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  • MEC (CCL28)

    MEC (CCL28)

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  • LD78-beta (CCL3L1)

    LD78-beta (CCL3L1)

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  • CTACK (CCL27)

    CTACK (CCL27)

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  • CXCL16

    CXCL16

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    CXCL17

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    Platelet Factor-4 (CXCL4)

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  • ENA-78 (CXCL5)

    ENA-78 (CXCL5)

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  • Eotaxin (CCL11,24,26)

    Eotaxin (CCL11,24,26)

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    Exodus-2 (CCL21)

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  • Fractalkine (CX3CL1)

    Fractalkine (CX3CL1)

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    CXCL6

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  • CD14

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    Pigment Epithelium-Derived Factor

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    Ankyrin Repeat Domain

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Search results

1000 results found for “selenoprotein”

Name

Description

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  • View Data Sheet

    Name :

    GFP

    Description:

    Glial Filament Protein

    Glial Filament Protein, GFP.

    Product # :

    PRO-522

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    Description

    Ultra Pure Glial Filament Protein having a Molecular mass of 52 kDa.

    Source

    Bovine Spinal Cord.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 2mM DTT, 1mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GFP is an intermediate filament. GFP and vimentin are linked to the same filament network; they are localized in the same filaments.
      mRNAs encoding the glial intermediate filament protein are spatially dispersed in the glial cell cytoplasm close to the location of the glial filaments.

    • Synonyms

      Glial Filament Protein, GFP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    Glial Filament Protein
  • 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.

    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.

    Ldoc1L Human
  • View Data Sheet

    Name :

    TXNL1 Human

    Description:

    Thioredoxin-Like 1 Human Recombinant

    Thioredoxin-like protein 1, TRP32, Txl, 32 kDa thioredoxin-related protein, TXNL, Thioredoxin-like 32kDa, TXL-1.

    Product # :

    PRO-084

    Price :

    Quantity :

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    Description

    TXNL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-289.a.a) and having a molecular mass of 34.4kDa. TXNL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TXNL1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TXNL1 is a cytoplasmic protein which takes part in endocytotic signaling pathways and acts as a redox sensor. TXNL1 is universally expressed in the body and its goal is to couple oxidative stress to endocytosis, thereby regulating the GDI. Moreover, overexpression of TXNL1 inhibits cell proliferation by predisposing the cell to G0/G1 arrest, signifying that TXNL1 also functions as a transcriptional repressor.

    • Synonyms

      Thioredoxin-like protein 1, TRP32, Txl, 32 kDa thioredoxin-related protein, TXNL, Thioredoxin-like 32kDa, TXL-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDTDIP KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDTTFLESD CDEQLLITVA FNQPVKLYSM KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN VNSVTIFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH

    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.

    Txnl1 Human
  • View Data Sheet

    Name :

    CXCL2 Mouse

    Description:

    GRO-Beta Mouse Recombinant (CXCL2)

    Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    Product # :

    CHM-338

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
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    • biological activity
    • More Info

    Description

    GRO-Beta Mouse Recombinant also caled mouse MIP-2 produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7849 Dalton. The CXCL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

    Purity

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

    Biological Activity

    The Biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 105-106units/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

    • Synonyms

      Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Mouse in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVVASELRCQ CLKTLPRVDF KNIQSLSVTP PGPHCAQTEV IATLKGGQKV CLDPEAPLVQ KIIQKILNKG KAN.

    • Background

      What is the molecular weight/Mw of CXCL2 MOUSE Protein?
      CXCL2 MOUSE Protein has a total Mw of 7.84kDa.

      What is the source or expression system of CXCL2 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL2 MOUSE Protein?
      CXCL2 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL2 MOUSE Protein?
      The Biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 105-106units/mg.

      What is the amino acid sequence of CXCL2 MOUSE Protein?
      AVVASELRCQ CLKTLPRVDF KNIQSLSVTP PGPHCAQTEV IATLKGGQKV CLDPEAPLVQ KIIQKILNKG KAN.

      What applications can CXCL2 MOUSE Protein be used in?
      CXCL2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL2 MOUSE Protein?
      The endotoxin level is minimal, CXCL2 MOUSE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.015 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 GRO-b 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.

    Gro Beta Mouse
  • View Data Sheet

    Name :

    LYN Human

    Description:

    v-yes-1 Yamaguchi Sarcoma Viral Related Oncogene Human Recombinant

    Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.

    Product # :

    PRO-136

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    Description

    LYN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 535 amino acids (1-512) and having a molecular mass of 61.0kDa. LYN is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosine-protein kinase Lyn (LYN) belongs to the src family of non-receptor protein tyrosine kinases, which is primarily expressed in haematopoietic tissues. LYN protein is involved in induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. LYN protein stimulates SAPK by a MKK7- and MEKK1-dependent mechanism. The LYN - MEKK1 - MKK7 - SAPK pathway is efficient in the induction of apoptosis by genotoxic agents.

    • Synonyms

      Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.

    • 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 MGSMGCIKSK GKDSLSDDGV DLKTQPVRNT ERTIYVRDPT SNKQQRPVPE SQLLPGQRFQ TKDPEEQGDI VVALYPYDGI HPDDLSFKKG EKMKVLEEHG EWWKAKSLLT KKEGFIPSNY VAKLNTLETE EWFFKDITRK DAERQLLAPG NSAGAFLIRE SETLKGSFSL SVRDFDPVHG DVIKHYKIRS LDNGGYYISP RITFPCISDM IKHYQKQADG LCRRLEKACI SPKPQKPWDK DAWEIPRESI KLVKRLGAGQ FGEVWMGYYN NSTKVAVKTL KPGTMSVQAF LEEANLMKTL QHDKLVRLYA VVTREEPIYI ITEYMAKGSL LDFLKSDEGG KVLLPKLIDF SAQIAEGMAY IERKNYIHRD LRAANVLVSE SLMCKIADFG LARVIEDNEY TAREGAKFPI KWTAPEAINF GCFTIKSDVW SFGILLYEIV TYGKIPYPGR TNADVMTALS QGYRMPRVEN CPDELYDIMK MCWKEKAEER PTFDYLQSVL DDFYTATEGQ YQQQP.

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    Lyn Human
  • View Data Sheet

    Name :

    GRXB E.Coli

    Description:

    Glutaredoxin-2 E.Coli Recombinant

    Glutaredoxin-2, Grx2, grxB, b1064, JW1051.

    Product # :

    ENZ-130

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    Description

    GRXB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (1-215 a.a.) and having a molecular mass of 26.5kDa.GRXB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutaredoxin-2 (GrxB) is amember of the glutaredoxin family. Glutaredoxins are small redox enzymes of approximately 100 amino-acid residues which use glutathione as a cofactor. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. GrxB is involved in reducing some disulfides in a coupled system with glutathione reductase. GrxB doesn’t act as hydrogen donor for ribonucleotide reductase.

    • Synonyms

      Glutaredoxin-2, Grx2, grxB, b1064, JW1051.

    • 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 MKLYIYDHCP YCLKARMIFG LKNIPVELHV LLNDDAETPT RMVGQKQVPI LQKDDSRYMP ESMDIVHYVD KLDGKPLLTG KRSPAIEEWL RKVNGYANKL LLPRFAKSAF DEFSTPAARK YFVDKKEASA GNFADLLAHS DGLIKNISDD LRALDKLIVK PNAVNGELSE DDIQLFPLLR NLTLVAGINW PSRVADYRDN MAKQTQINLL SSMAI.

    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.

    Grxb 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.

    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 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.

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    Vaspin Human
  • View Data Sheet

    Name :

    YWHAG Human

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant

    14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    Product # :

    PKA-238

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    Description

    YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids (1-247) and having a molecular mass of 28 kDa. YWHAG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAG solution containing 20mM Tris 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

    • Synonyms

      14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    • 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

      MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN.

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    Ywhag Human
  • View Data Sheet

    Name :

    YWHAQ Human

    Description:

    Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta Human Recombinant

    14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

    Product # :

    PKA-254

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    Description

    YWHAQ Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-245) and having a molecular mass of 27 kDa. YWHAQ is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAQ solution containing 20mM Tris 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, ?, ?, ?, ?, ?, ? and ? that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.

    • Synonyms

      14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWRVISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLKMKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYEILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN.

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    Ywhaq Human
  • View Data Sheet

    Name :

    REG1A Human

    Description:

    Regenerating Islet-Derived 1 Alpha Human Recombinant

    Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.

    Product # :

    PRO-289

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    Description

    The Recombinant Human REG 1 alpha is produced with N-terminal fusion His Tag. The Recombinant Human REG 1 alpha His-Tagged Fusion Protein, has a molecular weight of 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 alpha and 12 additional amino acid residues – His Tag.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 5mM Tris, 25mM NaCl, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
      Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system.

    • Synonyms

      Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS HMQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN.

    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.

    Reg1A Human
  • View Data Sheet

    Name :

    CTGF Human, HEK

    Description:

    Connective Tissue Growth Factor Human Recombinant , HEK

    CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.

    Product # :

    CYT-687

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    Description

    The CTGF Human Recombinant produced in HEK293 cells, is 36kDa protein containing a total of 329 amino acid residues (aa 27-349) including a C-terminal 6×His tag.

    Source

    HEK293 cells.

    Formulation

    CTGF filtered (0.2µm) solution in 0.1M Citrate buffer pH 4.7 and 20% (w/v) glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
      CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
      Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
      The full length protein consists of four modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
      Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
      Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
      Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
      Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
      In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
      CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

    • Synonyms

      CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.

    • Physical Appearance

      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

      QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

    • Background

      What is the molecular weight/Mw of CTGF Protein?
      CTGF Protein has a total Mw of 36kDa.

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

      What is the Purity of CTGF Protein?
      CTGF Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CTGF Protein?
      QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.

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

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

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    Ctgf Humam Hek
  • View Data Sheet

    Name :

    Y.Enterocolitica (O:9) YopB

    Description:

    Yersinia Enterocolitica (O:9) YopB Recombinant

    Protein YopD, pYV0054.

    Product # :

    PRO-2575

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    Description

    Recombinant Yersinia Enterocolitica (O:9) YopB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain having a calculated molecular mass of 43kDa. Y.Enterocolitica (O:9) YopB is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Y.Enterocolitica (O:9) YopB is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

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    • Introduction

      Gastroenteritis which has been identified as caused by Yersinia Enterocolitica has been discovered by virulent isolates of the bacteria. During infection, pores are being formed in the presence of adapter protein Yersiniosis. YopB's Interaction with the target membrane to form pores enables the entrance of YopE effectors to the cytoplasmic space of the host’s cell.

    • Synonyms

      Protein YopD, pYV0054.

    • 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.

    • Immunological Activity

      1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with positive/negative samples.

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    Yopb Protein
  • View Data Sheet

    Name :

    AMTN Human

    Description:

    Amelotin Human Recombinant

    UNQ689, Amelotin, PRO1329.

    Product # :

    PRO-1301

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    Description

    AMTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (17-209 a.a.) and having a molecular mass of 22.2kDa.AMTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AMTN protein solution (0.5mg/ml) contains mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      AMTN is a member of the amelotin family. AMTN is a lately discovered secreted enamel protein. AMTN mainly expressed during the maturation stage of enamel formation. AMTN gathers in a basal lamina-like structure at the interface between ameloblasts and enamel mineral and it co-localizes with one more lately described enamel protein, odontogenic ameloblast- related protein (ODAM(.

    • Synonyms

      UNQ689, Amelotin, PRO1329.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSLPQLKPA LGLPPTKLAP DQGTLPNQQQ SNQVFPSLSL IPLTQMLTLG PDLHLLNPAA GMTPGTQTHP LTLGGLNVQQ QLHPHVLPIF VTQLGAQGTI LSSEELPQIF TSLIIHSLFP GGILPTSQAG ANPDVQDGSL PAGGAGVNPA TQGTPAGRLP TPSGTDDDFA VTTPAGIQRS THAIEEATTE SANGIQ.

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    Amtn Human
  • View Data Sheet

    Name :

    EREG Human

    Description:

    Epiregulin Human Recombinant

    EREG, Epiregulin, ER.

    Product # :

    CYT-609

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    Description

    Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

    More Info

    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      EREG, Epiregulin, ER.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 5.6kDa.

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

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

      What is the Biological Activity of EREG Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

      What is the amino acid sequence of EREG Protein?
      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

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

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

    Epiregulin Human
  • View Data Sheet

    Name :

    SPP1 Human, HEK

    Description:

    Osteopontin Human Recombinant, HEK

    Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    Product # :

    CYT-047

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    Description

    Osteopontin Human Recombinant is a single, glycosylated, polypeptide chain produced in HEK293 cells, is a full length protein (amino acids 17-314) fused with a polyhistidine tag at the C-terminus, having a total calculated molecular mass of 34.5kDa (The actual molecular mass may be approximately 60-65kDa in SDS-PAGE under reducing conditions due to glycosylation).Osteopontin is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    Osteopontin was lyophilized from a 0.2µM filtered solution of 20mM PBS and 150mM NaCl, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
      Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

    • Synonyms

      Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      It is recommended to reconstitute the lyophilized SPP1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETL
      PSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDEL
      VTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDIT
      SHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRK
      ANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDS
      ASSEVNVDHHHHHH.

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    Spp1 Human Hek
  • View Data Sheet

    Name :

    CAPG Antibody

    Description:

    Capping Protein Gelsolin-Like, Mouse Anti Human

    AFCP, CAPG, Macrophage-capping protein, Actin regulatory protein CAP-G, MCP.

    Product # :

    ANT-643

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    Formulation

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

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    • Introduction

      CAPG is part of the gelsolin/villin family of actin-regulatory proteins. CAPG reversibly blocks the barbed ends of F-actin filaments in a Ca2+ and phosphoinositide-regulated method, though it does not separate preformed actin filaments. By capping the barbed ends of actin filaments, CAPG contributes to the control of actin-based motility in non-muscle cells. CAPG is involved in macrophage function. CAPG is involved in regulating cytoplasmic and/or nuclear structures via possible interactions with actin. CAPG binds DNA. CAPG lacks a nuclear export sequence present in structurally related proteins. CAPG is a tumor suppressor protein that plays a role in the tumorigenic progression of certain cancers. Dysregulated expression of CAPG was found in premalignant and malignant oral carcinogenesis.

    • Synonyms

      AFCP, CAPG, Macrophage-capping protein, Actin regulatory protein CAP-G, MCP.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CAPG mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CAPG amino acids 1-348 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT1D10AT.

    • Applications

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

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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    Capg Antibody
  • View Data Sheet

    Name :

    ENO1 Human

    Description:

    Enolase-1 Human Recombinant

    NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    Product # :

    ENZ-452

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    Description

    The ENO1 Human Recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 47.1kDa and containing 434 amino acids (1-434 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ENO1 protein solution (1mg/ml) is formulated in 20mM Tris-HCl pH-7.5 1mM MgSO4 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20,000pmol/min/ug, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.

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    • Introduction

      ENO1 is a homodimeric soluble protein that encodes a smaller monomeric structural lens protein, tau-crystallin. ENO1 is a glycolytic enzyme expressed in mainly all tissues. ENO1 isoenzyme full length protein is found in the cytoplasm. The shorter protein is formed from another translation start that is restricted to the nucleus, and binds to a component in the c-myc promoter. ENO1 is involved in anaerobic metabolism under hypoxic conditions and plays a role as a cell surface plasminogen receptor during tissue invasion. Irregular expression of Enolase-1 is linked with tumor progression in several cases of breast and lung cancer. Enolase-1 is as an auto antigen associated with Hashimoto's encephalopathy and severe asthma. ENO1 is the target protein of serum anti-endothelial antibody in Behcet's disease.

    • Synonyms

      NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK AKFAGRNFRN PLAK.

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    Eno1 Human
  • View Data Sheet

    Name :

    S100A7A Human

    Description:

    S100 Calcium Binding Protein A7A Human Recombinant

    NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.

    Product # :

    PRO-756

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    Description

    The S100A7A Human Recombinant is manufactured with N-terminal fusion of 9 amino acids His Tag. The S100A7A His -Tagged Fusion Protein is a 12.3kDa protein containing 109 amino acid residues and 9 additional amino acid residues - His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      S100A7A takes part in epidermal differentiation and inflammation thus is significant for the pathogenesis of psoriasis and other diseases.

    • Synonyms

      NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.

    • Stability

      Store lyophilized S100A7A Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted S100A7A can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add pyrogen free water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MMKHHHHHHASNT­QAERSIIG MIDMFHKYTG RDGKIEKPSL LTMMKENFPN FLSACDKKGI HYLATVFEKK DKNEDKKIDF SEFLSLLGDI AADYHKQSHG AAPCSGGSQ.

    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.

    S100A7A Human
  • View Data Sheet

    Name :

    CTHRC1 Human, Sf9

    Description:

    Collagen Triple Helix Repeat Containing 1 Human Recombinant, Sf9

    Collagen triple helix repeat-containing protein 1 isoform 1, CTHRC1, Protein NMTC1.

    Product # :

    PRO-2606

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    Description

    CTHRC1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 222 amino acids (31-243a.a.) and having a molecular mass of 24.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTHRC1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTHRC1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Collagen triple helix repeat-containing protein 1 or CTHRC1 acts as a negative regulator of collagen matrix deposition. The protein is secreted from a 28kDa protein which is glycosylated and very conserved from lower chordates to mammals. CTHRC1 is found qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers.CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells.

    • Synonyms

      Collagen triple helix repeat-containing protein 1 isoform 1, CTHRC1, Protein NMTC1.

    • 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

      ADPSEIPKGK QKAQLRQREV VDLYNGMCLQ GPAGVPGRDG SPGANGIPGT PGIPGRDGFK GEKGECLRES FEESWTPNYK QCSWSSLNYG IDLGKIAECT FTKMRSNSAL RVLFSGSLRL KCRNACCQRW YFTFNGAECS GPLPIEAIIY LDQGSPEMNS TINIHRTSSV EGLCEGIGAG LVDVAIWVGT CSDYPKGDAS TGWNSVSRII IEELPKHHHH HH.

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

    Cthrc1 Protein
  • View Data Sheet

    Name :

    MMP9 Rat

    Description:

    Matrix Metalloproteinase-9 Rat Recombinant

    Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    Product # :

    ENZ-1185

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    Description

    MMP9 Rat produced in HEK293 cells is a single, glycosylated polypeptide chain containing 695 amino acids (20-708 a.a.) and having a molecular mass of 77.2kDa. MMP9 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    MMP9 Rat protein solution (0.5mg/ml) contains 20mM Tris-HCl pH-7.5, 100mM NaCl , 1mM CaCl2 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    > 2000 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-7.5 at 25C.

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    • Synonyms

      Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    • 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

      APHQRQPTYV VFPRDLKTSN LTDTQLAEDY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS ETLKAIRSPR CGVPDVGKFQ TFEGDLKWHH HNITYWIQSY TEDLPRDVID DSFARAFAVW SAVTPLTFTR VYGLEADIVI QFGVAEHGDG YPFDGKDGLL AHAFPPGPGI QGDAHFDDDE LWSLGKGAVV PTYFGNANGA PCHFPFTFEG RSYLSCTTDG RNDGKPWCGT TADYDTDRKY GFCPSENLYT EHGNGDGKPC VFPFIFEGHS YSACTTKGRS DGYRWCATTA NYDQDKLYGF CPTRADVTVT GGNSAGEMCV FPFVFLGKQY STCTGEGRSD GRLWCATTSN FDADKKWGFC PDQGYSLFLV AAHEFGHALG LDHSSVPEAL MYPMYHYHED SPLHEDDIKG IQHLYGRGSK PDPRPPATTA AEPQPTAPPT MCPTAPPMAY PTGGPTVAPT GAPSPGPTGP PTAGPSEAPT ESSTPVDNPC NVDVFDAIAD IQGALHFFKD GRYWKFSNHG GSQLQGPFLI ARTWPALPAK LNSAFEDPQS KKIFFFSGRK MWVYTGQTVL GPRSLDKLGL GSEVTLVTGL LPRRGGKALL ISRERIWKFD LKSQKVDPQS VTRLDNEFSG VPWNSHNVFH YQDKAYFCHD KYFWRVSFHN RVNQVDHVAY VTYDLLQCPH HHHHH.

    • Background

      Matrix metalloproteinase-9 (MMP-9) is a key member of the matrix metalloproteinase family involved in the remodeling of the extracellular matrix (ECM). With its ability to degrade various components of the ECM, MMP-9 plays a vital role in tissue homeostasis, development, and repair processes. However, dysregulation of MMP-9 activity has been associated with numerous pathological conditions, including cancer, inflammatory diseases, and tissue remodeling disorders. This research paper aims to provide a comprehensive analysis of the functions, regulatory mechanisms, and implications of the MMP-9 protein. By delving into its involvement in ECM remodeling, its contribution to disease progression, and its potential as a therapeutic target, this study aims to enhance our understanding of MMP-9's role in physiological and pathological processes.

      Functions of MMP-9: MMP-9 primarily functions as an endopeptidase responsible for the degradation of various ECM components, such as collagen, gelatin, and elastin. Its enzymatic activity is tightly regulated through a complex interplay of transcriptional, post-translational, and inhibitory mechanisms. Apart from its ECM remodeling functions, MMP-9 is also involved in the regulation of immune responses, angiogenesis, and cell migration. Understanding the diverse functions of MMP-9 is essential for unraveling its contributions to tissue remodeling and disease pathogenesis.

      Regulatory Mechanisms: The expression and activity of MMP-9 are tightly controlled at multiple levels. Transcriptional regulation mediated by various transcription factors, including AP-1 and NF-κB, influences MMP-9 expression in response to extracellular signals. Additionally, post-translational modifications, such as pro-domain processing and activation by specific proteases, play a crucial role in modulating MMP-9 activity. Furthermore, the action of endogenous inhibitors, such as tissue inhibitors of metalloproteinases (TIMPs), serves as a regulatory mechanism to prevent excessive ECM degradation. Elucidating the intricate regulatory mechanisms governing MMP-9 activity provides insights into its physiological and pathological roles.

      Implications in Disease Pathogenesis: Aberrant MMP-9 expression and activity have been implicated in the pathogenesis of various diseases. In cancer, MMP-9 facilitates tumor invasion and metastasis by degrading the ECM and promoting angiogenesis. Inflammatory diseases, such as rheumatoid arthritis and chronic obstructive pulmonary disease, exhibit increased MMP-9 activity, contributing to tissue damage and inflammation. Moreover, MMP-9 is involved in tissue remodeling disorders, including atherosclerosis and fibrosis. Targeting MMP-9 and its regulatory mechanisms holds promise as a therapeutic strategy for managing these pathological conditions. Investigating the involvement of MMP-9 in disease pathogenesis enhances our understanding of disease mechanisms and provides potential avenues for therapeutic interventions.

      Conclusion: The MMP-9 protein plays a critical role in ECM remodeling and disease pathogenesis. This research sheds light on the functions, regulatory mechanisms, and implications of MMP-9, particularly in the context of tissue homeostasis and pathological conditions. Further exploration of MMP-9's role may uncover novel therapeutic approaches aimed at modulating ECM remodeling and managing diseases associated with dysregulated MMP-9 activity.

      Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on MMP-9 for a comprehensive list of references and sources.

    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.

    Mmp9 Rat
  • View Data Sheet

    Name :

    AHSG Human HEK

    Description:

    Alpha-2-HS-Glycoprotein Human Recombinant HEK

    Alpha-2-HS-glycoprotein, Fetuin-A, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, AHSG, FETUA, AHS, A2HS, HSGA, PRO2743.

    Product # :

    PRO-1644

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    Description

    AHSG Human Recombinant produced by transfected human cells is a single polypeptide chain containing 357 amino acids (19-367). AHSG is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    AHSG was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fetuin is a liver-produced negative acute phase protein composed of two subunits, the A and B chains.
      Fetuin homologs have been identified in several species including rat, sheep, pig, rabbit, guinea pig, cattle, mouse and human. Multiple physiological roles for these homologs have been suggested, including ability to bind to hydroxyapatite crystals and to specifically inhibit the tyrosine kinase (TK) activity of the receptor (IR).
      Fetuin-A (alpha2-Heremans-Schmid glycoprotein; AHSG) is an important circulating inhibitor of calcification in vivo, and is downregulated during the acute-phase response.
      Sera from patients on long-term dialysis with low AHSG concentrations showed impaired ex-vivo capacity to inhibit CaxPO4 precipitation.
      Fetuin may influence the resolution of inflammation by modulating the phagocytosis of apoptotic cells by macrophages.
      ASHG blocks TGF-beta-dependent signaling in osteoblastic cells, and mice lacking ASHG display growth plate defects, increased bone formation with age, and enhanced cytokine-dependent osteogenesis.

    • Synonyms

      Alpha-2-HS-glycoprotein, Fetuin-A, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, AHSG, FETUA, AHS, A2HS, HSGA, PRO2743.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized AHSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AHSG 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 AHSG in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIE
      IDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRK
      VCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTD
      CVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCTVFQTQPVTSQPQPEGANEAVPTP
      VVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSH
      PRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKVVDHHHHHH.

    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.

    Ahsg Human Hek
  • View Data Sheet

    Name :

    MRTO4 Human

    Description:

    mRNA Turnover 4 Human Recombinant

    MRNA Turnover 4 Homolog (S. Cerevisiae), MRT4 MRNA Turnover 4 Homolog (S. Cerevisiae), 60S Acidic Ribosomal Protein PO, Chromosome 1 Open Reading Frame 33, C1orf33, MRT4, DJ657E11.4.

    Product # :

    PRO-1233

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    Description

    MRTO4 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (1-239) and having a molecular mass of 29.9 kDa.MRTO4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MRTO4 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      mRNA turnover protein 4 homolog (MRTO4) is a member of the ribosomal protein L10P family. MRTO4 is a protein sharing a low level of sequence similarity with ribosomal protein P0. Though the precise function of the MRTO4 is presently unknown, it seems to be involved in mRNA turnover and ribosome assembly. MRTO4 is a nucleolar component of the ribosome assembly apparatus which shares remarkable similarity and contends for binding to the 25S rRNA GAR domain with the ribosomal protein P0. The MRTO4 gene is located on human chromosome 1, which extends over 260 million base pairs, is comprised of over 3,000 genes and contains approximately 8% of the human genome.

    • Synonyms

      MRNA Turnover 4 Homolog (S. Cerevisiae), MRT4 MRNA Turnover 4 Homolog (S. Cerevisiae), 60S Acidic Ribosomal Protein PO, Chromosome 1 Open Reading Frame 33, C1orf33, MRT4, DJ657E11.4.

    • 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 MGSMPKSKRD KKVSLTKTAK KGLELKQNLI EELRKCVDTY KYLFIFSVAN MRNSKLKDIR NAWKHSRMFF GKNKVMMVAL GRSPSDEYKD NLHQVSKRLR GEVGLLFTNR TKEEVNEWFT KYTEMDYARA GNKAAFTVSL DPGPLEQFPH SMEPQLRQLG LPTALKRGVV TLLSDYEVCK EGDVLTPEQA RVLKLFGYEM AEFKVTIKYM WDSQSGRFQQ MGDDLPESAS ESTEESDSED DD

    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.

    Mrto4 Human
  • View Data Sheet

    Name :

    AOC1 Human

    Description:

    Amine Oxidase Copper Containing 1 Human Recombinant

    Amiloride-sensitive amine oxidase (copper-containing), DAO, Diamine oxidase, Amiloride-binding protein 1, Amine oxidase copper domain-containing protein 1, Histaminase, Kidney amine oxidase, KAO, ABP, ABP1, DAO1

    Product # :

    PRO-2657

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    Description

    AOC1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-751 a.a) containing a total of 738 amino acids, having a molecular mass of 84.2kDa. AOC1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The AOC1 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Amine Oxidase Copper Containing 1 or AOC1 is n enzyme, part of the copper-containing amine oxidase group of proteins. AOC1 is responsible for oxidation of many different biogenic amines, such as neurotransmitters, xenobiotic amines & histamine. Dietary histamine intolerance and histaminosis can be caused from AOC1 deficiencies. This enzyme can also cause Tumor Progression by AKT & EMT transduction promotion in stomach cancer.

    • Synonyms

      Amiloride-sensitive amine oxidase (copper-containing), DAO, Diamine oxidase, Amiloride-binding protein 1, Amine oxidase copper domain-containing protein 1, Histaminase, Kidney amine oxidase, KAO, ABP, ABP1, DAO1

    • 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

      EPSPGTLPRK AGVFSDLSNQ ELKAVHSFLW SKKELRLQPS STTTMAKNTV FLIEMLLPKK YHVLRFLDKG ERHPVREARA VIFFGDQEHP NVTEFAVGPL PGPCYMRALS PRPGYQSSWA SRPISTAEYA LLYHTLQEAT KPLHQFFLNT TGFSFQDCHD RCLAFTDVAP RGVASGQRRS WLIIQRYVEG YFLHPTGLEL LVDHGSTDAG HWAVEQVWYN GKFYGSPEEL ARKYADGEVD VVVLEDPLPG GKGHDSTEEP PLFSSHKPRG DFPSPIHVSG PRLVQPHGPR FRLEGNAVLY GGWSFAFRLR SSSGLQVLNV HFGGERIAYE VSVQEAVALY GGHTPAGMQT KYLDVGWGLG SVTHELAPGI DCPETATFLD TFHYYDADDP VHYPRALCLF EMPTGVPLRR HFNSNFKGGF NFYAGLKGQV LVLRTTSTVY NYDYIWDFIF YPNGVMEAKM HATGYVHATF YTPEGLRHGT RLHTHLIGNI HTHLVHYRVD LDVAGTKNSF QTLQMKLENI TNPWSPRHRV VQPTLEQTQY SWERQAAFRF KRKLPKYLLF TSPQENPWGH KRTYRLQIHS MADQVLPPGW QEEQAITWAR YPLAVTKYRE SELCSSSIYH QNDPWHPPVV FEQFLHNNEN IENEDLVAWV TVGFLHIPHS EDIPNTATPG NSVGFLLRPF NFFPEDPSLA SRDTVIVWPR DNGPNYVQRW IPEDRDCSMP PPFSYNGTYR PVHHHHHH

    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.

    Aoc1 Human
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