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Search results

1000 results found for “Neurotrophic factors”

Name

Description

Product #

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  • View Data Sheet

    Name :

    HSF2BP Human

    Description:

    Heat Shock Transcription Factor 2 Binding Protein Human Recombinant

    Heat Shock Transcription Factor 2 Binding Protein, Heat Shock Factor 2 Binding Protein, HSF2BP.

    Product # :

    HSP-062

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    HSF2BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 40kDa.HSF2BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HSF2BP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSF2BP, also known as HSF2 binding protein links with HSF2. This interaction takes place between the trimerization domain of HSF2 and the amino terminal hydrophilic region of HSF2BP which contains two leucine zipper motifs. Therefore, HSF2BP is involved in modulating HSF2 activation.

    • Synonyms

      Heat Shock Transcription Factor 2 Binding Protein, Heat Shock Factor 2 Binding Protein, HSF2BP.

    • 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 MGSMGEAGAA EEACRHMGTK EEFVKVRKKD LERLTTEVMQ IRDFLPRILN GEVLESFQKL KIVEKNLERK EQELEQLKMD CEHFKARLET VQADNIREKK EKLALRQQLN EAKQQLLQQA EYCTEMGAAA CTLLWGVSSS EEVVKAILGG DKALKFFSIT GQTMESFVKS LDGDVQELDS DESQFVFALA GIVTNVAAIA CGREFLVNSS RVLLDTILQL LGDLKPGQCT KLKVLMLMSL YNVSINLKGL KYISESPGFI PLLWWLLSDP DAEVCLHVLR LVQSVVLEPE VFSKSASEFR SSLPLQRILA MSKSRNPRLQ TAAQELLEDL RTLEHNV.

    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.

    Hsf2Bp Human
  • View Data Sheet

    Name :

    Activin-A Rat

    Description:

    Activin-A Rat Recombinant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-147

    Price :

    Quantity :

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    Shipped at Room temp

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    • description
    • source
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    • More Info

    Description

    Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

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

      Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 26.2 kDa.

      What is the source or expression system of Activin A Protein?
      Ecoli

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

      What is the Biological Activity of Activin A Protein?
      Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.

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

      What is the amino acid sequence of ACTIVIN A Protein?
      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

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

    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.

    Inhba Rat
  • View Data Sheet

    Name :

    DKK3 Human, HEK

    Description:

    Dickkopf-Related Protein 3 Human Recombinant, HEK

    Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    Product # :

    PRO-1638

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    DKK3 Human Recombinant is a single polypeptide chain containing 337 amino acids (22-350). DKK3 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    DKK3 was lyophilized from a 0.2µM filtered solution of 20mM PB and 150mM NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.

    • Synonyms

      Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized DKK3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DKK3 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 DKK3 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAA
      KASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNNQTGQMVFSETVITSVG
      DEEGRRSHECIIDEDCGPSMYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHC
      TKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLIT
      WELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREVPDEYEVG
      SFMEEVRQELEDLERSLTEEMALGEPAAAAAALLGGEEIVDHHHHHH.

    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.

    Dkk3 Human Hek
  • View Data Sheet

    Name :

    NDUFS4 Human

    Description:

    Histidine NADH Dehydrogenase Fe-S Protein 4 Human Recombinant

    AQDQ, NDUFS4, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 mitochondrial, NADH-ubiquinone oxidoreductase 18 kDa subunit, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ.

    Product # :

    ENZ-421

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
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    • formulation
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    • More Info

    Description

    NDUFS4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (43-175 a.a.) and having a molecular mass of 15.5 kDa.The NDUFS4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFS4 solution contains 20mM Tris pH-8 & 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NDUFS4 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), the primary multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I is involved in cellular ATP production, the main source of energy for numerous vital processes in living cells. NDUFS4 removes electrons from NADH and passes them by a series of diverse protein-coupled redox centers to the electron acceptor ubiquinone. NDUFS4 presents a hotspot of mutations in the genetic apparatus of oxidative phosphorylation and the correct assembly of the subunit it encodes is essential for completion of the assembly of complex I.

    • Synonyms

      AQDQ, NDUFS4, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 mitochondrial, NADH-ubiquinone oxidoreductase 18 kDa subunit, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MAQDQTQDTQ LITVDEKLDI TTLTGVPEEH IKTRKVRIFV PARNNMQSGV NNTKKWKMEF DTRERWENPL MGWASTADPL SNMVLTFSTK EDAVSFAEKN GWSYDIEERK VPKPKSKSYG ANFSWNKRTR VSTK.

    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.

    Ndufs4 Human
  • View Data Sheet

    Name :

    NDUFV3 Human

    Description:

    NADH Dehydrogenase Flavoprotein 3 Human Recombinant

    NADH Dehydrogenase (Ubiquinone) Flavoprotein 3 10kDa, Renal Carcinoma Antigen NY-REN-4, NADH-Ubiquinone Oxidoreductase 9 KDa Subunit, EC 1.6.5.311, CI-10k, Complex I 10kDa

    Product # :

    ENZ-749

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    Description

    NDUFV3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (35-108) and having a molecular mass of 10.8kDa.NDUFV3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFV3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NDUFV3 is one of no less than 41 subunits which form the NADH-ubiquinone oxidoreductase complex that is involved in the mitochondrial respiratory chain and assists in catalyzing the rotenone-sensitive oxidation of NADH and the reduction of ubiquinone. NDUFV3 is 1 of 3 proteins found in the flavoprotein fraction of the complex but it exact function is unknown. Two transcript variants encoding altered isoforms are known for this gene.

    • Synonyms

      NADH Dehydrogenase (Ubiquinone) Flavoprotein 3 10kDa, Renal Carcinoma Antigen NY-REN-4, NADH-Ubiquinone Oxidoreductase 9 KDa Subunit, EC 1.6.5.311, CI-10k, Complex I 10kDa

    • 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 MGSSAESGKS EKGQPQNSKK QSPPKKPAPV PAEPFDNTTY KNLQHHDYST YTFLDLNLEL SKFRMPQPSS GRESPRH

    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.

    Ndufv3 Human
  • View Data Sheet

    Name :

    SNCA Mouse

    Description:

    Alpha-Synuclein Mouse Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, α-Synuclein, SNCA, Syn, SNCA.

    Product # :

    PRO-858

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    Description

    SNCA Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 14.4 kDa. The SNCA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA protein contains 20mM Tris-HCl buffer (pH 7.5) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, α-Synuclein, SNCA, Syn, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGNIAA ATGFVKKDQM GKGEEGYPQE GILEDMPVDP GSEAYEMPSE EGYQDYEPEA.

    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.

    Snca Mouse
  • View Data Sheet

    Name :

    NUDCD2 Human

    Description:

    NudC Domain Containing 2 Human Recombinant

    NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 2.

    Product # :

    PRO-1881

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    Description

    NUDCD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-157 a.a) and having a molecular mass of 20kDa.NUDCD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUDCD2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NudC Domain Containing 2 also known as NUDCD2 contains 1 CS domain and interacts with LIS1. NUDCD2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone.

    • Synonyms

      NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAPFEE RSGVVPCGTP WGQWYQTLEE VFIEVQVPPG TRAQDIQCGL QSRHVALSVG GREILKGKLF DSTIADEGTW TLEDRKMVRI VLTKTKRDAA NCWTSLLESE YAADPWVQDQ MQRKLTLERF QKENPGFDFS GAEISGNYTK GGPDFSNLEK

    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.

    Nudcd2 Human
  • View Data Sheet

    Name :

    CXCL5 Rat

    Description:

    Epithelial Neutrophil-Activating Protein 78 Rat Recombinant (CXCL5)

    C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

    Product # :

    CHM-267

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    Description

    Epithelial Neutrophil-Activating Protein 78 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 10.0kDa.The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.

    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 human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

    • Synonyms

      C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA-78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

    • Background

      What is the molecular weight/Mw of CXCL5 RAT Protein?
      CXCL5 RAT Protein has a total Mw of 10.0kDa.

      What is the source or expression system of CXCL5 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 RAT Protein?
      CXCL5 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 RAT Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CXCL5 RAT Protein?
      APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

      What applications can CXCL5 RAT Protein be used in?
      CXCL5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 RAT Protein?
      The endotoxin level is minimal, CXCL5 RAT 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.

    Ena 78 Rat
  • View Data Sheet

    Name :

    ETFB Human

    Description:

    Electron-Transfer-Flavoprotein Beta Polypeptide Human Recombinant

    Electron-transfer-flavoprotein beta polypeptide, MADD, beta-ETF.

    Product # :

    PRO-220

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    Description

    ETFB Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 275 amino acids (1-255a.a.) and having a molecular mass of 30.0kDa. The ETFB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ETFB solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ETF is a heterodimer composed of alpha and beta subunit. ETFB protein is electron-transfer-flavoprotein, beta polypeptide that transports electrons between primary flavoprotein dehydrogenases involved in mitochondrial fatty acid and amino acid catabolism and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase.

    • Synonyms

      Electron-transfer-flavoprotein beta polypeptide, MADD, beta-ETF.

    • 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 MAELRVLVAV KRVIDYAVKI RVKPDRTGVV TDGVKHSMNP FCEIAVEEAV RLKEKKLVKE VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPPAEAERLG PLQVARVLAK LAEKEKVDLV LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA SQVTLEGDKL
      KVEREIDGGL ETLRLKLPAV VTADLRLNEP RYATLPNIMK AKKKKIEVIK PGDLGVDLTS KLSVISVEDP PQRTAGVKVE TTEDLVAKLK EIGRI.

    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.

    Etfb Human
  • View Data Sheet

    Name :

    PARK7 Human

    Description:

    Parkinson Disease Protein 7 Human Recombinant

    Protein DJ-1, Oncogene DJ1, Parkinson disease protein 7, PARK7, DJ1, DJ-1, FLJ27376.

    Product # :

    PRO-575

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    Description

    PARK7 Human Recombinant fused to an N-terminal 36 aa His-Tag, produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 1-189) containing 225 amino acids and having a molecular mass of 24 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).

    • Synonyms

      Protein DJ-1, Oncogene DJ1, Parkinson disease protein 7, PARK7, DJ1, DJ-1, FLJ27376.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASK RALVILAKGA EEMETVIPVD VMRRAGIKVT VAGLAGKDPV QCSRDVVICP DASLEDAKKE GPYDVVVLPG GNLGAQNLSE SAAVKEILKE QENRKGLIAA ICAGPTALLA HEIGFGSKVT THPLAKDKMM NGGHYTYSEN RVEKDGLILT SRGPGTSFEF ALAIVEALNG KEVAAQVKAP LVLKD.

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    Park7 Human
  • View Data Sheet

    Name :

    C12ORF5 Human, His

    Description:

    Chromosome 12 Open Reading Frame 5 Human Recombinant, His Tag

    Probable fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    Product # :

    PRO-051

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    Description

    C12ORF5 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids (1-270 a.a.) and having a molecular mass of 32.6kDa. The C12ORF5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C12ORF5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TP53-induced glycolysis and apoptosis regulator (TIGAR or C12ORF5), is a 270 amino acid protein induced by the p53 tumor suppressor pathway that functions to protect against oxidative stress. C12ORF5 specifically functions to block glycolysis, leading the pathway to the pentose phosphate shunt and decreasing the intracellular concentration of reactive oxygen species. Therefore, it is thought that C12ORF5 may act to modulate the apoptotic response to p53, thus allowing cells to survive mild or transient stresses.

    • Synonyms

      Probable fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    • 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 MGSHMARFAL TVVRHGETRF NKEKIIQGQG VDEPLSETGF KQAAAAGIFL NNVKFTHAFS SDLMRTKQTM HGILERSKFC KDMTVKYDSR LRERKYGVVE GKALSELRAM AKAAREECPV FTPPGGETLD QVKMRGIDFF EFLCQLILKE ADQKEQFSQG SPSNCLETSL AEIFPLGKNH SSKVNSDSGI PGLAASVLVV SHGAYMRSLF DYFLTDLKCS LPATLSRSEL MSVTPNTGMS LFIINFEEGR EVKPTVQCIC MNLQDHLNGL TETR.

    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.

    C12Orf5 Human
  • View Data Sheet

    Name :

    CX3CL1 Human

    Description:

    Fractalkine Human Recombinant (CX3CL1)

    Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    Product # :

    CHM-235

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    Description

    Fractalkine Human Recombinant- produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8638 Dalton. The Fractalkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CX3CL1 was lyophilized from a 0.2μm filtered concentrated (1.0 mg/ml) solution in 20mM Phosphate buffer, pH 7.4, 50mM NaCl.

    Purity

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

    Biological Activity

    The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CX3CL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CX3CL1 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 CX3CL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN Protein?
      CX3CL1 HUMAN Protein has a total Mw of 8.63kDa.

      What is the source or expression system of CX3CL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CX3CL1 HUMAN Protein?
      CX3CL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN Protein?
      The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

      What is the amino acid sequence of CX3CL1 HUMAN Protein?
      QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.

      What applications can CX3CL1 HUMAN Protein be used in?
      CX3CL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN Protein?
      The endotoxin level is minimal, CX3CL1 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.

    Fractalkine Human
  • View Data Sheet

    Name :

    TREM2 Human

    Description:

    Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    Product # :

    PRO-1794

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    Description

    TREM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (19-161 a.a) and having a molecular mass of 20.4kDa.TREM2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TREM2 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMHN TTVFQGVAGQ SLQVSCPYDS MKHWGRRKAW CRQLGEKGPC QRVVSTHNLW LLSFLRRWNG STAITDDTLG GTLTITLRNL QPHDAGLYQC QSLHGSEADT LRKVLVEVLA DPLDHRDAGD LWFPGESESF EDAHVEHSIS R.

    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.

    Trem2 Human
  • View Data Sheet

    Name :

    VAMP2 Human

    Description:

    Synaptobrevin-2 Human Recombinant

    Vesicle-associated membrane protein 2, SYB2, VAMP-2, Synaptobrevin-2, VAMP2, FLJ11460.

    Product # :

    PRO-578

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    Description

    VAMP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (1-89) and having a molecular mass of 13.8 kDa. The VAMP contains 37 amino acids His-Tag fused at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 1X PBS pH 7.4 and 1mM EDTA.

    Purity

    Greater than 95.0% as dtermined by SDS-PAGE.

    More Info

    • Introduction

      Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

    • Synonyms

      Vesicle-associated membrane protein 2, SYB2, VAMP-2, Synaptobrevin-2, VAMP2, FLJ11460.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA TAATAPPAAP AGEGGPPAPP PNLTSNRRLQ QTQAQVDEVV DIMRVNVDKV LERDQKLSEL DDRADALQAG ASQFETSAAK LKRKYW.

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    Vamp2 Human
  • View Data Sheet

    Name :

    IL 10 Human, His

    Description:

    Interleukin-10 Human Recombinant, His

    B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

    Product # :

    CYT-486

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    Description

    Interleukin-10 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 181 amino acids fragment (19-178) and having a total molecular mass of 20.94kDa with a 20 amino acids N-Terminal His tag. The IL-10 His-Tag protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-10 His is supplied in 20mM Tris-HCl pH-8 and 20% glycerol.

    Purity

    Greater than 95.0% by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-10 is a multifunctional cytokine produced by a variety of cell types including T helper cells activated B cells and activated macrophages. Interleukin-10 regulates immune-mediated inflammation and modulates the function of cells such as lymphocytes, monocytes, natural killer cells and dendritic cells.

    • Synonyms

      B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

    • 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

      MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.

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    Il 10 Human His
  • View Data Sheet

    Name :

    Leptin Receptor Chicken

    Description:

    Leptin Receptor Chicken Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    Product # :

    CYT-509

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    Description

    Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    • Physical Appearance

      Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.

    • Stability

      Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 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 calibrated solution of Leptin Binding Domain as a Reference Standard.

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    Leptin Receptor Chicken
  • View Data Sheet

    Name :

    OPG Mouse

    Description:

    Osteoprotegerin Mouse Recombinant

    Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.

    Product # :

    CYT-956

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    Description

    OPG Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 388 amino acids (22-401a.a.) and having a molecular mass of 44.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).OPG is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.

    • 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

      ETLPPKYLHY DPETGHQLLC DKCAPGTYLK QHCTVRRKTL CVPCPDHSYT DSWHTSDECV YCSPVCKELQ SVKQECNRTH NRVCECEEGR YLEIEFCLKH RSCPPGSGVV QAGTPERNTV CKKCPDGFFS GETSSKAPCI KHTNCSTFGL LLIQKGNATH DNVCSGNREA TQKCGIDVTL CEEAFFRFAV PTKIIPNWLS VLVDSLPGTK VNAESVERIK RRHSSQEQTF QLLKLWKHQN RDQEMVKKII QDIDLCESSV QRHLGHSNLT TEQLLALMES LPGKKISPEE IERTRKTCKS SEQLLKLLSL WRIKNGDQDT LKGLMYALKH LKTSHFPKTV THSLRKTMRF LHSFTMYRLY QKLFLEMIGN QVQSVKISCL LEHHHHHH.

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    Opg Mouse
  • View Data Sheet

    Name :

    IGF2 Human

    Description:

    IGF-2 Human Recombinant

    Somatomedin-A, IGF2, INSIGF, pp9974, C11orf43, FLJ22066, FLJ44734.

    Product # :

    CYT-265

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    Description

    Insulin-Like Growth Factor- II Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids and having a molecular mass of 7.5k Dalton. IGF-II is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the dose dependent proliferation of FDC-P1 cells and is typically 8.39ng/mL corresponding to a specific activity of 1.2x105units/mg..

    More Info

    • Introduction

      IGF-2 is a member of the INS family of polypeptide growth factors that is involved in development and growth. It is an imprinted gene and is expressed only from the paternally inherited allele. It is a candidate gene for eating disorders. There is a read-through, INS-IGF2, which aligns to this gene at the 3' region and to the upstream INS gene at the 5' region. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Somatomedin-A, IGF2, INSIGF, pp9974, C11orf43, FLJ22066, FLJ44734.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGF-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFII 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 IGF2 in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AYRPSETLCG GELVDTLQFV CGDRGFYFSR PASRVSRRSR GIVEECCFRS CDLALLETYC ATPAKSE.

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    Igf Ii Human
  • View Data Sheet

    Name :

    PHF11 Human

    Description:

    PHF11 Protein Human Recombinant

    PHD finger protein 11, BRCA1 C-terminus-associated protein, Renal carcinoma antigen NY-REN-34, PHF11, BCAP, APY, IGEL, IGER, IGHER, NYREN34, NY-REN-34, RP11-185C18.3.

    Product # :

    PRO-1268

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    Description

    PHF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (1-331 a.a.) and having a molecular mass of 39.7kDa.PHF11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PHF11 protein 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

      PHD finger protein 11 (PHF11) is a regulator of TH1-type cytokine gene expression. The decline in PHF11 expression observed with an AD-associated genotype may promote the intense TH2 reactions which characterize numerous allergic individuals. PHF11 is linked with raised total serum IgE levels, asthma and acute atopic dermatitis (AD) in children. Even though PHF11 includes a plant homeodomain, a motif frequently found in transcriptional regulators, PHF11 function of has yet been examined.

    • Synonyms

      PHD finger protein 11, BRCA1 C-terminus-associated protein, Renal carcinoma antigen NY-REN-34, PHF11, BCAP, APY, IGEL, IGER, IGHER, NYREN34, NY-REN-34, RP11-185C18.3.

    • 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).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAQASPPRPE RVLGASSPEA RPAQEALLLP TGVFQVAEKM EKRTCALCPK DVEYNVLYFA QSENIAAHEN CLLYSSGLVE CEDQDPLNPD RSFDVESVKK EIQRGRKLKC KFCHKRGATV GCDLKNCNKN YHFFCAKKDD AVPQSDGVRG IYKLLCQQHA QFPIIAQSAK FSGVKRKRGR KKPLSGNHVQ PPETMKCNTF IRQVKEEHGR HTDATVKVPF LKKCKEAGLL NYLLEEILDK VHSIPEKLMD ETTSESDYEE IGSALFDCRL FEDTFVNFQA AIEKKIHASQ QRWQQLKEEI ELLQDLKQTL CSFQENRDLM SSSTSISSLS Y.

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    Phf11 Human
  • View Data Sheet

    Name :

    COMT Human

    Description:

    Catechol-O-Methyltransferase Human Recombinant

    COMT, EC 2.1.1.6, Catechol O-methyltransferase.

    Product # :

    ENZ-400

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    Description

    COMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (51-271 a.a.) & having a molecular mass of 24.4 kDa. The COMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COMT protein in 20mM Tris-HCl buffer, pH-8, 1mM MgCl2 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol substrates such as the neurotransmitters. This O-methylation results in one of the main degradative pathways of the catecholamine transmitters. COMT COMT is located in the postsynaptic neuron and is involved in the metabolism of catechol estrogen drugs used in the treatment of hypertension, asthma, Parkinson disease and the inactivation of catecholamine neurotransmitters though enzymatic degradation. COMT appears in tissues in 2 forms, a soluble form and a membrane-bound form which differ in their N-termini. COMT inhibitors increase its availability and are used in the treatment of patients with Parkinson's disease.

    • Synonyms

      COMT, EC 2.1.1.6, Catechol O-methyltransferase.

    • 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

      MGDTKEQRIL NHVLQHAEPG NAQSVLEAID TYCEQKEWAM NVGDKKGKIV DAVIQEHQPS VLLELGAYCG YSAVRMARLL SPGARLITIE INPDCAAITQ RMVDFAGVKD KVTLVVGASQ DIIPQLKKKY DVDTLDMVFL DHWKDRYLPD TLLLEECGLL RKGTVLLADN VICPGAPDFL AHVRGSSCFE CTHYQSFLEY REVVDGLEKA IYKGPGSEAG P.

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    Comt Human
  • View Data Sheet

    Name :

    KLF7 (80-230) Human

    Description:

    Kruppel-Like Factor 7 (80-230) Human Recombinant

    UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.

    Product # :

    PRO-2824

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    Description

    The KLF7 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The KLF7 His-Tagged Fusion Protein, produced in E. coli, is a 22kDa protein containing 126 amino acid residues of the KLF7 Human, 80-230 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      UKLF, Krueppel-like factor 7, Ubiquitous krueppel-like factor, KLF7.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized KLF7 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      Kruppel-Like Factor 7 (KLF7) which is a part of the KLF family, plays an important roles in many biological processes, including cellular proliferation, differentiation and apoptosis.

      KLF7 functions as a transcription factor, binding to specific DNA sequences to regulate gene expression.

      KLF7 takes part in the regulation of metabolic pathways, including glucose homeostasis. KLF7 modulates insulin sensitivity and plays a role in adipocyte differentiation.

      KLF7 contributes to the progression of type 2 diabetes by inhibiting hormone expression and secretion in pancreatic beta-cells and also by deregulating adipocytokine secretion in adipocytes.

      KLF7 is critical in the development and maturation of neurons. KLF7 promotes the differentiation of neural progenitor cells and influences axon growth and synaptic plasticity.

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    Klf7 Protein
  • View Data Sheet

    Name :

    Leptin Mouse, PEG

    Description:

    Pegylated Mouse Leptin Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-591

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    Description

    Leptin Mono-Pegylated Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus. Pegylated Mouse Leptin contains PEG 20 kDa at its N-terminus and having a molecular mass of 35.6 kDa as determined by mass spectrometry. Since its enlarged hydrodymanic volume Pegylated Leptin runs on SDS-PAGE as A 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Mouse Leptin half-life in circulation after SC injection was over 20 hours. Mouse Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

    Source

    Escherichia Coli.

    Formulation

    The mouse Leptin was lyophilized from a concentrated (0.65mg/ml) solution containing 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by Gel-Filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated mouse Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated mouse Leptin in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH-8.5 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.

    Leptin Mouse Pegylated
  • View Data Sheet

    Name :

    HSF1 Antibody

    Description:

    Heat Shock Transcription Factor-1, Mouse Anti Human

    HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.

    Product # :

    ANT-328

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    • formulation
    • More Info

    Formulation

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

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    • Introduction

      The transcription of heat-shock genes is rapidly induced after temperature stress in response to environmental changes, and it is also involved in oogenesis, spermatogenesis, and placental development. Hsp90, is a major repressor of HSF1 gene. HSF1 is known for its participation in heat shock response. HSF1 protein regulates the transcription of hundreds of targets, such as genes involved in protein folding, detoxification, energy generation, carbohydrate metabolism, and cell wall organization. HSF1 binds to MTA1 in vitro & in breast carcinoma. Suppression of estrogen-dependent transcription may contribute to role of HSF1 in cancer. Human cancer lines of diverse origins express higher dependence on HSF1 function to maintain proliferation and survival than their non-transformed counterparts. HSF1 induces anticoagulation and relaxation factors in vascular endothelial cells and could therefore be used to treat cardiovascular disease. HSF1 is directly involved in the regulation of HO1 havi

    • Synonyms

      HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.

    • Immunogen

      Anti-human HSF1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSF1 amino acids 1-529 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PJ7F9AT.

    • Applications

      HSF1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000~ 2,000. Recommended starting dilution is 1:1,000.

    • 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

      HSF1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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    Hsf1 Antibody
  • View Data Sheet

    Name :

    FASLG Human

    Description:

    FAS Ligand Human Recombinant

    Tumor necrosis factor ligand superfamily member 6, Apoptosis antigen ligand, APTL, CD95 ligand, CD95-L, Fas antigen ligand, Fas ligand, FasL, CD178, FASLG, APT1LG1, CD95L, TNFSF6, ALPS1B.

    Product # :

    CYT-031

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    • sds-page

    Description

    FASLG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (130-281 a.a.) and having a molecular mass of 19.6kDa.FASLG is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    FASL-sds-page - Product image 1

    More Info

    • Introduction

      The type II transmembrane protein FASLG is a member of the tumor necrosis factor (TNF) superfamily. A fas ligand/receptor interaction has a significant part in the regulation of the immune system and the advancement of cancer. FASLG is expressed on the activated T cell surface as a nondisulfidelinked homotrimer. FASLG binding to Fas/CD95/TNFRSF6 on a nearby cell prompts apoptosis in the Fas expressing cell. FASLG is released from the cell surface by metalloproteinases as a soluble molecule that stays trimeric and is able to bind with Fas, but its capability to activate apoptosis is radically reduced. In addition, FASLG binds to DcR3 - a soluble trap receptor with no signal transduction capabilities. Flawed Fas-mediated apoptosis causes oncogenesis in addition to drug resistance in existing tumors. Constitutive expression of FASLG in a variety of tumors enables their immune evasion. Both mouse and human FASLG are active on mouse and human cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 6, Apoptosis antigen ligand, APTL, CD95 ligand, CD95-L, Fas antigen ligand, Fas ligand, FasL, CD178, FASLG, APT1LG1, CD95L, TNFSF6, ALPS1B.

    • 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 MQIGHPSPPP EKKELRKVAH LTGKSNSRSM PLEWEDTYGI VLLSGVKYKK GGLVINETGL YFVYSKVYFR GQSCNNLPLS HKVYMRNSKY PQDLVMMEGK MMSYCTTGQM WARSSYLGAV FNLTSADHLY VNVSELSLVN FEESQTFFGL YKL.

    • Background

      What is the molecular weight/Mw of FASL Protein?
      FASL Protein has a total Mw of 19.6kDa.

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

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

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

      What is the amino acid sequence of FASL Protein?
      MGSSHHHHHH SSGLVPRGSH MQIGHPSPPP EKKELRKVAH LTGKSNSRSM PLEWEDTYGI VLLSGVKYKK GGLVINETGL YFVYSKVYFR GQSCNNLPLS HKVYMRNSKY PQDLVMMEGK MMSYCTTGQM WARSSYLGAV FNLTSADHLY VNVSELSLVN FEESQTFFGL YKL.

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

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

    Faslg Human
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