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Search results

1000 results found for “Lyase”

Name

Description

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  • View Data Sheet

    Name :

    MSRB3 Human

    Description:

    Methionine Sulfoxide Reductase B3 Human Recombinant

    Methionine-R-sulfoxide reductase B3, MSRB3, DFNB74, FLJ36866, DKFZp686C1178.

    Product # :

    ENZ-093

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    Description

    MSRB3 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (21-185 a.a.) and having a molecular mass of 19kDa. The MSRB3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MSRB3 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Methionine sulfoxide reductase B3 (MSRB3) is a member of the methionine sulfoxide reductases (MSR) family proteins. MSRB3 catalyzes the reduction of methionine sulfoxide to methionine. The MSRB3 enzyme acts as a monomer and requires zinc as a cofactor. MSRs are thought to defend against reactive oxygen species-induced oxidative damage in various organs, including the most environmentally exposed organ, the human skin. MSRB3 has a vital role in cold tolerance by eliminating MetO and ROS which accumulate at the ER during cold acclimation.

    • Synonyms

      Methionine-R-sulfoxide reductase B3, MSRB3, DFNB74, FLJ36866, DKFZp686C1178.

    • 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

      MCGLPSGSCR DKKNCKVVFS QQELRKRLTP LQYHVTQEKG TESAFEGEYT HHKDPGIYKC VVCGTPLFKS ETKFDSGSGW PSFHDVINSE AITFTDDFSY GMHRVETSCS QCGAHLGHIF DDGPRPTGKR YCINSAALSF TPADSSGTAE GGSGVASPAQ ADKAELLEHH HHHH.

    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.

    Msrb3 Human
  • View Data Sheet

    Name :

    SDSL Human

    Description:

    Serine Dehydratase-Like Human Recombinant

    Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.

    Product # :

    ENZ-180

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    Description

    SDSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 37.3 kDa.SDSL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SDSL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SDSL belongs to the serine/threonine dehydratase family and function as a serinespecific dehydratase. SDSL utilizes pyridoxal phosphate and is one of three key enzymes which take part in the metabolism of Glycine and serine.

    • Synonyms

      Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.

    • 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 MGSHMDGPVA EHAKQEPFHV VTPLLESWAL SQVAGMPVFL KCENVQPSGS FKIRGIGHFC QEMAKKGCRH LVCSSGGNAG IAAAYAARKL GIPATIVLPE STSLQVVQRL QGEGAEVQLT GKVWDEANLR AQELAKRDGW ENVPPFDHPL IWKGHASLVQ ELKAVLRTPP GALVLAVGGG GLLAGVVAGL LEVGWQHVPI IAMETHGAHC FNAAITAGKL VTLPDITSVA KSLGAKTVAA RALECMQVCK IHSEVVEDTE AVSAVQQLLD DERMLVEPAC GAALAAIYSG LLRRLQAEGC LPPSLTSVVV IVCGGNNINS RELQALKTHL GQV.

    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.

    Sdsl Human
  • View Data Sheet

    Name :

    ANXA6 Human

    Description:

    Annexin A6 Human Recombinant

    ANX6, ANXA6, Annexin-VI, Lipocortin-6, Lipocortin-VI, Annexin-6, CPB-II, Annexin A6, p68, p70, Protein III, Chromobindin-20, 67 kDa calelectrin, Calphobindin-II, CBP68.

    Product # :

    PRO-767

    Price :

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    Description

    ANXA6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 693 amino acids (1-673 a.a.) and having a molecular mass of 78 kDa. ANXA6 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA6 protein solution contains 20mM Tris-HCl, pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ANXA6 is part of the family of calcium-dependent membrane and phospholipid binding proteins. ANXA6 mediats the endosome aggregation and vesicle fusion in secreting epithelia during exocytosis. ANXA6 correlates with CD21. ANXA6 regulates the release of Ca(2+) from intracellular stores. ANXA6 is differentially expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period.

    • Synonyms

      ANX6, ANXA6, Annexin-VI, Lipocortin-6, Lipocortin-VI, Annexin-6, CPB-II, Annexin A6, p68, p70, Protein III, Chromobindin-20, 67 kDa calelectrin, Calphobindin-II, CBP68.

    • 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 MAKPAQGAKY RGSIHDFPGF DPNQDAEALY TAMKGFGSDK EAILDIITSR SNRQRQEVCQ SYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYCDAKE IKDAISGIGT DEKCLIEILA SRTNEQMHQL VAAYKDAYER DLEADIIGDT SGHFQKMLVV LLQGTREEDD VVSEDLVQQD VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS LYSMIKNDTS GEYKKTLLKL SGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA DFNPDADAK ALRKAMKGLG TDEDTIIDII THRSNVQRQQ IRQTFKSHFG RDLMTDLKSE ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI RAINEAYKED YHKSLEDALS SDTSGHFRRI LISLATGHRE EGGENLDQAR EDAQVAAEIL EIADTPSGDK TSLETRFMTI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDAF VAIVQSVKNK PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD FLKALLALCG GED.

    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.

    Anxa6 Human
  • View Data Sheet

    Name :

    OXSM Human

    Description:

    3-Oxoacyl-ACP Synthase, Mitochondrial Human Recombinant

    3-Oxoacyl-ACP Synthase Mitochondrial, Type II Mitochondrial Beta-Ketoacyl Synthase, 3-Ketoacyl-Acyl Carrier Protein Synthase, FASN2D, KASI, EC 2.3.1, Beta-Ketoacyl-ACP Synthase.

    Product # :

    ENZ-751

    Price :

    Quantity :

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    Description

    OXSM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (28-459) and having a molecular mass of 48.1kDa.OXSM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OXSM solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      OXSM, a beta-ketoacyl synthetase, is essential for elongation of fatty acid chains in the mitochondria. Alternatively spliced transcript variants were found.

    • Synonyms

      3-Oxoacyl-ACP Synthase Mitochondrial, Type II Mitochondrial Beta-Ketoacyl Synthase, 3-Ketoacyl-Acyl Carrier Protein Synthase, FASN2D, KASI, EC 2.3.1, Beta-Ketoacyl-ACP Synthase.

    • 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 MGSKRKFFGT VPISRLHRRV VITGIGLVTP LGVGTHLVWD RLIGGESGIV SLVGEEYKSI PCSVAAYVPR GSDEGQFNEQ NFVSKSDIKS MSSPTIMAIG AAELAMKDSG WHPQSEADQV ATGVAIGMGM IPLEVVSETA LNFQTKGYNK VSPFFVPKIL VNMAAGQVSI RYKLKGPNHA VSTACTTGAH AVGDSFRFIA HGDADVMVAG GTDSCISPLS LAGFSRARAL STNSDPKLAC RPFHPKRDGF VMGEGAAVLV LEEYEHAVQR RARIYAEVLG YGLSGDAGHI TAPDPEGEGA LRCMAAALKD AGVQPEEISY INAHATSTPL GDAAENKAIK HLFKDHAYAL AVSSTKGATG HLLGAAGAVE AAFTTLACYY QKLPPTLNLD CSEPEFDLNY VPLKAQEWKT EKRFIGLTNS FGFGGTNATL CIAGL.

    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.

    Oxsm Human
  • View Data Sheet

    Name :

    LAMP1 Human

    Description:

    Lysosomal-Associated Membrane Protein Human 1 Recombinant

    Lysosome-associated membrane glycoprotein 1, LAMP1, CD107a, LAMPA, LGP120, LAMP-1, CD107 antigen-like family member A.

    Product # :

    PRO-2478

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    Description

    LAMP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 363 amino acids (29-382a.a.) and having a molecular mass of 39.4kDa. (Molecular size on SDS-PAGE will appear at approximately 57-70kDa).LAMP1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LAMP1 protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lysosomal-Associated Membrane Protein 1 (LAMP1) is a part of the LAMP family. LAMP1 is a membrane protein which is expressed in the endosome-lysosome membranes of cells and is implicated in tumor cell metastasis. A glycoform of LAMP1 is expressed on the surface of activated macrophages and promotes T cell costimulation and a Th1 biased immune response. LAMP1 is also found on the plasma membrane during the activation of NK cells, CD8 & T cells, monocytes, basophils, and platelets.

    • Synonyms

      Lysosome-associated membrane glycoprotein 1, LAMP1, CD107a, LAMPA, LGP120, LAMP-1, CD107 antigen-like family member A.

    • 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

      ADPAMFMVKN GNGTACIMAN FSAAFSVNYD TKSGPKNMTF DLPSDATVVL NRSSCGKENT SDPSLVIAFG RGHTLTLNFT RNATRYSVQL MSFVYNLSDT HLFPNASSKE IKTVESITDI RADIDKKYRC VSGTQVHMNN VTVTLHDATI QAYLSNSSFS RGETRCEQDR PSPTTAPPAP
      PSPSPSPVPK SPSVDKYNVS GTNGTCLLAS MGLQLNLTYE RKDNTTVTRL LNINPNKTSA SGSCGAHLVT LELHSEGTTV LLFQFGMNAS SSRFFLQGIQ LNTILPDARD PAFKAANGSL RALQATVGNS YKCNAEEHVR VTKAFSVNIF KVWVQAFKVE GGQFGSVEEC LLDENSMHHH
      HHH

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    Lamp1 Human
  • View Data Sheet

    Name :

    TSTD1 Human

    Description:

    Thiosulfate Sulfurtransferase Like Domain Containing 1 Human Recombinant

    Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 1, TSTD1, KAT.

    Product # :

    ENZ-094

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    Description

    TSTD1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids (1-115 a.a.) and having a molecular mass of 14.6kDa.TSTD1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TSTD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thiosulfate sulfurtransferase like domain containing 1 (TSTD1) is a member of a family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. TSTD1 is localized around the nuclear membranes. TSTD1 is expressed in a number of human tissues, including the kidney, liver, skeletal muscle, heart, colon, thymus, spleen, placenta and lung. TSTD1 may participate in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes.

    • Synonyms

      Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 1, TSTD1, KAT.

    • 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 MAGAPTVSLP ELRSLLASGR ARLFDVRSRE EAAAGTIPGA LNIPVSELES ALQMEPAAFQ ALYSAEKPKL EDEHLVFFCQ MGKRGLQATQ LARSLGYTGA RNYAGAYREW LEKES.

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    Tstd1 Human
  • View Data Sheet

    Name :

    GPT Human, His Active

    Description:

    Glutamic-Pyruvate Transaminase, His Tag Active Human Recombinant

    Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    Product # :

    ENZ-1000

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    Description

    GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPT solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

    • Synonyms

      Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    • 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 MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS

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    Gpt Human His Active
  • View Data Sheet

    Name :

    WWOX Human

    Description:

    WW Domain Containing Oxidoreductase Human Recombinant

    FOR, WOX1, FRA16D, HHCMA56, PRO0128, SDR41C1, D16S432E, WWOX, WW domain-containing oxidoreductase, Fragile site FRA16D oxidoreductase.

    Product # :

    ENZ-422

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    Description

    WWOX Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 254 amino acids (1-234 a.a.) and having a molecular mass of 28.3 kDa.The WWOX is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The WWOX solution (1mg/ml) contains 20mM Tris pH-8, & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      WWOX is a proapoptotic protein and a tumor suppressor protein. WWOX is found in all eukaryotes and involved in the regulation of a broad range of cellular functions such as protein degradation, transcription, and RNA splicing. WWOX functions synergistically with TP53/p53 to control genotoxic stress-induced cell death. WWOX takes part in tumor necrosis factor (TNF)-mediated cell death. Loss of WWOX expression is associated with pancreatobiliary cancers. Reduced expression levels of WWOX protein is associated with the pathogenesis of basal-like differentiation in breast cancer. Loss of WWOX expression is associated with extrahepatic cholangiocarcinoma. WWOX gene alteration is an early genetic alteration contributes to oral carcinogenesis. WWOX induces apoptosis and inhibits human hepatocellular carcinoma cell growth through a mechanism enhanced by JNK inhibition.

    • Synonyms

      FOR, WOX1, FRA16D, HHCMA56, PRO0128, SDR41C1, D16S432E, WWOX, WW domain-containing oxidoreductase, Fragile site FRA16D oxidoreductase.

    • 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 MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG KRKRVAGDLP YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK PTTRQRYDGS TTAMEILQGR DFTGKVVVVT GANSGIGFET AKSFALHGAH VILACRNMAR ASEAVSRILE EWQQGAATTV YCAAVPELEG LGGMYFNNCC RCMPSPEAQS EETARTLWAL SERLIQERLG SQSG.

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    Wwox Human
  • View Data Sheet

    Name :

    DUSP3 Antibody

    Description:

    Dual Specificity Phosphatase 3, Mouse Anti Human

    Dual specificity phosphatase 3, VHR, Vaccinia virus phosphatase VH1-related, Dual specificity protein phosphatase VHR, Vaccinia H1-related phosphatase, serine/threonine specific protein phosphatase, DUSP3.

    Product # :

    ANT-594

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      DUSP3 belongs to the dual specificity protein phosphatase subfamily which inactivates their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. DUSP3 negatively regulate members of the mitogen-activated protein kinase superfamily that are related to cellular proliferation and differentiation. DUSP3 is expressed in both breast and ovarian tissues and displays activity both for tyrosine-protein phosphate and serine-protein phosphate, but exhibits a strong preference toward phosphotyrosines, specifically dephosphorylates and inactivates ERK1 and ERK2.

    • Synonyms

      Dual specificity phosphatase 3, VHR, Vaccinia virus phosphatase VH1-related, Dual specificity protein phosphatase VHR, Vaccinia H1-related phosphatase, serine/threonine specific protein phosphatase, DUSP3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human DUSP3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human DUSP3 amino acids 1-185 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT9E6AT.

    • Applications

      DUSP3 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution for Western blot analysis is 1:3000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      DUSP3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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    Dusp3 Antibody
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    bdnf activity - Product image 1

    Citations

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

      What is the source or expression system of BDNF Protein?
      Escherichia Coli.

      What is the Purity of BDNF Protein?
      BDNF Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

      What applications can BDNF Protein be used in?
      BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BDNF Protein?
      The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.

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    Bdnf Human
  • View Data Sheet

    Name :

    ACAT2 Human

    Description:

    Acetyl-Coenzyme A acetyltransferase 2 Human Recombinant

    Acetyl-CoA acetyltransferase cytosolic, Cytosolic acetoacetyl-CoA thiolase, ACAT2, Acetyl CoA transferase-like protein, ACAT-2.

    Product # :

    ENZ-295

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    Description

    ACAT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kDa. The ACAT2 is fused to 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACAT2 Human solution containing 20mM Tris pH-8, 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus.

    • Synonyms

      Acetyl-CoA acetyltransferase cytosolic, Cytosolic acetoacetyl-CoA thiolase, ACAT2, Acetyl CoA transferase-like protein, ACAT-2.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNAG SDPVVIVSAA RTIIGSFNGA LAAVPVQDLG STVIKEVLKR ATVAPEDVSE
      VIFGHVLAAG CGQNPVRQAS VGAGIPYSVP AWSCQMICGS GLKAVCLAVQ SIGIGDSSIV VAGGMENMSK APHLAYLRTG VKIGEMPLTD SILCDGLTDA FHNCHMGITA ENVAKKWQVS REDQDKVAVL SQNRTENAQK AGHFDKEIVP VLVSTRKGLI EVKTDEFPRH GSNIEAMSKL KPYFLTDGTG TVTPANASGI NDGAAAVVLM KKSEADKRGL TPLARIVSWS QVGVEPSIMG IGPIPAIKQA VTKAGWSLED VDIFEINEAF AAVSAAIVKE LGLNPEKVNI EGGAIALGHP LGASGCRILV TLLHTLERMG RSRGVAALCI GGGMGIAMCV QR.

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    Acat2 Human
  • View Data Sheet

    Name :

    ADPRH Human

    Description:

    ADP-Ribosylarginine Hydrolase Human Recombinant

    [Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

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    ENZ-631

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    Description

    ADPRH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 42.1kDa.ADPRH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADPRH solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.

    • Synonyms

      [Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

    • 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 MGSHMEKYVA AMVLSAAGDA LGYYNGKWEF LQDGEKIHRQ LAQLGGLDAL DVGRWRVSDD TVMHLATAEA LVEAGKAPKL TQLYYLLAKH YQDCMEDMDG RAPGGASVHN AMQLKPGKPN GWRIPFNSHE GGCGAAMRAM CIGLRFPHHS QLDTLIQVSI ESGRMTHHHP TGYLGALASA LFTAYAVNSR PPLQWGKGLM ELLPEAKKYI VQSGYFVEEN LQHWSYFQTK WENYLKLRGI LDGESAPTFP ESFGVKERDQ FYTSLSYSGW GGSSGHDAPM IAYDAVLAAG DSWKELAHRA FFHGGDSDST AAIAGCWWGV MYGFKGVSPS NYEKLEYRNR
      LEETARALYS LGSKEDTVIS L.

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    Adprh Human
  • View Data Sheet

    Name :

    AICDA Human

    Description:

    Activation-Induced Cytidine Deaminase Human Recombinant

    Single-stranded DNA cytosine deaminase, Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.

    Product # :

    ENZ-651

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    Description

    AICDA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-198) and having a molecular mass of 26.1kDa.AICDA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AICDA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Activation-Induced Cytidine Deaminase (AICDA) belongs to the the cytidine deaminase family. AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination in B-lymphocytes. AICDA is necessary for a number of crucial steps of B-cell terminal differentiation needed for efficient antibody responses. AICDA has a role in the epigenetic regulation of gene expression by participating in DNA demethylation. AICDA is strongly expressed in the lymph nodes and tonsils.

    • Synonyms

      Single-stranded DNA cytosine deaminase, Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.

    • 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 MDSLLMNRRK FLYQFKNVRW AKGRRETYLC YVVKRRDSAT SFSLDFGYLR NKNGCHVELL FLRYISDWDL DPGRCYRVTW FTSWSPCYDC ARHVADFLRG NPNLSLRIFT ARLYFCEDRK AEPEGLRRLH RAGVQIAIMT FKDYFYCWNT FVENHERTFK
      AWEGLHENSV RLSRQLRRIL LPLYEVDDLR DAFRTLGL.

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    Aicda Human
  • View Data Sheet

    Name :

    NAA50 Human

    Description:

    N Alpha-Acetyltransferase 50, NatE Catalytic Subunit Human Recombinant

    N-alpha-acetyltransferase 50, N-acetyltransferase 13, N-acetyltransferase 5, hNAT5, N-acetyltransferase san homolog, hSAN, NatE catalytic subunit, NAA50, MAK3, NAT13, NAT5, SAN.

    Product # :

    ENZ-424

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    Description

    NAA50 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (1-169) and having a molecular mass of 21.9kDa.NAA50 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NAA50 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      N-alpha-acetyltransferase 50 (NAA50) consists of 169 amino acid cytoplasmic protein belonging to the acetyltransferase family and GNAT subfamily. NAA50 is a likely catalytic component of the ARD1A-NARG1 complex which displays alpha acetyltransferase activity. NAA50 has also been shown to interact with MAK10 and is encoded by a gene that maps to human chromosome 3q13.2.

    • Synonyms

      N-alpha-acetyltransferase 50, N-acetyltransferase 13, N-acetyltransferase 5, hNAT5, N-acetyltransferase san homolog, hSAN, NatE catalytic subunit, NAA50, MAK3, NAT13, NAT5, SAN.

    • 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 MGSHMKGSRI ELGDVTPHNI KQLKRLNQVI FPVSYNDKFY KDVLEVGELA KLAYFNDIAV GAVCCRVDHS QNQKRLYIMT LGCLAPYRRL GIGTKMLNHV LNICEKDGTF DNIYLHVQIS NESAIDFYRK FGFEIIETKK NYYKRIEPAD AHVLQKNLKV
      PSGQNADVQK TDN.

    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.

    Naa50 Human
  • View Data Sheet

    Name :

    FBL Human

    Description:

    Fibrillarin Human Recombinant

    rRNA 2'-O-methyltransferase fibrillarin, 34 kDa nucleolar scleroderma antigen, FBL, FIB1, FLRN, fibrillarin, FIB, RNU3IP1.

    Product # :

    ENZ-566

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    Description

    FBL Human Recombinant fused with 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 262 amino acids (83-321 a.a.) and having a molecular mass of 28.9kDa. The FBL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FBL solution contains Phosphate buffered saline (pH 7.4), 30% glycerol, and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FBL is a significant small nucleolar protein in eukaryotes, which has an essential role in pre-rRNA processing during ribosomal biogenesis. Fibrillarin is a component of several ribonucleoproteins including a nucleolar small nuclear ribonucleoprotein (SnRNP) and one of the two classes of small nucleolar ribonucleoproteins (snoRNPs). Fibrillarin contains an N-terminal repetitive domain which is rich in glycine and arginine residues, like fibrillarins in other species. Fibrillarin’s central region is similar to an RNA-binding domain and contains an RNP consensus sequence. FBL is linked to the U3, U8, and U13 small nuclear RNAs and is positioned in the dense fibrillar component (DFC) of the nucleolus. Antisera from roughly 8% of humans with the autoimmune disease scleroderma recognize fibrillarin.

    • Synonyms

      rRNA 2'-O-methyltransferase fibrillarin, 34 kDa nucleolar scleroderma antigen, FBL, FIB1, FLRN, fibrillarin, FIB, RNU3IP1.

    • 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 RSMGKNVMVE PHRHEGVFIC RGKEDALVTK NLVPGESVYG EKRVSISEGD DKIEYRAWNP FRSKLAAAIL GGVDQIHIKP GAKVLYLGAA SGTTVSHVSD IVGPDGLVYA VEFSHRSGRD LINLAKKRTN IIPVIEDARH PHKYRMLIAM VDVIFADVAQ PDQTRIVALN AHTFLRNGGH FVISIKANCI DSTASAEAVF ASEVKKMQQE NMKPQEQLTL EPYERDHAVV VGVYRPPPKV KN.

    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.

    Fbl Human
  • View Data Sheet

    Name :

    CAT Human

    Description:

    Catalase Human Recombinant

    Catalase, CAT.

    Product # :

    ENZ-629

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    Description

    CAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 547 amino acids (1-527) and having a molecular mass of 61.9kDa.CAT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CAT solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >30,000 unit/mg.

    Citations

    More Info

    • Introduction

      Catalase (CAT) is a key antioxidant enzyme in the body’s defense against oxidative stress. Furthermore, Catalase is a heme enzyme which is present in the peroxisome of virtually all aerobic cells. Catalase converts the reactive oxygen species hydrogen peroxide to water and oxygen and thus diminishes the toxic effects of hydrogen peroxide. Catalase stimulates growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. Catalase gene polymorphisms are linked with decreases in catalase activity nevertheless, to date, acatalasemia is the only disease known to be caused by the CAT gene.

    • Synonyms

      Catalase, CAT.

    • Physical Appearance

      Sterile filtered yellowish 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 MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL.

    • Unit Definition

      One unit will decompose 1.0 umole of H2O2 per minute at pH 8.0 at 25°C.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cat Human
  • View Data Sheet

    Name :

    UPP1 E.coli

    Description:

    Uridine Phosphorylase E.coli Recombinant

    UPASE, UDRPASE, UPP, UDP.

    Product # :

    ENZ-258

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    Description

    UPP1 E.Coli Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 29.3 kDa. UPP1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UPP1 solution (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.

    • Synonyms

      UPASE, UDRPASE, UPP, UDP.

    • 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 MSKSDVFHLG LTKNDLQGAT LAIVPGDPDR VEKIAALMDK PVKLASHREF TTWRAELDGK PVIVCSTGIG GPSTSIAVEE LAQLGIRTFL RIGTTGAIQP HINVGDVLVT TASVRLDGAS LHFAPLEFPA VADFECTTAL VEAAKSIGAT THVGVTASSD TFYPGQERYD TYSGRVVRHF KGSMEEWQAM GVMNYEMESA TLLTMCASQG LRAGMVAGVI VNRTQQEIPN AETMKQTESH AVKIVVEAAR RLL.

    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.

    Upp1
  • View Data Sheet

    Name :

    GSTM1 Mouse, His

    Description:

    Glutathione S-Transferase M1 Mouse Recombinant, His Tag

    GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    Product # :

    ENZ-456

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    Description

    GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 28.1kDa. The GTM1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM1 solution contains 20 mM Tris-HCl buffer ( pH8.0), 1mM DTT and 10% glycerol

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 11 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

    Citations

    More Info

    • Introduction

      Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

    • Synonyms

      GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    • 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 MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK.

    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.

    Gstm1 Mouse His
  • View Data Sheet

    Name :

    PTPN6 Human

    Description:

    Protein Tyrosine Phosphatase Non Receptor Type-6 Human Recombinant

    Tyrosine-protein phosphatase non-receptor type 6, EC 3.1.3.48, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SHP-1, PTPN6, HCP, HCPH, SHP1, HPTP1C, SHP-1L.

    Product # :

    PKA-221

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    Description

    PTPN6 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 300 amino acids and having a molecular mass of 34.3 kDa. The protein coding region of the catalytic domain of PTPN6 (amino acids 243-541). The catalytic domain of PTPN6 was overexpressed as insoluble protein aggregates (inclusion bodies). The recombinant PTPN6 protein was purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. Additional amino acid(Met) is attached at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 25mM Tris-HCl, pH 7.5, 2mM b-mercaptoethanol, 1mM EDTA, 1mMDTT and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PTPN6 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.

    • Synonyms

      Tyrosine-protein phosphatase non-receptor type 6, EC 3.1.3.48, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SHP-1, PTPN6, HCP, HCPH, SHP1, HPTP1C, SHP-1L.

    • 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

      MGFWEEFES LQKQEVKNLH QRLEGQRPEN KGKNRYKNIL PFDHSRVILQ GRDSNIPGSD YINANYIKNQ LLGPDENAKT YIASQGCLEA TVNDFWQMAW QENSRVIVMT TREVEKGRNK CVPYWPEVGM QRAYGPYSVT NCGEHDTTEY KLRTLQVSPL DNGDLIREIW HYQYLSWPDH GVPSEPGGVL SFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ENISTKGLDCDIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEVLQSQK GQESEYGNITY.

    • Unit Definition

      One unit will hydrolyze 1 nanomole of p-nitrophenylphosphatate per minute at pH 7.5 at 37°C using 10mM of substrate.

    • Specific Activity

      >5,000 U/mg of PTPN6.

    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.

    Ptpn6 Human
  • View Data Sheet

    Name :

    DnaK ATPase-BD E.Coli

    Description:

    DnaK ATPase Binding Domain E.Coli Recombinant

    HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

    Product # :

    HSP-010

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    Description

    Recombinant DnaK Substrate Binding Domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids and having a molecular mass of 41.6 kDa.

    Source

    Escherichia Coli.

    Formulation

    The DnaK protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP-70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.
      DnaK(amino acids1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain (residues 385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques.

    • Synonyms

      HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

    • 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

      MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVTNPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVLKKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYGLDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYLVEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKEPRKDVNPDEA VAIGAAVQGG VLTG.

    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.

    Dnak Atpase Bd
  • View Data Sheet

    Name :

    Ostreolysin

    Description:

    Ostreolysin Pleurotus Ostreatus Recombinant

    Product # :

    PRO-2600

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    Description

    Pleurotus Ostreatus Ostreolysin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15 kDa. The Ostreolysin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Ostreolysin protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Ostreolysin has potent anti-carcinogenic activity in several colon cancer cell lines. 

    Citations

    More Info

    • Introduction

      Ostreolysin is extracted from Pleurotus ostreatus (oyster mushroom). It is a pore forming protein, which contains a lytic part to both cholesterol and sphingomyelin containing membranes. Because of their cholesterol content and the appearance of ostreolysin in the detergent resistant membranes, ostreolysin is cytotoxic towards the ovary cells of Chinese hamster. It seems that Ostreolysin spots a rich lipid cholesterol phase, presumably the liquid ordered phase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pleurotus Ostreatus Ostreolysin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted Ostreolysin should be stored at 4°C below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Ostreolysin in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The N-terminal amino sequence is Ala-Tyr-Ala-Gln-Trp-Val.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 2.64 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNA-man computer analysis program.

    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.

    Ostreolysin
  • View Data Sheet

    Name :

    Prolactin Mouse

    Description:

    Prolactin Mouse Recombinant

    Mammotropin, Luterotropic hormone, Lutetropin, PRL.

    Product # :

    CYT-321

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    Description

    Prolactin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.5 kDa. The Prolactin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Leu-Pro-Ile-Cys-Ser.

    Citations

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    • Introduction

      Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

    • Synonyms

      Mammotropin, Luterotropic hormone, Lutetropin, PRL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Pro-Ile-Cys.

    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.

    Prolactin Mouse
  • View Data Sheet

    Name :

    TYRP1 Human

    Description:

    Tyrosinase Related Protein 1 Human Recombinant

    Tyrosinase Related Protein 1, Tyrosinase-Related Protein 1, Melanoma Antigen Gp75, Glycoprotein 75, DHICA Oxidase, Catalase B, CAS2, TRP1, TYRP, TRP, 5,6-Dihydroxyindole-2-Carboxylic Acid Oxidase, EC 1.14.18.1, EC 1.14.18.-, EC 1.14.18, B-PROTEIN, TRP-1, TYRRP, CATB, GP75, OCA3, 5,6-dihydroxyindole-2-carboxylic acid oxidase.

    Product # :

    PRO-2350

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    Description

    TYRP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 462 amino acids (25-477a.a) and having a molecular mass of 52.5kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).TYRP1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TYRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TYRP1, also known as 5, 6-dihydroxyindole-2-carboxylic acid oxidase, is a melanosomal enzyme which is a member of the tyrosinase family and takes a significant part in the melanin biosynthetic pathway. TYRP1 is a melanocyte-specific gene which is involved in eumelanin synthesis. Furthermore, TYRP1 is implicated in the oxidation of 5,6-dihydroxyindole-2-carboxylic acid-DHICA into indole-5,6-quinone-2-carboxylic acid. TYRP1 is regulated by the microphthalmia-associatedtranscription factor-MITF.

    • Synonyms

      Tyrosinase Related Protein 1, Tyrosinase-Related Protein 1, Melanoma Antigen Gp75, Glycoprotein 75, DHICA Oxidase, Catalase B, CAS2, TRP1, TYRP, TRP, 5,6-Dihydroxyindole-2-Carboxylic Acid Oxidase, EC 1.14.18.1, EC 1.14.18.-, EC 1.14.18, B-PROTEIN, TRP-1, TYRRP, CATB, GP75, OCA3, 5,6-dihydroxyindole-2-carboxylic acid oxidase.

    • 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

      ADLQFPRQCA TVEALRSGMC CPDLSPVSGP GTDRCGSSSG RGRCEAVTAD SRPHSPQYPH DGRDDREVWP LRFFNRTCHC NGNFSGHNCG TCRPGWRGAA CDQRVLIVRR NLLDLSKEEK NHFVRALDMA KRTTHPLFVI ATRRSEEILG PDGNTPQFEN ISIYNYFVWT HYYSVKKTFL GVGQESFGEV DFSHEGPAFL TWHRYHLLRL EKDMQEMLQE PSFSLPYWNF ATGKNVCDIC TDDLMGSRSN FDSTLISPNS VFSQWRVVCD SLEDYDTLGT LCNSTEDGPI RRNPAGNVAR PMVQRLPEPQ DVAQCLEVGL FDTPPFYSNS TNSFRNTVEG YSDPTGKYDP AVRSLHNLAH LFLNGTGGQT HLSPNDPIFV LLHTFTDAVF DEWLRRYNAD ISTFPLENAP IGHNRQYNMV PFWPPVTNTE MFVTAPDNLG YTYEIQWPSR EFSVPEHHHH HH.

    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.

    Tyrp1 Human
  • View Data Sheet

    Name :

    MAP2K1 Human

    Description:

    Mitogen-Activated Protein Kinase Kinase 1 Human Recombinant

    MAP2K1, MEK1, PRKMK1, MKK1, MAPKK 1, MAP kinase kinase 1.

    Product # :

    PKA-112

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    MAP2K1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 402 amino acids (1-393a.a.) and having a molecular mass of 44.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MAP2K1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MAP2K1 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The MAP2K1 protein is encoded by the MAP2K1 gene. This enzyme serves as a MAP (mitogen activated protein) kinase, it is a part of the dual specificity protein kinase family. Extracellular signal-regulated kinases such as MAP kinases has an important role in assimilation of various biochemical signals. MAP2K1 is located upstream to the MAP kinases and activates them by multiple intra and extracellular signals. The enzyme serves as a key factor in the signal transduction pathway of MAP kinase, therefore it takes part in the cell development (transcription regulation, proliferation, differentiation etc.).

    • Synonyms

      MAP2K1, MEK1, PRKMK1, MKK1, MAPKK 1, MAP kinase kinase 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

      ADPMPKKKPT PIQLNPAPDG SAVNGTSSAE TNLEALQKKL EELELDEQQR KRLEAFLTQK QKVGELKDDD FEKISELGAG NGGVVFKVSH KPSGLVMARK LIHLEIKPAI RNQIIRELQV LHECNSPYIV GFYGAFYSDG EISICMEHMD GGSLDQVLKK AGRIPEQILG KVSIAVIKGL TYLREKHKIM HRDVKPSNIL VNSRGEIKLC DFGVSGQLID SMANSFVGTR SYMSPERLQG THYSVQSDIW SMGLSLVEMA VGRYPIPPPD AKELELMFGC QVEGDAAETP PRPRTPGRPL SSYGMDSRPP MAIFELLDYI VNEPPPKLPS GVFSLEFQDF VNKCLIKNPA ERADLKQLMV HAFIKRSDAE EVDFAGWLCS TIGLNQPSTP THAAGVHHHH HH.

    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.

    Map2K1 Human
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