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Search results

1000 results found for “ahcy”

Name

Description

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  • View Data Sheet

    Name :

    Borrelia BmpA

    Description:

    Borrelia Burgdorferi Basic Membrane Protein A Recombinant

    Product # :

    BOR-006

    Price :

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    Description

    Recombinant Borrelia Burgdorferi Basic Membrane Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 36,239 Dalton. Borrelia BmpA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia BmpA (1.3mg/1ml) is supplied in 20mM HEPES buffer pH-8.0, 6M Urea and 200mM NaCl.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Applications

      Western blot with Lyme positive plasma.

    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.

    Borrelia Bmpa
  • View Data Sheet

    Name :

    Borrelia OspA

    Description:

    Borrelia Burgdorferi Outer Surface Protein A Recombinant

    Product # :

    BOR-013

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    Description

    Recombinant Borrelia Burgdorferi (strain B31) OspA produced in E.coli is a non-glycosylated, full-length polypeptide chain having a calculated molecular mass of 27kDa. Borrelia OspA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia OspA is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

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

    Borrelia Ospa
  • View Data Sheet

    Name :

    BPNT1 Human

    Description:

    3(2) 5-Bisphosphate Nucleotidase 1 Human Recombinant

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

    Product # :

    ENZ-061

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

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

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

    Bpnt1 Human
  • View Data Sheet

    Name :

    PDGF AA Human, Yeast

    Description:

    Platelet-derived Growth Factor AA Human Recombinant, Yeast

    Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

    Product # :

    CYT-568

    Price :

    Quantity :

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    Shipped at Room temp

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    • Citations

    Description

    PDGF-AA Human Recombinant produced in Yeast is a homodimeric, glycosilated, polypeptide chain containing 2 x 110 amino acids and having a total molecular mass of 34 kDa. PDGF-AA is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    The protein was lyophilized with 20mM sodium phosphate buffer.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was found to be 1ng/ml  corresponding to a Specific Activity of 1,000,000IU/mg calculated by the ability to stimulate the proliferation of mouse 3T3 fibroblasts (PNAS 94, 10205, 1997. Biochemistry, 1996, 35, 12077).

    Citations

    More Info

    • Introduction

      PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.

    • Synonyms

      Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Pdgf Aa Human Yeast
  • View Data Sheet

    Name :

    Placental Lactogen Sf9, Human

    Description:

    Placental Lactogen Human Recombinant, Sf9

    Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407

    Product # :

    CYT-1164

    Price :

    Quantity :

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    Description

    Placental Lactogen Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 197 amino acids (27-217 aa) and having a molecular mass of 23.1kDa.Placental Lactogen is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Placental Lactogen solution (0.25mg/ml) contains 30% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by cell proliferation assay using Nb2-11 Rat lymphoma cells. ED50 range for this effect is ≤ 0.8 ng/ml.

    Citations

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta.Placental Lactogen has both GH and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407

    • 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

      VQTVPLSRLF DHAMLQAHRA HQLAIDTYQE FEETYIPKDQ KYSFLHDSQT SFCFSDSIPT PSNMEETQQK SNLELLRISL LLIESWLEPV RFLRSMFANN LVYDTSDSDD YHLLKDLEEG IQTLMGRLED GSRRTGQILK QTYSKFDTNS HNHDALLKNY GLLYCFRKDM DKVETFLRMV QCRSVEGSCG FHHHHHH

    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.

    Csh1 Human
  • View Data Sheet

    Name :

    TNFRSF12A Human, sf9

    Description:

    TNF Ligand Receptor Superfamily Member 12A Human Recombinant, Sf9

    Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

    Product # :

    CYT-1021

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    Description

    TNFRSF12A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (28-80a.a.) and having a molecular mass of 32.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). TNFRSF12A is expressed with a 239 amino acids hIgG- His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF12A protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The gene for TNFRSF12A was initially recognized as a fibroblast growth factor inducible immediate early response gene Fn14 in mouse NIH 3T3 fibroblasts. Human TNFRSF12A cDNA encodes a 129 amino acid residue type I transmembrane protein with a 27 aa signal peptide, a 53 aa extracellular domain, a 21 aa transmembrane domain and a 28 aa cytoplasmic domain. Human and mouse TNFRSF12A hold 82% aa sequence identity. TNFRSF12 is the tiniest member of the TNF receptor superfamily and has only one cysteine rich region in its extracellular domain. The TNFRSF12A cytoplasmic domain holds one TRAF binding motif which binds TRAFs 1, 2, and 3. TNFRSF12A binds its ligand TWEAK/TNFSF12A with high affinity to initiate a signal transduction cascade which subject to the cell type, causes different cellular responses such as cell death, cell proliferation, and angiogenesis.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

    • 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

      EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWPLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

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    Tnfrsf12A Protein
  • View Data Sheet

    Name :

    KLK11 Human, Sf9

    Description:

    Kallikrein-11, 4 Human Recombinant, Sf9

    Kallikrein-11 isoform 1, KLK11, PRSS20, TLSP.

    Product # :

    ENZ-1089

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    Description

    KLK11 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 241 amino acids (19-250a.a.) and having a molecular mass of 26.7 kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).KLK11 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    KLK11 protein solution ( 0.5mg/m ) contains 50mM Tris-HCl (pH 7.5), 0.1M NaCl, 2mM CaCl2 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.

    • Synonyms

      Kallikrein-11 isoform 1, KLK11, PRSS20, TLSP.

    • 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

      ADLETRIIKG FECKPHSQPW QAALFEKTRL LCGATLIAPR WLLTAAHCLK PRYIVHLGQH NLQKEEGCEQ TRTATESFPH PGFNNSLPNK DHRNDIMLVK MASPVSITWA VRPLTLSSRC VTAGTSCLIS GWGSTSSPQL RLPHTLRCAN ITIIEHQKCE NAYPGNITDT MVCASVQEGG KDSCQGDSGG PLVCNQSLQG IISWGQDPCA ITRKPGVYTK VCKYVDWIQE TMKNNHHHHH H.

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

    Kallikrein 11
  • View Data Sheet

    Name :

    TPSAB1 Human, Sf9

    Description:

    Tryptase Alpha/Beta 1 Human Recombinant, Sf9

    Tryptase alpha/beta-1, TPSAB1, TPS1, TPS2, TPSB1, Tryptase I, Tryptase alpha-1.

    Product # :

    ENZ-1062

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    Description

    TPSAB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (31-275 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 251 amino acids and having a molecular mass of 28.2kDa.TPSAB1 shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TPSAB1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tryptase alpha/beta-1 (TPSAB1) is a tryptase which is the key neutral protease present in mast cells and is discharged upon the coupled activation-degranulation response of this cell type. TPSAB1 is enzymatically active only as a heparin-stabilized tetramer, and is resistant to all known endogenous proteinase inhibitors. TPSAB1 is implicated as a mediator in the pathogenesis of asthma and other allergic and inflammatory disorders.

    • Synonyms

      Tryptase alpha/beta-1, TPSAB1, TPS1, TPS2, TPSB1, Tryptase I, Tryptase alpha-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

      IVGGQEAPRS KWPWQVSLRV HGPYWMHFCG GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ LLPVSRIIVH PQFYTAQIGA DIALLELEEP VNVSSHVHTV TLPPASETFP PGMPCWVTGW GDVDNDERLP PPFPLKQVKV PIMENHICDA KYHLGAYTGD DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG VVSWGEGCAQ PNRPGIYTRV TYYLDWIHHY VPKKPHHHHH H.

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    Tpsab1 Protein
  • View Data Sheet

    Name :

    CD81 Human

    Description:

    CD81 Human Recombinant

    CD81 Molecule, CD81 Antigen (Target Of Antiproliferative Antibody 1), 26 KDa Cell Surface Protein TAPA-1, Tetraspanin-28, CD81 Antigen, Tspan-28, TSPAN28, TAPA1, Target Of The Antiproliferative Antibody 1, CVID6, S5.7, 26 kDa cell surface protein TAPA-1, Target of the antiproliferative antibody 1, Tetraspanin-28, Tspan-28.

    Product # :

    PRO-2472

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    Description

    CD81 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (113-201a.a.) and having a molecular mass of 37.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CD81 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD81 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CD81 antigen isoform 1, also known as CD81, is part of the tetraspanin family. CD81 interacts directly with immunoglobulin superfamily member 8 (IGSF8, CD316) and CD36. In B cells, CD81 is part of a complex with CD21, CD19 and Leu13. Furthermore, this complex decreases the threshold for B cell activation through B cell receptors by linking Ag specific recognition and CD21 mediator recognition. While on T cells CD81 connects with CD4 and CD8 and provides a costimulatory signal with CD3.

    • Synonyms

      CD81 Molecule, CD81 Antigen (Target Of Antiproliferative Antibody 1), 26 KDa Cell Surface Protein TAPA-1, Tetraspanin-28, CD81 Antigen, Tspan-28, TSPAN28, TAPA1, Target Of The Antiproliferative Antibody 1, CVID6, S5.7, 26 kDa cell surface protein TAPA-1, Target of the antiproliferative antibody 1, Tetraspanin-28, Tspan-28.

    • 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

      ADPFVNKDQI AKDVKQFYDQ ALQQAVVDDD ANNAKAVVKT FHETLDCCGS STLTALTTSV LKNNLCPSGS NIISNLFKED CHQKIDDLFS GKLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

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

    Cd81 Human
  • View Data Sheet

    Name :

    FGF23 Human

    Description:

    Fibroblast Growth Factor-23 Human Recombinant

    Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    Product # :

    CYT-020

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    Description

    Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

    Citations

    More Info

    • Introduction

      FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.

    • Synonyms

      Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 FGF-23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

    • Background

      Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.

      Mechanism
      Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.

      Interactions
      Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.

      Function
      Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
      As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.

      Structure
      FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
      Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
      Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.

      What is the molecular weight/Mw of FGF23 HUMAN Protein?
      FGF23 HUMAN Protein has a total Mw of 22.5kDa.

      What is the source or expression system of FGF23 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FGF23 HUMAN Protein?
      FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF23 HUMAN Protein?
      The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

      What is the amino acid sequence of FGF23 HUMAN Protein?
      MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

      What applications can FGF23 HUMAN Protein be used in?
      FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF23 HUMAN Protein?
      The endotoxin level is minimal, FGF23 HUMAN Protein was purified using conventional chromatography techniques.

    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.

    Fgf23 Human
  • View Data Sheet

    Name :

    MIF Human, Active

    Description:

    Macrophage Migration Inhibitory Factor Human Recombinant (Active)

    Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    Product # :

    CYT-596

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    Description

    MIF human Recombinant was cloned into an E.coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chain containing 115 amino acids and having a molecular mass of 12.5 kDa.

    Source

    Escherichia Coli.

    Formulation

    MIF-Protein was lyophilized from 10mM sodium phosphate buffer pH-7.5.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Human PBMCs were cultured with 0 to 1000ng/ml Human MIF. Production of IL-8 was measured via ELISA after 24 hours. The ED50 which was found to be 88-132ng/ml.

    Citations

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIF-protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF-protein 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 MIF-Protein in sterile 18MΩ-cm H2O at a concentration between 0.1mg-1mg per 1ml.

    • Amino Acid Sequence

      MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLM
      AFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVY
      INYYDMNAANVGWNNSTFA.

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    Mif Human Active
  • View Data Sheet

    Name :

    MMP 7 Human

    Description:

    Matrix Metalloproteinase-7 Human Recombinant

    Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.

    Product # :

    ENZ-867

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    Description

    MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.MMP7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MMP7 protein solution (1mg/ml) containing 20mM Tris 8.0 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

    • Synonyms

      Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.

    • 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

      MYSLFPNSPK WTSKVVTYRI VSYTRDLPHI TVDRLVSKAL NMWGKEIPLH FRKVVWGTAD IMIGFARGAH GDSYPFDGPG NTLAHAFAPG TGLGGDAHFD EDERWTDGSS LGINFLYAAT HELGHSLGMG HSSDPNAVMY PTYGNGDPQN FKLSQDDIKG IQKLYGKRSN SRKK.

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    Mmp 7 Human
  • View Data Sheet

    Name :

    POLB Human

    Description:

    Polymerase (DNA directed), Beta Human Recombinant

    DNA polymerase beta, DNA directed DNA polymerase beta, DNA pol beta, DNA polymerase beta, DNA polymerase beta subunit, MGC125976, Pol B, Pol beta, PolB, Polymerase (DNA directed) beta.

    Product # :

    ENZ-168

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    Description

    POLB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (1-335 a.a) and having a molecular mass of 40.3kDa.POLB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POLB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DNA polymerase beta (POLB) is a member of the DNA polymerase type-X family. In eukaryotic cells, POLB performs base excision repair necessary for DNA maintenance, replication, recombination, and drug resistance. POLB has 2 separate domains; the larger is the polymerase domain itself, whereas a small basic N-terminal domain contains an AP lyase activity which excises the abasic sugar-phosphate residue at the strand break. POLB fills single nucleotide gaps in DNA produced by the base excision repair pathway of mammalian cells. POLB overexpression, as seen in some human tumors, could convene an increase in spontaneous mutagenesis.

    • Synonyms

      DNA polymerase beta, DNA directed DNA polymerase beta, DNA pol beta, DNA polymerase beta, DNA polymerase beta subunit, MGC125976, Pol B, Pol beta, PolB, Polymerase (DNA directed) beta.

    • 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 MSKRKAPQET LNGGITDMLT ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVSGIGPSA ARKFVDEGIK TLEDLRKNED KLNHHQRIGL KYFGDFEKRI PREEMLQMQD
      IVLNEVKKVD SEYIATVCGS FRRGAESSGD MDVLLTHPSF TSESTKQPKL LHQVVEQLQK VHFITDTLSK GETKFMGVCQ LPSKNDEKEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP LGVTGVAGEP LPVDSEKDIF DYIQWKYREP KDRSE.

    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.

    Polb Human
  • View Data Sheet

    Name :

    CDA Human

    Description:

    Cytidine Deaminase Human Recombinant

    Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.

    Product # :

    ENZ-007

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    Description

    CDA Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids (1-146 a.a.) and having a molecular mass of 18.3kDa. The CDA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDA solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT, 2mM EDTA, 100mM NaCl and 40% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 10,000pmol/min/ug, and is defined as the amount of required to deaminate 1.0pmole of cytidine per min at pH 7.5 at 25C.

    Citations

    More Info

    • Introduction

      Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. CDA is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as Ara-C and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function. CDA can form homotetramers and is generally expressed in granulocytes. Mutations in the CDA gene are linked to decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.

    • Synonyms

      Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.

    • 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 MAQKRPACTL KPECVQQLLV CSQEAKQSAY CPYSHFPVGA ALLTQEGRIF KGCNIENACY PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG ACRQVMREFG TNWPVYMTKP DGTYIVMTVQ ELLPSSFGPE DLQKTQ.

    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.

    Cda Human
  • View Data Sheet

    Name :

    LOX Human

    Description:

    Lysyl Oxidase Human Recombinant

    Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.

    Product # :

    ENZ-829

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    Description

    LOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (169-417a.a) and having a molecular mass of 31.4kDa.LOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lysyl Oxidase also known as LOX is an extracellular copper enzyme which initiates the crosslinking of collagens and elastin. LOX catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. Adding up to crosslinking extracellular matrix proteins, LOX plays a part in tumor suppression. Moreover, defects in LOX are the cause of autosomal recessive cutis laxa type I, CL type I. Two transcript variants encoding dissimilar isoforms have been found for LOX.

    • Synonyms

      Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl 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

      MGSSHHHHHH SSGLVPRGSH MGSDDPYNPY KYSDDNPYYN YYDTYERPRP GGRYRPGYGT GYFQYGLPDL VADPYYIQAS TYVQKMSMYN LRCAAEENCL ASTAYRADVR DYDHRVLLRF PQRVKNQGTS DFLPSRPRYS WEWHSCHQHY HSMDEFSHYD LLDANTQRRV AEGHKASFCL EDTSCDYGYH RRFACTAHTQ GLSPGCYDTY GADIDCQWID ITDVKPGNYI LKVSVNPSYL VPESDYTNNV VRCDIRYTGH HAYASGCTIS PY.

    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.

    Lox Human
  • View Data Sheet

    Name :

    UBL3 Human

    Description:

    Ubiquitin-Like 3 Human Recombinant

    Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.

    Product # :

    PRO-230

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    Description

    UBL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-114a.a) and having a molecular mass of 15.0kDa.UBL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBL3 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UBL3 - a member of the ubiquitin-like family is found in the membrane. UBL3 holds two N-glycosylation sites, a C-terminal prenylation site and a protein kinase C phosphorylation site. Even though Ubiquitin-like proteins are not directly involved in protein degradation, it seems they have several mechanistic similarities to the ubiquitin pathway.

    • Synonyms

      Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      UBL3 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSNVPADMI NLRLILVSGK TKEFLFSPND SASDIAKHVY DNWPMDWEEE QVSSPNILRL IYQGRFLHGN VTLGALKLPF GKTTVMHLVA RETLPEPNSQ GQRNREKTGE SNCC

    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.

    Ubl3 Human
  • View Data Sheet

    Name :

    MGMT Human

    Description:

    O-6-Methylguanine-DNA Methyltransferase Human Recombinant

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

    Product # :

    ENZ-389

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

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

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

    MGMT Human
  • View Data Sheet

    Name :

    Myostatin Human

    Description:

    Myostatin Human Recombinant

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-418

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    Description

    Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton. The GDF-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing no additives.

    Purity

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

    Biological Activity

    The ED50 as determined by the inhibition of the proliferation of MPC-11 cells is < 20ng/ml, corresponding to a Specific Activity of 50,000units/mg.

    Citations

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Myostatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Myostatin 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 Myostatin in sterile 20mM HCl at 0.1 mg/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 Asp-Phe-Gly-Leu-Asp.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.55 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 Myostatin as a Reference Standard.

    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.

    Myostatin Human
  • View Data Sheet

    Name :

    ACAT1 Human

    Description:

    Acetyl-Coenzyme A acetyltransferase 1 Human Recombinant

    Acetyl-CoA acetyltransferase, mitochondrial, EC 2.3.1.9, Acetoacetyl-CoA thiolase, T2, ACAT1, ACAT, MAT, THIL.

    Product # :

    ENZ-665

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    Description

    ACAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 417 amino acids (34-427) and having a molecular mass of 43.8 kDa.ACAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ACAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Acetoacetyl-CoA thiolase (ACAT1) is an enzyme member of the membrane-bound acyltransferase family and Sterol o-acyltransferase subfamily. The ACAT1 enzyme catalyzes the reversible formation of acetoacetyl-CoA from 2 molecules of acetyl-CoA. ACAT1 plays a part in lipoprotein compilation and dietary cholesterol absorption. Added to its acyltransferase activity, ACAT1 acts as a ligase.

    • Synonyms

      Acetyl-CoA acetyltransferase, mitochondrial, EC 2.3.1.9, Acetoacetyl-CoA thiolase, T2, ACAT1, ACAT, MAT, THIL.

    • 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 MGSVSKPTLK EVVIVSATRT PIGSFLGSLS LLPATKLGSI AIQGAIEKAG IPKEEVKEAY MGNVLQGGEG QAPTRQAVLG AGLPISTPCT TINKVCASGM KAIMMASQSL MCGHQDVMVA GGMESMSNVP YVMNRGSTPY GGVKLEDLIV KDGLTDVYNK
      IHMGSCAENT AKKLNIARNE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV TVKGQPDVVV KEDEEYKRVD FSKVPKLKTV FQKENGTVTA ANASTLNDGA AALVLMTADA AKRLNVTPLA RIVAFADAAV EPIDFPIAPV YAASMVLKDV GLKKEDIAMW EVNEAFSLVV LANIKMLEID
      PQKVNINGGA VSLGHPIGMS GARIVGHLTH ALKQGEYGLA SICNGGGGAS AMLIQKL.

    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.

    Acat1 Human
  • View Data Sheet

    Name :

    HDDC3 Human

    Description:

    HD domain containing 3 Human Recombinant

    Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1, HD domain-containing protein 3, Metazoan SpoT homolog 1, MESH1, Penta-phosphate guanosine-3'-pyrophosphohydrolase, (ppGpp)ase, HDDC3.

    Product # :

    ENZ-184

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    Description

    HDDC3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (1-140) and having a molecular mass of 17.9kDa.HDDC3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HDDC3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Guanosine-3',5'-bis(diphosphate)-pyrophosphohydrolase MESH1 (HDDC3) contains an active site for ppGpp hydrolysis and a conserved His-Asp-box motif for Mn(2+) binding. In accordance with its structure, HDDC3 effectively catalyzes the hydrolysis of guanosine 3',5'-diphosphate (ppGpp) both in vitro and in vivo. In addition, HDDC3 suppresses SpoT-deficient lethality and RelA-induced delayed cell growth in bacteria.

    • Synonyms

      Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1, HD domain-containing protein 3, Metazoan SpoT homolog 1, MESH1, Penta-phosphate guanosine-3'-pyrophosphohydrolase, (ppGpp)ase, HDDC3.

    • 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 MGSEAAQLLE AADFAARKHR QQRRKDPEGT PYINHPIGVA RILTHEAGIT DIVVLQAALL HDTVEDTDTT LDEVELHFGA QVRRLVEEVT DDKTLPKLER KRLQVEQAPH SSPGAKLVKL ADKLYNLRDL NRCTPEVKIQ.

    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.

    Hddc3 Human
  • View Data Sheet

    Name :

    ADH1A Human

    Description:

    Alcohol Dehydrogenase 1A Human Recombinant

    Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1A, ADH1.

    Product # :

    ENZ-580

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    Description

    ADH1A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (1-375) and having a molecular mass of 42kDa.ADH1A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADH1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Alcohol dehydrogenase 1A (ADH1A) is a member of the alcohol dehydrogenase family. ADH1A has a key role in ethanol metabolism. ADH1A along with coenzyme NAD catalyzes the reversible conversion of organic alcohols to ketones or aldehydes. The physiologic function of ADH1A in the liver is the elimination of ethanol formed by microorganisms in the intestinal tract. ADH1A is monomorphic and predominant in fetal and infant livers, growing to be less active in gestation and only weakly active during adulthood.

    • Synonyms

      Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1A, ADH1.

    • 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 MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK
      IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK
      FSLDALITHV LPFEKINEGF DLLHSGKSIR TILMF.

    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.

    Adh1A Human
  • View Data Sheet

    Name :

    CTSZ Human

    Description:

    Cathepsin-Z Human Recombinant

    Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

    Product # :

    ENZ-748

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    Description

    CTSZ Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (62-303) and having a molecular mass of 29.5kDa.CTSZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

    • 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 MGSLPKSWDW RNVDGVNYAS ITRNQHIPQY CGSCWAHAST SAMADRINIK RKGAWPSTLL SVQNVIDCGN AGSCEGGNDL SVWDYAHQHG IPDETCNNYQ AKDQECDKFN QCGTCNEFKE CHAIRNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TERLANYTGG IYAEYQDTTY INHVVSVAGW GISDGTEYWI VRNSWGEPWG ERGWLRIVTS TYKDGKGARY NLAIEEHCTF GDPIV.

    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.

    Ctsz Human
  • View Data Sheet

    Name :

    SDR16C5 Human

    Description:

    Short Chain Dehydrogenase/Reductase Family 16C, Member 5 Human Recombinant

    RDH#2, RDH-E2, RDHE2, Epidermal retinol dehydrogenase 2, EPHD-2, Retinal short-chain dehydrogenase reductase 2, retSDR2, Short-chain dehydrogenase/reductase family 16C member 5, SDR16C5.

    Product # :

    PRO-1385

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    Description

    SDR16C5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (32-269 a.a.) and having a molecular mass of 28.3kDa. SDR16C5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SDR16C5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Short chain dehydrogenase/reductase family 16C, member5 (SDR16C5) is active in the oxidative direction as well as in the reductive one. SDR16C5 oxidizes all-trans-retinol in all-trans-retinaldehyde. No activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH.

    • Synonyms

      RDH#2, RDH-E2, RDHE2, Epidermal retinol dehydrogenase 2, EPHD-2, Retinal short-chain dehydrogenase reductase 2, retSDR2, Short-chain dehydrogenase/reductase family 16C member 5, SDR16C5.

    • 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 MGSPKPRKNV AGEIVLITGA GSGLGRLLAL QFARLGSVLV LWDINKEGNE ETCKMAREAG ATRVHAYTCD CSQKEGVYRV ADQVKKEVGD VSILINNAGI VTGKKFLDCP DELMEKSFDV NFKAHLWTYK AFLPAMIAND HGHLVCISSS AGLSGVNGLA DYCASKFAAF GFAESVFVET FVQKQKGIKT TIVCPFFIKT GMFEGCTTGC PSLLPILEPK YAVEKIVEAI LQEKMYLYMP K.

    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.

    Sdr16C5 Human
  • View Data Sheet

    Name :

    HMGN3 Human

    Description:

    High Mobility Group Nucleosomal Binding Domain 3 Human Recombinant

    High Mobility Group Nucleosomal Binding Domain 3, TRIP7, TR-Interacting Protein 7, High Mobility Group Nucleosome-Binding Domain-Containing Protein 3, Thyroid Hormone Receptor Interacting Protein 7, Thyroid Receptor-Interacting Protein 7, Thyroid Hormone Receptor Interactor 7, PNAS-24, PNAS-25, TRIP-7, High mobility group nucleosome-binding domain-containing protein 3.

    Product # :

    PRO-2068

    Price :

    Quantity :

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    More Info

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

    Description

    HMGN3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77 a.a) and having a molecular mass of 10.8 kDa. HMGN3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HMGN3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH7.0) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      High Mobility Group Nucleosomal Binding Domain 3 (HMGN3), binds thyroid hormone receptor beta, however it occurs only in the presence of thyroid hormone. Thyroid hormone receptors are hormone-dependent transcription factors which regulate expression of a variety of particular target genes. HMGN3 is considered to reduce the compactness of the chromatin fiber in nucleosomes, in that way enhancing transcription from chromatin templates.

    • Synonyms

      High Mobility Group Nucleosomal Binding Domain 3, TRIP7, TR-Interacting Protein 7, High Mobility Group Nucleosome-Binding Domain-Containing Protein 3, Thyroid Hormone Receptor Interacting Protein 7, Thyroid Receptor-Interacting Protein 7, Thyroid Hormone Receptor Interactor 7, PNAS-24, PNAS-25, TRIP-7, High mobility group nucleosome-binding domain-containing protein 3.

    • 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 MGSMPKRKSP ENTEGKDGSK VTKQEPTRRS ARLSAKPAPP KPEPKPRKTS AKKEPGAKIS RGAKGKKEEK QEAGKEGTEN.

    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.

    Hmgn3 Human
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