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Search results

1000 results found for “lactoferrin”

Name

Description

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  • View Data Sheet

    Name :

    BMP 2 Human, Monomer

    Description:

    Bone Morphogenetic Protein-2 Human Recombinant, Monomer

    BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.

    Product # :

    CYT-627

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    Description

    Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 115 amino acids (283-396) and having a molecular mass of 13009 Dalton. The BMP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-2 solution contains 10mM NaAc pH=3.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.

    • Synonyms

      BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.

    • Background

      What is the molecular weight/Mw of BMP2 Protein?
      BMP2 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP2 Protein?
      Escherichia Coli.

      What is the Purity of BMP2 Protein?
      BMP2 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP2 Protein?
      The biological functionality of BMP2 Protein will be determined in the future.

      What is the amino acid sequence of BMP2 Protein?
      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.

      What applications can BMP2 Protein be used in?
      BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP2 Protein?
      The endotoxin level is minimal, BMP2 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.

    Bmp 2 Human Monomer
  • View Data Sheet

    Name :

    FGF 18 Mouse

    Description:

    Fibroblast Growth Factor-18 Mouse Recombinant

    Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

    Product # :

    CYT-064

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    • sds-page

    Description

    FGF-18 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 21kDa.The FGF-18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-18 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    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 dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

    sds-page

    fgf18 mouse sds-page - Product image 1

    More Info

    • Introduction

      Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a heparin binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

    • Synonyms

      Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.

    • Background

      What is the molecular weight/Mw of FGF18 Protein?
      FGF18 Protein has a total Mw of 21kDa.

      What is the source or expression system of FGF18 Protein?
      Escherichia Coli.

      What is the Purity of FGF18 Protein?
      FGF18 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF18 Protein?
      The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

      What is the amino acid sequence of FGF18 Protein?
      EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.

      What applications can FGF18 Protein be used in?
      FGF18 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF18 Protein?
      The endotoxin level is minimal, FGF18 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.

    Fgf 18 Mouse
  • View Data Sheet

    Name :

    CCL16 Human

    Description:

    LEC/NCC-4 Human Recombinant

    C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

    Product # :

    CHM-237

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    CCL16 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids and having a molecular mass of 11.2 kDa. The CCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL16 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Human CCL16, also called HCC-4, liver-expressed chemokine (LEC), and lymphocyte and monocyte chemoattractant (LMC), is a novel CC chemokine recognized by bioinformatics. NCC-4 cDNA encodes a 120 amino acids along with a 23 amino acids signal peptide that is cleaved to generate 97 amino acid protein. HCC4 is vaguely related to other CC chemokines, showing less than 30% sequence identity. Among CC chemokines, CCL-16 has the largest similarity to HCC-1. 2 potential polyadenylation signals are present on the human HCC-4 gene, and as a result, 2 transcripts containing roughly 1,500 base pairs and 500 base pairs have been detected. HCC-4 is expressed weakly by some lymphocytes, including NK cells, T cells, and some T cell clones. The expression of HCC-4 in monocytes is greatly upregulated in the presence of IL-10.
      CCL16 shows chemotactic activity for lymphocytes and monocytes rather than to neutrophils. NCC-4 has potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. CCL16 demonstrates chemotactic activity for monocytes and thp-1 monocytes, rather than for resting lymphocytes and neutrophils. HCC-4 induces a calcium flux in thp-1 cells that desensitized prior to the expression of rantes.

    • Synonyms

      C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL16 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 CCL16in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

    • Background

      What is the molecular weight/Mw of CCL16 HUMAN Protein?
      CCL16 HUMAN Protein has a total Mw of 11.2kDa.

      What is the source or expression system of CCL16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL16 HUMAN Protein?
      CCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL16 HUMAN Protein?
      Determined by its ability to chemoattract total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL16 HUMAN Protein?
      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

      What applications can CCL16 HUMAN Protein be used in?
      CCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL16 HUMAN Protein?
      The endotoxin level is minimal, CCL16 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.

    Ccl16 Human
  • View Data Sheet

    Name :

    GADD45G Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Gamma Human Recombinant

    DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.

    Product # :

    PRO-570

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    Description

    GADD45G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids and having a molecular mass of 17.1 kDa.

    Source

    Escherichia Coli.

    Formulation

    The GADD45G protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GADD45G is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45G reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45G acts as a new-age tumor suppressor however is being frequently inactivated epigenetically in multiple tumors. GADD45G mRNA expression is down-regulated in hepatocellular carcinoma. GADD45G causes cell cycle arrest at G2/M transition when transfected into Hep-G2 cells. GADD45 Gamma induction by androgens involves new protein synthesis. Overexpression of GADD45 Gamma inhibits cell growth and causes morphological modifications in prostate cell lines thus GADD45 gamma takes part in differentiation induction by androgens.

    • Synonyms

      DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.

    • 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

      MTLEEVRGQD TVPESTARMQ GAGKALHELL LSAQRQGCLT AGVYESAKVL NVDPDNVTFC VLAAGEEDEG DIALQIHFTL IQAFCCENDIDIVRVGDVQR LAAIVGAGEE AGAPGDLHCI LISNPNEDAW KDPALEKLSL FCEESRSVND WVPSITLPE.

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    Gadd45G Human
  • View Data Sheet

    Name :

    GAGA-POZ

    Description:

    GAGA-POZ Drosophila Melanogaster Recombinant

    Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.

    Product # :

    PRO-435

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    Description

    GAGA-POZ Drosophila Melanogaster Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids & having a molecular mass of 14 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein containing 10mM HEPES (pH-7.4) and 25mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      The GAGA factor is a sequence-specific DNA-binding protein, which participates in the regulation of the expression of a variety of different classes of genes in Drosophila such as many developmentally regulated genes, stress induced genes, and cell cycle regulated genes, as well as housekeeping genes. GAGA contains a C-terminal glutamine-rich domain and a highly conserved N-terminal POZ domain which reported to be involved in self-oligomerization in a number of other POZ domain containing proteins. In case of GAGA protein, the N-terminal POZ domain mediates the formation of oligomers both in vitro and in vivo.

    • Synonyms

      Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.

    • 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

      MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLLDLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQTVTKDDYTTH.

    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.

    Gaga Factor
  • View Data Sheet

    Name :

    LCN1 Human

    Description:

    Lipocalin-1 Human Recombinant

    Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.

    Product # :

    ENZ-825

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    Description

    LCN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (19-176 a.a) and having a molecular mass of 20.1kDa. LCN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipocalin-1 (LCN1) belongs to the lipocalin family of small secretory proteins. Lipocalins are extracellular transport proteins, which bind to various hydrophobic ligands. LCN1 protein is the principal lipid binding protein in tears and is overproduced in response to numerous stimuli including infection and stress. LCN1 is a marker for chromosome aneuploidy as well as an autoantigen in Sjogren's syndrome.

    • Synonyms

      Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.

    • 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 MGSHMHHLLA SDEEIQDVSG TWYLKAMTVD REFPEMNLES VTPMTLTTLE GGNLEAKVTM LISGRCQEVK AVLEKTDEPG KYTADGGKHV AYIIRSHVKD HYIFYCEGEL HGKPVRGVKL VGRDPKNNLE ALEDFEKAAG ARGLSTESIL IPRQSETCSP GSD.

    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.

    Lcn1 Human
  • View Data Sheet

    Name :

    LCN2 Human, Pichia

    Description:

    Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant, Pichia

    Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.

    Product # :

    ENZ-064

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    Description

    Neutrophil Gelatinase Associated Lipocalin Human Recombinant is expressed in Pichia pastoris having a molecular weight of approximately 21kDa.The LCN2 is purified by proprietary chromatographic techniques.

    Source

    Pichia pastoris.

    Formulation

    LCN2 was lyophilized from 0.02M NH4HCO3.

    Purity

    Greater than 96% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
      They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

    • Synonyms

      Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LCN2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCN2 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 LCN2 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.

    Lcn2 Human Pichia
  • View Data Sheet

    Name :

    LDOC1L Human

    Description:

    Leucine Zipper, Down-Regulated in Cancer 1-Like Human Recombinant

    Protein LDOC1L, Leucine zipper protein down-regulated in cancer cells-like, Mammalian retrotransposon-derived protein 6, LDOC1L, MAR6, MART6, dJ1033E15.2.

    Product # :

    PRO-1153

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    Description

    LDOC1L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-239 a.a) and having a molecular mass of 28.7kDa.LDOC1L is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LDOC1L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% glycerol, 2mM DTT, 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine zipper down-regulated in cancer 1-like (LDOC1L) is a member of the LDOC1 family. LDOC1L is a nuclear protein containing a leucine zipper-like motif and a proline-rich region that shares noticeable similarity with an SH3-binding domain. LDOC1L localizes to the nucleus and is downregulated in certain cancer cell lines. LDOC1L is believed to regulate the transcriptional response mediated by the nuclear factor kB (NFkB).

    • Synonyms

      Protein LDOC1L, Leucine zipper protein down-regulated in cancer cells-like, Mammalian retrotransposon-derived protein 6, LDOC1L, MAR6, MART6, dJ1033E15.2.

    • 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 MGSHMVQPQT SKAESPALAA SPNAQMDDVI DTLTSLRLTN SALRREASTL RAEKANLTNM LESVMAELTL LRTRARIPGA LQITPPISSI TSNGTRPMTT PPTSLPEPFS GDPGRLAGFL MQMDRFMIFQ ASRFPGEAER VAFLVSRLTG EAEKWAIPHM QPDSPLRNNY QGFLAELRRT YKSPLRHARR AQIRKTSASN RAVRERQMLC RQLASAGTGP CPVHPASNGT SPAPALPARA RNL.

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    Ldoc1L Human
  • View Data Sheet

    Name :

    TrxR Yeast

    Description:

    Thioredoxin Reductase (NADPH) Yeast Recombinant

    Thioredoxin Reductase (NADPH), NTR, TrxR.

    Product # :

    ENZ-278

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    Description

    Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 20mM phosphate buffer pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 5.8 IU/mg.

    More Info

    • Introduction

      Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.

    • Synonyms

      Thioredoxin Reductase (NADPH), NTR, TrxR.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Unit Definition

      One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).

    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.

    Thioredoxin Reductase Yeast
  • View Data Sheet

    Name :

    Leptin tA Human, PEG

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant, Pegylated

    Product # :

    CYT-702

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    Description

    Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below - 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant pegylated Human Recombinant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Ta Human Pegylated
  • View Data Sheet

    Name :

    GrpE E.Coli

    Description:

    HSP-70 Cofactor (HSP24) E.Coli Recombinant

    HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    Product # :

    HSP-014

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    Description

    GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

    • Synonyms

      HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    • 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

      MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.

    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.

    Grpe Ecoli
  • View Data Sheet

    Name :

    Vaspin Human

    Description:

    Vaspin Recombinant Human

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-1132

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 394 amino acids and having a molecular mass of 45.1kDa. Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 0.02 % Tween-20.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN) is a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Vaspin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vaspin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Vaspin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK.

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    Vaspin Protein
  • View Data Sheet

    Name :

    Vaspin Human, His

    Description:

    Vaspin Human Recombinant, His Tag

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-459

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid Vaspin although stable at 10°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

    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.

    Vaspin Human
  • View Data Sheet

    Name :

    VEGI Human, His

    Description:

    Vascular Endothelial Growth InhibitorHuman Recombinant, His Tag

    Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

    Product # :

    CYT-589

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    Description

    VEGI Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids(72-251a.a.) and having a molecular mass of 22.7kDa. The VEGI is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

    • 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 MLKGQEFAPS HQQVYAPLRA DGDKPRAHLT VVRQTPTQHF KNQFPALHWE HELGLAFTKN RMNYTNKFLL IPESGDYFIY SQVTFRGMTS ECSEIRQAGR PNKPDSITVV ITKVTDSYPE PTQLLMGTKS VCEVGSNWFQ PIYLGAMFSL QEGDKLMVNV SDISLVDYTK EDKTFFGAFL L

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    Vegi Human His
  • View Data Sheet

    Name :

    Leptin Human, Mutant

    Description:

    Leptin Mutant D23L Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1243

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    Description

    Human Leptin Mutant D23L is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. Leptin Mutant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    Leptin Mutant was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Human Leptin Mutant D23L is fully biologically active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Leptin Mutant D23L although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Mutant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids of recombinant human leptin was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Background

      Leptin’s main part is to regulate long-term energy balance. Leptin is a hormone which mainly produced by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

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    Mutant Leptin
  • View Data Sheet

    Name :

    ORM1

    Description:

    Orosomucoid 1 Human Recombinant

    Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 1.

    Product # :

    PRO-889

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    Description

    ORM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (19-201) and having a molecular mass of 21.7 kDa.The ORM1 is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ORM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The acute phase plasma protein ORM1 synthesized by the liver mediates the interaction between blood cells and endothelial cells. In addition, together with haptoglobin and C reactive protein, ORM1 regulates the extravasation of the cells through infection and inflammation. Expression of ORM1 is induced by acute-phase stimulatory mediators such as bacterial lipopolysaccharides.

    • Synonyms

      Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 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

      MQIPLCANLV PVPITNATLD QITGKWFYIA SAFRNEEYNK SVQEIQATFF YFTPNKTEDT IFLREYQTRQ DQCIYNTTYL NVQRENGTIS RYVGGQEHFA HLLILRDTKT YMLAFDVNDE KNWGLSVYAD KPETTKEQLG EFYEALDCLR IPKSDVVYTD WKKDKCEPLE KQHEKERKQE EGES.

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    Orm1 Human
  • View Data Sheet

    Name :

    CST3 Mouse

    Description:

    Cystatin-C Mouse Recombinant

    Post G-globulin, CST 3, CST3, Gamma-Trace, Cystatin 3, Amyloid Angiopathy and Cerebral Hemorrhage, Cystatin-C precursor, neuroendocrine basic polypeptide.

    Product # :

    PRO-597

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    Description

    Cystatin-C Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15kDa. The Mouse Cystatin-C is fused to His tag at N-Terminus.The Mouse Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Post G-globulin, CST 3, CST3, Gamma-Trace, Cystatin 3, Amyloid Angiopathy and Cerebral Hemorrhage, Cystatin-C precursor, neuroendocrine basic polypeptide.

    • Physical Appearance

      Sterile 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

      Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MRGSHHHHHH GMASATPKQG PRMLGAPEEA DANEEGVRRA LDFAVSEYNK GSNDAYHSRA IQVVRARKQL VAGVNYFLDV EMGRTTCTKS QTNLTDCPFH DQPHLMRKAL CSFQIYSVPW KGTHSLTKFSCKNA.

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    Cystatin C Mouse
  • View Data Sheet

    Name :

    CST3 Rat, sf9

    Description:

    Cystatin C Rat Recombinant, sf9

    Cystatin-C, Cystatin-3.

    Product # :

    PRO-2311

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    Description

    CST3 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 128 amino acids (21-140a.a.) and having a molecular mass of 14.3kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). CST3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques

    Source

    Sf9, Baculovirus cells.

    Formulation

    CST3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-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

      GTSRPPPRLL GAPQEADASE EGVQRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGI NYYLDVEMGR TTCTKSQTNL TNCPFHDQPH LMRKALCSFQ IYSVPWKGTH TLTKSSCKNA LEHHHHHH.

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    Cst3 Rat Sf9
  • View Data Sheet

    Name :

    Adiponectin Mouse, HEK

    Description:

    Adiponectin Mouse Recombinant, HEK

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-435

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    Description

    The Acrp30 Mouse Recombinant is fused with FLAG tag having a total Mw of 26kDa.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M PBS buffer,0.075M NaCl, pH7.4.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml.  An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.

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    • Introduction

      Adiponectin is an important negative regulator in hematopoiesis and immune systems. It may be involved in ending inflammatory responses through its inhibitory functions. Inhibits endothelial nf-kappa-b signaling through a camp-dependent pathway. Inhibits tnf-alpha- induced expression of endothelial adhesion molecules. Involved in the control of fat metabolism and insulin sensitivity.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Stability

      Store lyophilized APM-1 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 reconstitute the lyophilized Acrp30 Mouse in sterile 18M-cm H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293.

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of ADIPONECTIN Protein?
      Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.

      What is the amino acid sequence of ADIPONECTIN Protein?
      EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.

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

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

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    Adiponectin Mouse Hek
  • View Data Sheet

    Name :

    CTSF Human, Sf9

    Description:

    Cathepsin-F Human Recombinant, Sf9

    CTSF, CATSF, CLN13.

    Product # :

    ENZ-1167

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    Description

    CTSF produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 474 amino acids (20-484.a.a) and having a molecular mass of 52.5kDa.CTSF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTSF protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of Z-Phe-ArgAMC to Z-Phe-Arg and AMC per minute at pH 5.0 at 37℃.

    More Info

    • Introduction

      Cathepsin F (CTSF) is a member of the peptidase C1 family. Cathepsins are papain family cysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF is involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.

    • Synonyms

      CTSF, CATSF, CLN13.

    • 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

      ADLAPAQPRA ASFQAWGPPS PELLAPTRFA LEMFNRGRAA GTRAVLGLVR GRVRRAGQGS LYSLEATLEE PPCNDPMVCR LPVSKKTLLC SFQVLDELGR HVLLRKDCGP VDTKVPGAGE PKSAFTQGSA MISSLSQNHP DNRNETFSSV ISLLNEDPLS QDLPVKMASI FKNFVITYNR TYESKEEARW RLSVFVNNMV RAQKIQALDR GTAQYGVTKF SDLTEEEFRT IYLNTLLRKE PGNKMKQAKS VGDLAPPEWD WRSKGAVTKV KDQGMCGSCW AFSVTGNVEG WFLNQGTLL SLSEQELLDC DKMDKACMGG LPSNAYSAIK NLGGLETEDD YSYQGHMQSC NFSAEKAKVY INDSVELSQN EQKLAAWLAK RGPISVAINA FGMQFYRHGI SRPLRPLCSP WLIDHAVLLV GYGNRSDVPF WAIKNSWGTD WGEKGYYYLH RGSGACGVNT MASSAVVDHH HHHH

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    Ctsf Protein
  • View Data Sheet

    Name :

    NENF Human

    Description:

    Neudesin Neurotrophic Factor Human Recombinant

    Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

    Product # :

    CYT-778

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    Description

    NENF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 32-172) containing 151 amino acids including a 10 a.a N-terminal His tag and having a molecular mass of 16.9kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neudesin Neurotrophic Factor (NENF) is a member of the cytochrome b5 family, MAPR subfamily. NENF contains 1 cytochrome b5 heme-binding domain. NENF exhibits neurotrophic activity and activates phosphorylation of MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT in primary cultured neurons. NENF doesn’t have mitogenic activity in primary cultured astrocytes. NENF may play a part in neuronal differentiation and may have a transient influence on neural cell proliferation in neural precursor cells. NENF neurotrophic activity is increased by binding to heme. NENF is up-regulated in immortal cells and induced in estrogen receptor positive breast cancer expressing progesterone receptor.

    • Synonyms

      Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. NENF is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASGQTPRPAERG PPVRLFTEEE LARYGGEEED QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL TGKDSTRGVA KMSLDPADLT HDTTGLTAKE LEALDEVFTK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F.

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    Nenf Human
  • View Data Sheet

    Name :

    NFKBIA Human

    Description:

    NF-kappa-B Inhibitor Alpha Human Recombinant

    Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha, nuclear factor of kappa light chain gene enhancer in B-cells, IKBA, I-kappa-B-alpha, IkappaBalpha, ikB-alpha, NFKBI, MAD-3, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha.

    Product # :

    PRO-960

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    Description

    NFKBIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-317) and having a molecular mass of 37.7 kDa.NFKBIA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NFKBIA belongs to the I-kappa-B family of proteins which is separated into four groups (IkB-a, IkB-b, IkB-g, IkB-e). NFKBIA inhibits the NFkB complex by binding and impounding it in the cytoplasm. When stimulated, NFKBIA is phosphorylated on serine residues targeting it for degradation by the ubiquitin pathway.

    • Synonyms

      Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha, nuclear factor of kappa light chain gene enhancer in B-cells, IKBA, I-kappa-B-alpha, IkappaBalpha, ikB-alpha, NFKBI, MAD-3, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha.

    • 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 MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ EIRLEPQEVP RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD LAFLNFQNNL QQTPLHLAVI TNQPEIAEAL LGAGCDPELR DFRGNTPLHL ACEQGCLASV GVLTQSCTTP HLHSILKATN YNGHTCLHLA SIHGYLGIVE LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG ADVNRVTYQG YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE DELPYDDCVF GGQRLTL

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    Nfkbia Human
  • View Data Sheet

    Name :

    SOCS3 Human

    Description:

    Suppressor Of Cytokine Signaling 3 Human Recombinant

    Suppressor Of Cytokine Signaling 3, CIS3, SSI3, Cytokine-Inducible SH2 Protein 3, STAT-Induced STAT Inhibitor 3, ATOD4, Cish3, MGC71791, CIS-3.

    Product # :

    PRO-1891

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    Description

    SOCS3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (1-225 a.a) and having a molecular mass of 29kDa.SOCS3 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOCS3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Suppressor of Cytokine Signaling 3, also known as SOCS3 belongs to the SOCS family; in addition SOCS3 is a member of the STAT-induced STAT inhibitor (SSI). The SSI family members are cytokine-inducible negative regulators of cytokine signaling. The expression of SOCS3 is induced by different cytokines, including IL6 and IL10. SOCS3 can bind to JAK2 kinase, and inhibit the activity of JAK2 kinase. Studies of the mouse counterpart of SOCS3 have shown the roles of SOCS3 in the negative regulation of fetal liver hematopoiesis, and placental development.

    • Synonyms

      Suppressor Of Cytokine Signaling 3, CIS3, SSI3, Cytokine-Inducible SH2 Protein 3, STAT-Induced STAT Inhibitor 3, ATOD4, Cish3, MGC71791, CIS-3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMVT HSKFPAAGMS RPLDTSLRLK TFSSKSEYQL VVNAVRKLQE SGFYWSAVTG GEANLLLSAE PAGTFLIRDS SDQRHFFTLS VKTQSGTKNL RIQCEGGSFS LQSDPRSTQP VPRFDCVLKL VHHYMPPPGA PSFPSPPTEP SSEVPEQPSA QPLPGSPPRR AYYIYSGGEK IPLVLSRPLS SNVATLQHLC RKTVNGHLDS YEKVTQLPGP IREFLDQYDA PL

    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.

    Socs3 Human
  • View Data Sheet

    Name :

    CDH1 Human, Sf9

    Description:

    E-Cadherin Human Recombinant, Sf9

    Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-1.

    Product # :

    PRO-2265

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CDH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 694 amino acids (24-709a.a.) and having a molecular mass of 76.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70kDa). CDH1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CDH1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.

    • Synonyms

      Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-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

      EPEPCHPGFD AESYTFTVPR RHLERGRVLG RVNFEDCTGR QRTAYFSLDT RFKVGTDGVI TVKRPLRFHN PQIHFLVYAW DSTYRKFSTK VTLNTVGHHH RPPPHQASVS GIQAELLTFP NSSPGLRRQK RDWVIPPISC PENEKGPFPK NLVQIKSNKD KEGKVFYSIT GQGADTPPVG VFIIERETGW LKVTEPLDRE RIATYTLFSH AVSSNGNAVE DPMEILITVT DQNDNKPEFT QEVFKGSVME GALPGTSVME VTATDADDDV NTYNAAIAYT ILSQDPELPD KNMFTINRNT GVISVVTTGL DRESFPTYTL VVQAADLQGE GLSTTATAVI TVTDTNDNPP IFNPTTYKGQ VPENEANVVI TTLKVTDADA PNTPAWEAVY TILNDDGGQF VVTTNPVNND GILKTAKGLD FEAKQQYILH VAVTNVVPFE VSLTTSTATV TVDVLDVNEA PIFVPPEKRV EVSEDFGVGQ EITSYTAQEP DTFMEQKITY RIWRDTANWL EINPDTGAIS TRAELDREDF EHVKNSTYTA LIIATDNGSP VATGTGTLLL ILSDVNDNAP IPEPRTIFFC ERNPKPQVIN IIDADLPPNT SPFTAELTHG ASANWTIQYN DPTQESIILK PKMALEVGDY KINLKLMDNQ NKDQVTTLEV SVCDCEGAAG VCRKAQPVEA GLQIPALEHH 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.

    Cdh1 Human Sf9
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