    More Info

    • Physical Appearance

      Sterile Filtered clear solution (200 U/µl).

    • Stability

      Stable for 5 days at 10°C, for longer period of time store at -20°C. Please prevent freeze-thaw cycles.

    • Unit Definition

      One unit is defined as the amount of enzyme required to catalyze the incorporation of 1nmol of deoxyribonucleotide into acid-insoluble forms in 10 minutes at 37oC, using poly(A)-oligo(dT)12-18 as the template-primer. Standard cDNA Synthesis Conditions50mM Tris-HCl (pH8.3), 75mM KCl, 3mM MgCl2, 10mM DTT, 1.0mM each dATP, dGTP, dCTP, and dTTP, 0.2 mg radom hexamer,1-5mg RNA, 200units M-MLV RT. The reaction volume was 20ml and the incubation was 45 min at 42oC.

    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.

    M Mlv Reverse Transcriptase
  • 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 :

    NDUFV2 Human

    Description:

    NADH Dehydrogenase Flavoprotein 2 Human Recombinant

    CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    Product # :

    ENZ-743

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    • purity
    • More Info

    Description

    NDUFV2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (33-249 a.a) and having a molecular mass of 26.1kDa.NDUFV2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NDUFV2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NADH Dehydrogenase Flavoprotein 2 (NDUFV2) is a 24 kDa Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysisthe. NDUFV2 is aslo involved in electron transfer. Mutations in NDUFV2 are implicated in Parkinson's disease, bipolar disorder, schizophrenia, and have been discovered in one case of early onset hypertrophic cardiomyopathy and encephalopathy.

    • Synonyms

      CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    • 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 MGSGAGGALF VHRDTPENNP DTPFDFTPEN YKRIEAIVKN YPEGHKAAAV LPVLDLAQRQ NGWLPISAMN KVAEVLQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK VGETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTAK DIEEIIDELK AGKIPKPGPR SGRFSCEPAG GLTSLTEPPK GPGFGVQAGL.

    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.

    Ndufv2 Human
  • View Data Sheet

    Name :

    IDNK E.Coli

    Description:

    Thermosensitive Gluconokinase E.Coli Recombinant

    Thermosensitive gluconokinase, Gluconate kinase 1, idnK.

    Product # :

    PKA-060

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    IDNK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 23.4kDa. IDNK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IDNK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thermosensitive Gluconokinase, also known as IDNK is a 187 a.a protein which is a member of the gluconokinase gntK/gntV family. IDNK catalyzes theconversion of ATP and D-gluconate to ADP and 6-phospho-D-gluconate. In addition, IDNK is considered to take part in gender determination, deletion of the distal portion of 9p is able to lead to a development of male to female sex reversal, the phenotype of a female with a male X, Y genotype.

    • Synonyms

      Thermosensitive gluconokinase, Gluconate kinase 1, idnK.

    • 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 MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE.

    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.

    Idnk Ecoli
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