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Search results

1000 results found for “glyoxalase”

Name

Description

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  • View Data Sheet

    Name :

    SOX2 Human

    Description:

    SRY (sex determining region Y)-box 2 Human Recombinant

    MCOPS3, ANOP3, MGC2413, SOX2, SRY (sex determining region Y)-box 2.

    Product # :

    PRO-820

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    Description

    SOX2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids (1-200 a.a.) and having a molecular mass of 23.1kDa. SOX2 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    The SOX2 solution contains 20mM Tris-HCl pH-8, 2mM DTT, 0.2M NaCl & 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SOX2 is a transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. SOX4 is important for early embryogenesis and for embryonic stem cell pluripotency.

    • Synonyms

      MCOPS3, ANOP3, MGC2413, SOX2, SRY (sex determining region Y)-box 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

      MYNMMETELK PPGPQQTSGG GGGNSTAAAA GGNQKNSPDR VKRPMNAFMV WSRGQRRKMA QENPKMHNSE ISKRLGAEWK LLSETEKRPF IDEAKRLRAL HMKEHPDYKY RPRRKTKTLM KKDKYTLPGG LLAPGGNSMA SGVGVGAGLG AGVNQRMDSY AHMNGWSNGS YSMMQDQLGY PQHPGLNAHG AAQMQPMHRY LEHHHHHH.

    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.

    Sox2 Human
  • View Data Sheet

    Name :

    UBE2V2 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2 Variant 2 Human Recombinant

    DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.

    Product # :

    ENZ-550

    Price :

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    Description

    UBE2V2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145 a.a.) and having a molecular mass of 18.5 kDa. The UBE2V2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2V2 Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2V2 comprises a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes however require the conserved cysteine residue that is vital for the catalytic activity of E2s. UBE2V2 shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. UBE2V2 participates in the differentiation of monocytes and enterocytes.

    • Synonyms

      DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.

    • 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 MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ ELRRLMMSKE NMKLPQPPEG QTYNN.

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

    Ube2V2 Human
  • View Data Sheet

    Name :

    UBE2W Human

    Description:

    Ubiquitin Conjugating Enzyme E2W Human Recombinant

    Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.

    Product # :

    ENZ-117

    Price :

    Quantity :

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    • description
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    Description

    UBE2W produced in E.Coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (1-151 a.a.) and having a molecular mass of 19.5kDa.UBE2W is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2W solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2W receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2W catalyzes monoubiquitination and 'Lys-11'-linked polyubiquitination. UBE2W is broadly expressed, particularly at highest levels in the testis.

    • Synonyms

      Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      UBE2W Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C.

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

    Ube2W Human
  • View Data Sheet

    Name :

    TDP2 Human

    Description:

    Tyrosyl-DNA Phosphodiesterase 2 Human Recombinant

    AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein II.

    Product # :

    ENZ-698

    Price :

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    Description

    TDP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362) and having a molecular mass of 43.3kDa. TDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TDP2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosyl-DNA Phosphodiesterase 2 (TDP2), belongs to the CCR4/nocturin family of divalent cation-dependent phosphodiesterases.TDP2 associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. TDP2 is characterized by similar sequence and structure as APE1 endonuclease, which participates in DNA repair and the activation of transcription factors.

    • Synonyms

      AD022, dJ30M3.3, EAP2, EAPII, RP1-30M3.3, TTRAP, 5'-tyrosyl-DNA phosphodiesterase,hTDP2, ETS1-associated protein 2, ETS1-associated protein 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 MGSMELGSCL EGGREAAEEE GEPEVKKRRL LCVEFASVAS CDAAVAQCFL AENDWEMERA LNSYFEPPVE ESALERRPET ISEPKTYVDL TNEETTDSTT SKISPSEDTQ QENGSMFSLI TWNIDGLDLN NLSERARGVC SYLALYSPDV IFLQEVIPPY YSYLKKRSSN YEIITGHEEG YFTAIMLKKS RVKLKSQEII PFPSTKMMRN LLCVHVNVSG NELCLMTSHL ESTRGHAAER MNQLKMVLKK MQEAPESATV IFAGDTNLRD REVTRCGGLP NNIVDVWEFL GKPKHCQYTW DTQMNSNLGI TAACKLRFDR IFFRAAAEEG HIIPRSLDLL GLEKLDCGRF PSDHWGLLCN LDIIL.

    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.

    Tdp2 Human
  • View Data Sheet

    Name :

    Cyclophilin C Human

    Description:

    Cyclophilin-C Human Recombinant

    Peptidylprolyl Isomerase C (Cyclophilin C), Cyclophilin C, Rotamase C, EC 5.2.1.8, PPIase C, CYPC, Peptidyl-Prolyl Cis-Trans Isomerase C, Parvulin, PPIC.

    Product # :

    ENZ-809

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
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    • More Info

    Description

    Cyclophilin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Phe29-Trp212) containing 194 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 21.3kDa.

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin-C was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cyclophilin-C belongs to the peptidyl-prolyl cis-trans isomerase (PPIase)) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Like other PPIases, the Cyclophilin-C protein can bind immunosuppressant cyclosporin A.

    • Synonyms

      Peptidylprolyl Isomerase C (Cyclophilin C), Cyclophilin C, Rotamase C, EC 5.2.1.8, PPIase C, CYPC, Peptidyl-Prolyl Cis-Trans Isomerase C, Parvulin, PPIC.

    • 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

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Cyclophilin-C is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASFRKRGPSVTA KVFFDVRIGD KDVGRIVIGL FGKVVPKTVE NFVALATGEK GYGYKGSKFH RVIKDFMIQG GDITTGDGTG GVSIYGETFP DENFKLKHYG IGWVSMANAG PDTNGSQFFI TLTKPTWLDG KHVVFGKVID GMTVVHSIEL QATDGHDRPL TNCSIINSGK IDVKTPFVVE IADW.

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    Cyclophilin C Human
  • View Data Sheet

    Name :

    UBE2S Human

    Description:

    Ubiquitin Conjugating Enzyme E2S Human Recombinant

    Ubiquitin-conjugating enzyme E2 S, Ubiquitin-protein ligase S, Ubiquitin carrier protein S, Ubiquitin-conjugating enzyme E2-24 kDa, E2-EPF5, E2-EPF, UBE2S, E2EPF, EPF5.

    Product # :

    ENZ-444

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    Description

    UBE2S Human Recombinant fused with a 36 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 258 amino acids (1-222 a.a.) and having a molecular mass of 27.9kDa.The UBE2S is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2S solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-conjugating enzyme E2S (UBE2S) belongs to the ubiquitin-conjugating enzyme family. UBE2S is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme-dependent manner, a typical property of ubiquitin carrier proteins. UBE2S catalyzes the covalent attachment of ubiquitin to other proteins. UBE2S acts as a crucial factor of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by purposely elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, augmenting the degradation of APC/C substrates by the proteasome and promoting mitotic exit. UBE2S also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is nevertheless uncertain whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and consequent degradation of VHL, resulting in an accumulation of HIF1A.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 S, Ubiquitin-protein ligase S, Ubiquitin carrier protein S, Ubiquitin-conjugating enzyme E2-24 kDa, E2-EPF5, E2-EPF, UBE2S, E2EPF, EPF5.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNSN VENLPPHIIR LVYKEVTTLT ADPPDGIKVF PNEEDLTDLQ VTIEGPEGTP YAGGLFRMKL LLGKDFPASP PKGYFLTKIF HPNVGANGEI CVNVLKRDWT AELGIRHVLL TIKCLLIHPN PESALNEEAG RLLLENYEEY AARARLLTEI HGGAGGPSGR AEAGRALASG TEASSTDPGA PGGPGGAEGP MAKKHAGERD KKLAAKKKTD KKRALRRL.

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    Ube2S 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

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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.

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    Echdc1 Human
  • View Data Sheet

    Name :

    UBA5 Human

    Description:

    Ubiquitin-Like Modifier Activating Enzyme 5 Human Recombinant

    Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.

    Product # :

    ENZ-602

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    Description

    UBA5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-404) and having a molecular mass of 47.4kDa.UBA5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBA5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-like modifier activating enzyme 5 (UBA5) is a member of the ubiquitin-activating E1 family and UBA5 subfamily. Ubiquitin and ubiquitin-like proteins are recognized as covalently conjugated to various cellular substrates by a three-step enzymatic pathway. The ubiquitin-activating enzyme (E1) has a vital role in the first step of ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. UBA5 activates an ubiquitin-like protein, ubiquitin-fold modifier 1 (Ufm1), by forming a high-energy thioester bond. UBA5 is located primarily in cytoplasm, while it generally localizes to the nucleus in presence of SUMO2.

    • Synonyms

      Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.

    • 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 MGSHMAESVE RLQQRVQELE RELAQERSLQ VPRSGDGGGG RVRIEKMSSE VVDSNPYSRL MALKRMGIVS DYEKIRTFAV AIVGVGGVGS VTAEMLTRCG IGKLLLFDYD KVELANMNRL FFQPHQAGLS KVQAAEHTLR NINPDVLFEV HNYNITTVEN
      FQHFMDRISN GGLEEGKPVD LVLSCVDNFE ARMTINTACN ELGQTWMESG VSENAVSGHI QLIIPGESAC FACAPPLVVA ANIDEKTLKR EGVCAASLPT TMGVVAGILV QNVLKFLLNF GTVSFYLGYN AMQDFFPTMS MKPNPQCDDR NCRKQQEEYK KKVAALPKQE VIQEEEEIIH
      EDNEWGIELV SEVSEEELKN FSGPVPDLPE GITVAYTIPK KQEDSVTELT VEDSGESLED LMAKMKNM.

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    Uba5 Human
  • View Data Sheet

    Name :

    Cyclophilin B Mouse

    Description:

    Cyclophilin-B Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

    Product # :

    ENZ-1039

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    Description

    Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.

    More Info

    • Introduction

      Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

    • 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 MGSMNDKKKG PKVTVKVYFD LQIGDESVGR VVFGLFGKTV PKTVDNFVAL ATGEKGFGYK NSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GERFPDENFK LKHYGPGWVS MANAGKDTNG SQFFITTVKT SWLDGKHVVF GKVLEGMDVV RKVESTKTDS
      RDKPLKDVII VDSGKIEVEK PFAIAKE.

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    Cyclophilin B Mouse
  • View Data Sheet

    Name :

    BACE2 Mouse, HEK

    Description:

    Beta-Secretase 2 Mouse Recombinant, HEK

    BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

    Product # :

    ENZ-1188

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    Description

    BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    BACE2 (0.25mg/ml) is filtered in 10% (w/v) glycerol and Phosphate-Buffered Saline pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20 pmol/min/ug in which one unit will convert 1.0pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to Mca- Pro-Leu-OH per minute at pH 3.5 at 25C.

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    • Synonyms

      BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

    • Physical Appearance

      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

      AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI

      WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.

    • Background

      BACE2 protein, a member of the beta-secretase family, has gained attention as a key player in the pathogenesis of neurological disorders, particularly Alzheimer's disease. This research aims to explore the function and potential therapeutic implications of BACE2 protein in neurodegenerative conditions. Understanding the role of BACE2 protein can provide valuable insights into its significance as a therapeutic target for the development of novel treatment strategies.

      Function of BACE2 Protein:

      BACE2 is a transmembrane aspartic protease predominantly expressed in the central nervous system. It exhibits distinct cleavage activity on various protein substrates, including neuregulins, APP-like proteins, and TGF-β. Unlike its close homolog BACE1, BACE2 has been proposed to have non-amyloidogenic processing capabilities and has shown potential neuroprotective effects.

      Implications of BACE2 Protein in Alzheimer's Disease:

      Alzheimer's disease is characterized by the accumulation of amyloid-beta (Aβ) peptides in the brain, which are generated through the sequential cleavage of amyloid precursor protein (APP). BACE1 is primarily responsible for the cleavage of APP, leading to the production of toxic Aβ peptides. In contrast, BACE2 has been suggested to compete with BACE1, thereby reducing the levels of Aβ generation. This has led to speculation about the neuroprotective role of BACE2 and its potential as a therapeutic target for Alzheimer's disease.

      BACE2 Protein and Neuronal Survival:

      Emerging evidence suggests that BACE2 may play a role in promoting neuronal survival and function. Studies have shown that BACE2 deficiency leads to impaired synaptic plasticity, reduced dendritic branching, and altered neurotransmitter release. BACE2 has also been implicated in the regulation of axonal growth and guidance during development. These findings highlight the potential importance of BACE2 in maintaining neuronal integrity.

      Association of BACE2 Protein with Other Neurological Disorders:

      Apart from Alzheimer's disease, BACE2 has been implicated in other neurological conditions as well. Genetic studies have identified BACE2 gene variants associated with an increased risk of Parkinson's disease, suggesting its involvement in the pathogenesis of this disorder. Furthermore, BACE2 has been linked to the regulation of insulin signaling and glucose homeostasis, making it a potential target for diabetes-associated cognitive decline.

      Therapeutic Implications of BACE2 Protein:

      Given its potential neuroprotective effects and modulatory role in amyloid processing, BACE2 protein has emerged as a promising therapeutic target for neurodegenerative disorders. Strategies aimed at enhancing BACE2 activity or selectively activating BACE2-mediated non-amyloidogenic processing pathways hold promise for reducing amyloid pathology and preserving neuronal function. However, further research is needed to better understand the complex mechanisms underlying BACE2 function and to develop safe and effective therapeutic interventions.

      Conclusion:

      The investigation of BACE2 protein has provided valuable insights into its role in neurodegenerative diseases, particularly Alzheimer's disease. The potential neuroprotective effects and modulation of amyloid processing pathways by BACE2 make it an intriguing therapeutic target. Future studies should focus on unraveling the precise mechanisms by which BACE2 influences disease pathogenesis and developing strategies to harness its therapeutic potential. The exploration of BACE2 protein opens new avenues for the development of innovative treatment approaches for neurodegenerative disorders.

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    Bace2 Mouse Hek
  • View Data Sheet

    Name :

    NQO1 Human, Active

    Description:

    NAD(P)H Dehydrogenase Quinone 1, Active 1 Human Recombinant

    NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    Product # :

    ENZ-1107

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    Description

    NQO1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids ( 1-274aa ) and having a molecular mass of 33.0 kDa. NQO1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NQO1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/ug. One unit will convert 1 pmoles resazurin to resorufin per minute at pH 7.5 at 25°C.

    More Info

    • Introduction

      NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.

    • Synonyms

      NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    • 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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES
      DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF
      QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG
      IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP
      LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK

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    Nqo1 Enzyme
  • View Data Sheet

    Name :

    CTSL Mouse

    Description:

    Cathepsin-L Mouse Recombinant

    Cathepsin L1, Cathepsin L, Major excreted protein, MEP, p39 cysteine proteinase.

    Product # :

    ENZ-944

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    Description

    CTSL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (18-334a.a.) and having a molecular mass of 36.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTSL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Cathepsin-L also known as CTSL is a member of the peptidase C1 family. CTSL, is a dimer composed of disulfide-linked heavy and light chains, both formed from a single protein precursor. Furthermore, CTSL is a lysosomal cysteine proteinase which takes a main part in intracellular protein catabolism. CTSL substrates include collagen and elastin, as well as alpha-1 protease inhibitor, which is the most important controlling element of neutrophil elastase activity. CTSL has been implicated in a number of pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. Multiple alternatively spliced transcript variants have been found for CTSL.

    • Synonyms

      Cathepsin L1, Cathepsin L, Major excreted protein, MEP, p39 cysteine proteinase.

    • 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

      TPKFDQTFSA EWHQWKSTHR RLYGTNEEEW RRAIWEKNMR MIQLHNGEYS NGQHGFSMEM NAFGDMTNEE FRQVVNGYRH QKHKKGRLFQ EPLMLKIPKS VDWREKGCVT PVKNQGQCGS CWAFSASGCL EGQMFLKTGK LISLSEQNLV DCSHAQGNQG CNGGLMDFAF QYIKENGGLD SEESYPYEAK DGSCKYRAEF AVANDTGFVD IPQQEKALMK AVATVGPISV AMDASHPSLQ FYSSGIYYEP NCSSKNLDHG VLLVGYGYEG TDSNKNKYWL VKNSWGSEWG MEGYIKIAKD RDNHCGLATA ASYPVVNLEH HHHHH.

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    Ctsl Mouse
  • View Data Sheet

    Name :

    HK1/2/3 Antibody

    Description:

    Hexokinase-1/2/3, Mouse Anti Human

    Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.

    Product # :

    ANT-726

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    • More Info

    Formulation

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

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    • Introduction

      Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. HK3 encodes hexokinase 3. Similar to hexokinases 1 and 2, this allosteric enzyme is inhibited by its product glucose-6-phosphate. Hexokinase3 lacks the hydrophobic N-terminal sequence critical for targeting to mitochondria. Hexpkinase3 may have anabolic functions, providing H6P for glycogen or lipid synthesis.

    • Synonyms

      Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human HK1/2/3mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HK1/2/3amino acids 1-923 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT4C12AT.

    • Applications

      HK1/2/3antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      HK1/2/3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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    Hk123 Antibody
  • View Data Sheet

    Name :

    COX5A Antibody

    Description:

    Cytochrome C Oxidase Subunit Va, Mouse Anti Human

    Cytochrome c oxidase subunit 5A, mitochondrial, Cytochrome c oxidase polypeptide Va, COX5A, VA, COX, COX-VA.

    Product # :

    ANT-605

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    Formulation

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

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    • Introduction

      Cytochrome C Oxidase Subunit Va (COX5A) is a member of the cytochrome c oxidase subunit 5A family. COX (Cytochrome C Oxidase), which is the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced Cytochrome C to oxygen. The COX component is a heteromeric complex comprised of three catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits serve in electron transfer, and the nuclear-encoded subunits act in the regulation and assembly of the complex. COX5A is the heme A-containing chain of Cytochrome C Oxidase,which is the terminal oxidase in mitochondrial electron transport.

    • Synonyms

      Cytochrome c oxidase subunit 5A, mitochondrial, Cytochrome c oxidase polypeptide Va, COX5A, VA, COX, COX-VA.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human COX5A mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human COX5A protein 42-150 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT7A6AT.

    • Applications

      COX5A antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      COX5A antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Cox5A Antibody
  • View Data Sheet

    Name :

    MX1 Human

    Description:

    Myxovirus Resistance 1 Human Recombinant

    MX Dynamin-Like GTPase 1, Myxoma Resistance Protein 1, IFI-78K, IFI78, MX, Myxovirus (Influenza) Resistance 1, 

    Product # :

    PRO-2091

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    • sds-page

    Description

    MX1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 685 amino acids (1-662 a.a) and having a molecular mass of 77.9kDa. MX1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MX1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    mx1 human sds-page - Product image 1

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    • Introduction

      Myxovirus Resistance 1, also known as MX1 is a guanosine triphosphate (GTP)-metabolizing protein which takes part in the cellular antiviral response. MX1 is induced by type I and type II IFN, and also antagonizes the replication process of some different RNA & DNA viruses. In addition, there is a related gene located adjacent to MX1 on chromosome 21, and there are multiple pseudogenes positioned in a cluster on chromosome 4.

    • Synonyms

      MX Dynamin-Like GTPase 1, Myxoma Resistance Protein 1, IFI-78K, IFI78, MX, Myxovirus (Influenza) Resistance 1,

    • 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 MGSMVVSEVD IAKADPAAAS HPLLLNGDAT VAQKNPGSVA ENNLCSQYEE KVRPCIDLID SLRALGVEQD LALPAIAVIG DQSSGKSSVL EALSGVALPR GSGIVTRCPL VLKLKKLVNE DKWRGKVSYQ DYEIEISDAS EVEKEINKAQ NAIAGEGMGI SHELITLEIS SRDVPDLTLI DLPGITRVAV GNQPADIGYK IKTLIKKYIQ RQETISLVVV PSNVDIATTE ALSMAQEVDP EGDRTIGILT KPDLVDKGTE DKVVDVVRNL VFHLKKGYMI VKCRGQQEIQ DQLSLSEALQ REKIFFENHP YFRDLLEEGK ATVPCLAEKL TSELITHICK SLPLLENQIK ETHQRITEEL QKYGVDIPED ENEKMFFLID KVNAFNQDIT ALMQGEETVG EEDIRLFTRL RHEFHKWSTI IENNFQEGHK ILSRKIQKFE NQYRGRELPG FVNYRTFETI VKQQIKALEE PAVDMLHTVT DMVRLAFTDV SIKNFEEFFN LHRTAKSKIE DIRAEQEREG EKLIRLHFQM EQIVYCQDQV YRGALQKVRE KELEEEKKKK SWDFGAFQSS SATDSSMEEI FQHLMAYHQE ASKRISSHIP LIIQFFMLQT YGQQLQKAML QLLQDKDTYS WLLKERSDTS DKRKFLKERL ARLTQARRRL AQFPG.

    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.

    Mx1 Human
  • View Data Sheet

    Name :

    GZMH Human, sf9

    Description:

    Granzyme-H Human Recombinant, sf9

    Granzyme H, Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), Cytotoxic T-Lymphocyte Proteinase, Cathepsin G-Like 2, CTSGL2, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cathepsin G-Like 2, Protein H-CCPX, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Protein H-CCPX, EC 3.4.21.79, EC 3.4.21, EC 3.4.21, CTLA1, CGL-2 , CGL2.

    Product # :

    ENZ-961

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    Description

    GZMH produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 234 amino acids (19-246 a.a.) and having a molecular mass of 26.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GZMH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Granzyme H also known as GZMH belongs to the peptidase S1 family. GZMH is an essential part for HBV eradication. The HBx protein, which is required for the replication of HBV, is cleaved at Met(79) by GZMH. Furthermore, GZMH inhibitor can abolish GZNH- as well as lymphokine-activated killer cell-mediated HBx degradation and HBV clearance. A HBx-deficient HBV is resistant to GzmH- in addition to lymphokine-activated killer cell-mediated viral clearance.

    • Synonyms

      Granzyme H, Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), Cytotoxic T-Lymphocyte Proteinase, Cathepsin G-Like 2, CTSGL2, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cathepsin G-Like 2, Protein H-CCPX, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Protein H-CCPX, EC 3.4.21.79, EC 3.4.21, EC 3.4.21, CTLA1, CGL-2 , CGL2.

    • 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

      EEIIGGHEAK PHSRPYMAFV QFLQEKSRKR CGGILVRKDF VLTAAHCQGS SINVTLGAHN IKEQERTQQF IPVKRPIPHP AYNPKNFSND IMLLQLERKA KWTTAVRPLR LPSSKAQVKP GQLCSVAGWG YVSMSTLATT LQEVLLTVQK DCQCERLFHG NYSRATEICV GDPKKTQTGF KGDSGGPLVC KDVAQGILSY GNKKGTPPGV YIKVSHFLPW IKRTMKRLHH 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.

    Gzmh Human Sf9
  • View Data Sheet

    Name :

    CKMT3 Human

    Description:

    Creatine Kinase Muscle Type-3 Human Recombinant

    Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.

    Product # :

    CKI-272

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    Description

    CKMT3 Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA.The CKMT3 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Each mg of protein contains 20mM Tris pH-8, 1mM EDTA and 1mM DTT.

    Purity

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

    Biological Activity

    The biological activity measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 500 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 2,000ng/ml.

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    • Introduction

      The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

    • Synonyms

      Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.

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

    Ckmmitiii 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

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    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.

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    • 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 :

    NDUFS5 Human

    Description:

    Histidine NADH Dehydrogenase Fe-S Protein 5 Human Recombinant

    CI-15k, CI15K, NADH dehydrogenase [ubiquinone] iron-sulfur protein 5, Complex I-15 kDa, NADH-ubiquinone oxidoreductase 15 kDa subunit, CI-15 kDa, NDUFS5.

    Product # :

    ENZ-771

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    Description

    NDUFS5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106a.a) and having a molecular mass of 14.9kDa. NDUFS5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFS5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Histidine NADH Dehydrogenase Fe-S Protein 5 (NDUFS5) belongs to the NADH dehydrogenase (ubiquinone) iron-sulfur protein family. NDUFS5 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which doesn’t take part in catalysis. Complex I is transferring the electrons from NADH to the respiratory chain.

    • Synonyms

      CI-15k, CI15K, NADH dehydrogenase [ubiquinone] iron-sulfur protein 5, Complex I-15 kDa, NADH-ubiquinone oxidoreductase 15 kDa subunit, CI-15 kDa, NDUFS5.

    • 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 MGSMPFLDIQ KRFGLNIDRW LTIQSGEQPY KMAGRCHAFE KEWIECAHGI GYTRAEKECK IEYDDFVECL LRQKTMRRAG TIRKQRDKLI KEGKYTPPPH HIGKGEPRP.

    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.

    Ndufs5 Human
  • View Data Sheet

    Name :

    DUSP26 Human

    Description:

    Dual Specificity Phosphatase 26 Human Recombinant

    Dual specificity protein phosphatase 26, Dual specificity phosphatase SKRP3, Low-molecular-mass dual-specificity phosphatase 4, DSP-4, LDP-4, Mitogen-activated protein kinase phosphatase 8, MAP kinase phosphatase 8, MKP-8, Novel amplified gene in thyroid anaplastic cancer, DUSP26, DUSP24, LDP4, MKP8, NATA1, SKRP3, Dual specificity phosphatase 26 (putative).

    Product # :

    ENZ-747

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    Description

    DUSP26 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-211a.a) and having a molecular mass of 26.3kDa.DUSP26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DUSP26 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Dual Specificity Phosphatase 26 (DUSP26) inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells. DUSP26 also induces activation of MAP kinase p38 and c-Jun N-terminal kinase. DUSP26 inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a decrease in its DNA-binding activity.

    • Synonyms

      Dual specificity protein phosphatase 26, Dual specificity phosphatase SKRP3, Low-molecular-mass dual-specificity phosphatase 4, DSP-4, LDP-4, Mitogen-activated protein kinase phosphatase 8, MAP kinase phosphatase 8, MKP-8, Novel amplified gene in thyroid anaplastic cancer, DUSP26, DUSP24, LDP4, MKP8, NATA1, SKRP3, Dual specificity phosphatase 26 (putative).

    • 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 MGSMCPGNWL WASMTFMARF SRSSSRSPVR TRGTLEEMPT VQHPFLNVFE LERLLYTGKT ACNHADEVWP GLYLGDQDMA NNRRELRRLG ITHVLNASHS RWRGTPEAYE GLGIRYLGVE AHDSPAFDMS IHFQTAADFI HRALSQPGGK ILVHCAVGVS RSATLVLAYL MLYHHLTLVE AIKKVKDHRG IIPNRGFLRQ LLALDRRLRQ GLEA.

    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.

    Dusp26 Human
  • View Data Sheet

    Name :

    ENPP1 Human

    Description:

    Ectonucleotide Pyrophosphatase Human 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-729

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    Description

    ENPP1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 98-925) containing a total of 840 amino acids, having a molecular mass of 96.5kDa (calculated) though it migrates at approximately 110kDa on SDS PAGE, the ENPP1 is also composed of a 2 a.a N-terminal linker, a 4 a.a C-terminal linker and fused to a 6 a.a His tag at C-Terminus.The Human ENPP1 is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ectonucleotide Pyrophosphatase (ENPP1) belongs to the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family. ENPP1 is a type II transmembrane glycoprotein comprised of 2 identical disulfide-bonded subunits. The ENPP1 protein has broad specificity and cleaves various substrates, including phosphodiester bonds of nucleotides and nucleotide sugars and pyrophosphate bonds of nucleotides and nucleotide sugars. The ENPP1 protein can hydrolyze nucleoside 5' triphosphates to their corresponding monophosphates and it may also hydrolyze diadenosine polyphosphates. ENPP1 gene mutations are linked with 'idiopathic' infantile arterial calcification and ossification of the posterior longitudinal ligament of the spine (OPLL).

    • 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 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      ASKPSCAKEV KSCKGRCFER TFGNCRCDAA CVELGNCCLD YQETCIEPEH IWTCNKFRCG EKRLTRSLCA CSDDCKDKGD CCINYSSVCQ GEKSWVEEPC ESINEPQCPA GFETPPTLLF SLDGFRAEYL HTWGGLLPVI SKLKKCGTYT KNMRPVYPTK TFPNHYSIVT GLYPESHGII DNKMYDPKMN ASFSLKSKEK FNPEWYKGEP IWVTAKYQGL KSGTFFWPGS DVEINGIFPD IYKMYNGSVP FEERILAVLQ WLQLPKDERP HFYTLYLEEP DSSGHSYGPV SSEVIKALQR VDGMVGMLMD GLKELNLHRC LNLILISDHG MEQGSCKKYI YLNKYLGDVK NIKVIYGPAA RLRPSDVPDK YYSFNYEGIA RNLSCREPNQ HFKPYLKHFL PKRLHFAKSD RIEPLTFYLD PQWQLALNPS ERKYCGSGFH GSDNVFSNMQ ALFVGYGPGF KHGIEADTFE NIEVYNLMCD LLNLTPAPNN GTHGSLNHLL KNPVYTPKHP KEVHPLVQCP FTRNPRDNLG CSCNPSILPI EDFQTQFNLT VAEEKIIKHE TLPYGRPRVL QKENTICLLS QHQFMSGYSQ DILMPLWTSY TVDRNDSFST EDFSNCLYQD FRIPLSPVHK CSFYKNNTKV SYGFLSPPQL NKNSSGIYSE ALLTTNIVPM YQSFQVIWRY FHDTLLRKYA EERNGVNVVS GPVFDFDYDG RCDSLENLRQ KRRVIRNQEI LIPTHFFIVL TSCKDTSQTP LHCENLDTLA FILPHRTDNS ESCVHGKHDS SWVEELLMLH RARITDVEHI TGLSFYQQRK EPVSDILKLK THLPTFSQED GPKLHHHHHH.

    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 Human
  • View Data Sheet

    Name :

    STX6 Human

    Description:

    Syntaxin-6 Human Recombinant

    Syntaxin 6.

    Product # :

    PRO-1711

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    Description

    STX6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 257 amino acids (1-234) and having a molecular mass of 29.2kDa.STX6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STX6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STX6 is a member of the syntaxin family and has 1 t-SNARE coiled-coil homology domain. STX6 takes part in intracellular vesicle transferring. STX6 binds EEA1 and Interacts with VPS45A, MARCH2, MARCH3 and GOPC. It is found in a complex comprising STX6, STX12, VAMP4 and VTI1A.

    • Synonyms

      Syntaxin 6.

    • 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 MGSMSMEDPF FVVKGEVQKA VNTAQGLFQR WTELLQDPST ATREEIDWTT NELRNNLRSI EWDLEDLDET ISIVEANPRK FNLDATELSI RKAFITSTRQ VVRDMKDQMS TSSVQALAER KNRQALLGDS GSQNWSTGTT DKYGRLDREL QRANSHFIEE QQAQQQLIVE QQDEQLELVS GSIGVLKNMS QRIGGELEEQ AVMLEDFSHE LESTQSRLDN VMKKLAKVSH MTSDRRQ

    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.

    Stx6 Human
  • View Data Sheet

    Name :

    GCSAM Human

    Description:

    Germinal Center-Associated, Signaling and Motility Human Recombinant

    GCAT2, HGAL, Germinal center-associated signaling and motility protein, Germinal center B-cell-expressed transcript 2 protein, Germinal center-associated lymphoma protein, GAL, GCET2 .

    Product # :

    PRO-1282

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    GCSAM Human Recombinant produced in E. coli is a single polypeptide chain containing 201 amino acids (1-178) and having a molecular mass of 23 kDa. GCSAM is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GCSAM solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      GCSAM is a protein which functions in signal transduction pathways and whose expression raises in germinal cell lymphomas. GCSAM contains a putative PDZ-interacting domain, an immunoreceptor tyrosine-based activation motif (ITAM), and two putative SH2 binding sites. In B cells, GCSAM expression is particularly induced by interleukin-4.

    • Synonyms

      GCAT2, HGAL, Germinal center-associated signaling and motility protein, Germinal center B-cell-expressed transcript 2 protein, Germinal center-associated lymphoma protein, GAL, GCET2 .

    • 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 MGSMGNSLLR ENRRQQNTQE MPWNVRMQSP KQRTSRCWDH HIAEGCFCLP WKKILIFEKR QDSQNENERM SSTPIQDNVD QTYSEELCYT LINHRVLCTR PSGNSAEEYY ENVPCKAERP RESLGGTETE YSLLHMPSTD PRHARSPEDE YELLMPHRIS SHFLQQPRPL MAPSETQFSH L.

    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.

    Gcsam Human
  • View Data Sheet

    Name :

    STK17A Human

    Description:

    Serine/Threonine Kinase 17A Human Recombinant

    DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.

    Product # :

    PKA-314

    Price :

    Quantity :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    STK17A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (64-321 a.a) and having a molecular mass of 31.9kDa.STK17A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STK17A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.

    • Synonyms

      DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.

    • 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 MGSGRELGRG KFAVVRKCIK KDSGKEFAAK FMRKRRKGQD CRMEIIHEIA VLELAQDNPW VINLHEVYET ASEMILVLEY AAGGEIFDQC VADREEAFKE KDVQRLMRQI LEGVHFLHTR DVVHLDLKPQ NILLTSESPL GDIKIVDFGL SRILKNSEEL REIMGTPEYV APEILSYDPI SMATDMWSIG VLTYVMLTGI SPFLGNDKQE TFLNISQMNL SYSEEEFDVL SESAVDFIRT LLVKKPEDRA TAEECLKHPW L.

    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.

    Stk17A Human
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