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Search results

1000 results found for “Centromere Protein”

Name

Description

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  • View Data Sheet

    Name :

    CXCL9 Human, His

    Description:

    MIG Human Recombinant (CXCL9), His Tag

    C-X-C motif chemokine 9, CMK, crg-10, Humig, MIG, SCYB9, Gamma-interferon-induced monokine, Monokine induced by interferon-gamma, HuMIG, Small-inducible cytokine B9, CXCL9.

    Product # :

    CHM-016

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    Description

    MIG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (23-125 a.a.) and having a molecular mass of 14kDa.MIG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIG protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MIG (CXCL9) is a small cytokine which is part of the CXC chemokine family. MIG, which is also recognized as monokine is induced by gamma interferon. MIG is related to 2 other CXC chemokines named CXCL10 and CXCL11, whose genes are located next to the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 obtain their chemotactic functions by interacting with the chemokine receptor CXCR3.

    • Synonyms

      C-X-C motif chemokine 9, CMK, crg-10, Humig, MIG, SCYB9, Gamma-interferon-induced monokine, Monokine induced by interferon-gamma, HuMIG, Small-inducible cytokine B9, CXCL9.

    • 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 MGSTPVVRKG RCSCISTNQG TIHLQSLKDL KQFAPSPSCE KIEIIATLKN GVQTCLNPDS ADVKELIKKW EKQVSQKKKQ KNGKKHQKKK VLKVRKSQRS RQKKTT.

    • Background

      What is the molecular weight/Mw of CXCL9 HUMAN, HIS Protein?
      CXCL9 HUMAN, HIS Protein has a total Mw of 14kDa.

      What is the source or expression system of CXCL9 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL9 HUMAN, HIS Protein?
      CXCL9 HUMAN, HIS Protein is > 85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL9 HUMAN, HIS Protein?
      The biological functionality of CXCL9 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL9 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSTPVVRKG RCSCISTNQG TIHLQSLKDL KQFAPSPSCE KIEIIATLKN GVQTCLNPDS ADVKELIKKW EKQVSQKKKQ KNGKKHQKKK VLKVRKSQRS RQKKTT.

      What applications can CXCL9 HUMAN, HIS Protein be used in?
      CXCL9 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL9 HUMAN, HIS Protein?
      The endotoxin level is minimal, CXCL9 HUMAN, HIS 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.

    Mig Human His
  • View Data Sheet

    Name :

    LGALS8 Human, His

    Description:

    Galectin-8 Human Recombinant, His Tag

    Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

    Product # :

    CYT-727

    Price :

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    • SDS-PAGE

    Description

    LGALS8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-317 a.a.) and having a molecular mass of 37.9 kDa. The LGALS8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-8 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 10% glycerol & 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.

    SDS-PAGE

    LGALS8 Human, His-SDS-PAGE - Product image 1

    More Info

    • Introduction

      LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.

    • Synonyms

      Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
      KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
      QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
      EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

    • Background

      What is the molecular weight/Mw of LGALS8 HUMAN, HIS Protein?
      LGALS8 HUMAN, HIS Protein has a total Mw of 37.9kDa.

      What is the source or expression system of LGALS8 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of LGALS8 HUMAN, HIS Protein?
      LGALS8 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS8 HUMAN, HIS Protein?
      The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.What is the amino acid
      sequence of LGALS8 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
      KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
      QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
      EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

      What applications can LGALS8 HUMAN, HIS Protein be used in?
      LGALS8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS8 HUMAN, HIS Protein?
      The endotoxin level is minimal, LGALS8 HUMAN, HIS 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.

    Lgals8 Human His
  • View Data Sheet

    Name :

    GIPC1 Human

    Description:

    GIPC PDZ Domain Member 1 Human Recombinant

    PDZ domain-containing protein GIPC1, GAIP C-terminus-interacting protein, RGS-GAIP-interacting protein, RGS19-interacting protein 1, Tax interaction protein 2, TIP-2, GIPC1, C19orf3, GIPC, RGS19IP1, NIP, GIPC, IIP-1, SEMCAP, Hs.6454, MGC3774, GLUT1CBP, MGC15889. SYNECTIN, SYNECTIIN.

    Product # :

    PRO-855

    Price :

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    Description

    GIPC1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-333 a.a) and having a molecular mass of 38.2kDa. The GIPC1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GIPC1 Human solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GIPC1 is a PDZ domain protein that cooperates with RGS-GAIP and the viral oncoprotein TAX, which transactivates viral and cellular promoters throughout interactions with different transcription factors. GIPC1 particularly localizes to clusters of vesicles close to the plasma membrane and takes part in G protein-coupled signaling pathway participating in regulating Clathrin-coated vesicular trafficking. GIPC1 cooperates with membrane bound Semaphorin F, which is takes part in neuronal axon growth, and controls the subcellular distribution of M-SemF in the brain.

    • Synonyms

      PDZ domain-containing protein GIPC1, GAIP C-terminus-interacting protein, RGS-GAIP-interacting protein, RGS19-interacting protein 1, Tax interaction protein 2, TIP-2, GIPC1, C19orf3, GIPC, RGS19IP1, NIP, GIPC, IIP-1, SEMCAP, Hs.6454, MGC3774, GLUT1CBP, MGC15889. SYNECTIN, SYNECTIIN.

    • 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 MPLGLGRRKK APPLVENEEA EPGRGGLGVG EPGPLGGGGS GGPQMGLPPP PPALRPRLVF HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPTAEVMFC TLNTHKVDMD KLLGGQIGLE DFIFAHVKGQ RKEVEVFKSE DALGLTITDN GAGYAFIKRI KEGSVIDHIH LISVGDMIEA INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGRP GSGPQLGTGR GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY.

    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.

    Gipc1 Human
  • View Data Sheet

    Name :

    PROSC Human

    Description:

    Proline Synthetase Co-Transcribed Human Recombinant

    Proline Synthetase Co-Transcribed Homolog (Bacterial), Proline Synthetase Co-Transcribed (Bacterial Homolog), Proline Synthase Co-Transcribed Bacterial Homolog Protein, Proline Synthetase Co-Transcribed Bacterial Homolog Protein, PROSC.

    Product # :

    PRO-481

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    • description
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    Description

    PROSC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275) and having a molecular mass of 32.7 kDa.PROSC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PROSC solution (0.5mg/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

      Proline Synthetase Co-Transcribed (PROSC) is a member of the UPF0001 family.

    • Synonyms

      Proline Synthetase Co-Transcribed Homolog (Bacterial), Proline Synthetase Co-Transcribed (Bacterial Homolog), Proline Synthase Co-Transcribed Bacterial Homolog Protein, Proline Synthetase Co-Transcribed Bacterial Homolog Protein, PROSC.

    • 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 MGSMWRAGSM SAELGVGCAL RAVNERVQQA VARRPRDLPA IQPRLVAVSK TKPADMVIEA YGHGQRTFGE NYVQELLEKA SNPKILSLCP EIKWHFIGHL QKQNVNKLMA VPNLFMLETV DSVKLADKVN SSWQRKGSPE RLKVMVQINT SGEESKHGLP PSETIAIVEH INAKCPNLEF VGLMTIGSFG HDLSQGPNPD FQLLLSLREE LCKKLNIPAD QVELSMGMSA DFQHAVEVGS TNVRIGSTIF GERDYSKKPT PDKCAADVKA PLEVAQEH.

    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.

    Prosc Human
  • View Data Sheet

    Name :

    METRN Mouse

    Description:

    Meteorin Mouse Recombinant

    Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

    Product # :

    PRO-2241

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    Description

    METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.

    • Synonyms

      Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

    • 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

      GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.

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    Metrn Mouse
  • View Data Sheet

    Name :

    DGCR6L Human

    Description:

    DiGeorge Syndrome Critical Region Gene 6-Like Human Recombinant

    Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.

    Product # :

    PRO-1454

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    Description

    DGCR6L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27.3kDa.DGCR6L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DGCR6L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 1mM DTT and 250mM Imidazole.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DiGeorge syndrome critical region 6-like protein (DGCR6L) shares homology with the Drosophila gonadal protein, it is expressed in gonadal tissues and germ cells, and with the human laminin gamma-1 chain which functions in cell attachment and migration. DGCR6L is located in a region of chromosome 22 involved in the DiGeorge syndrome, one aspect of a wider collection of anomalies referred to as the CATCH 22 syndrome. Moreover, it is one of two functional genes encoding nearly identical proteins which have analogous expression patterns.

    • Synonyms

      Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.

    • 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 MGSMERYAAA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVVQA AQQRELEAVE HRIREEQRAM DQKIILELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCRAGNAA LGLGGPWQSP AAQCDQKGSP VPP.

    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.

    Dgcr6L Human
  • View Data Sheet

    Name :

    PGK1 Human

    Description:

    Phosphoglycerate Kinase 1 Human Recombinant

    Phosphoglycerate kinase 1, Primer recognition protein 2, Cell migration-inducing gene 10 protein, PRP 2, PGKA, MIG10, MGC8947, MGC117307, MGC142128, PGK1.

    Product # :

    PKA-351

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    Description

    PGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 437 amino acids (1-417 a.a.) and having a molecular mass of 46.8kDa. PGK1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PGK1 solution containing 20mM Tris (pH 8.0), 10% Glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PGK1 is an X-linked enzyme that has a major role in the glycolytic pathway. PGK1 is a glycolytic enzyme which catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate, generating an ATP molecule. PGK1 may also act as a cofactor for polymerase alpha. Defects in the PGK1 gene are usually associated with chronic hemolytic anemia, though it can be accompanied by either mental retardation or muscular disease (rhabdomyolysis). Overexpression of PGK1 and its signalling targets are possibly an expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination. It was shown that PGK1 is differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.

    • Synonyms

      Phosphoglycerate kinase 1, Primer recognition protein 2, Cell migration-inducing gene 10 protein, PRP 2, PGKA, MIG10, MGC8947, MGC117307, MGC142128, PGK1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      PGK1 although stable at 4°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 MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI.

    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.

    Pgk1 Human
  • View Data Sheet

    Name :

    ACTR3 Human

    Description:

    ARP3 Actin-Related Protein 3 Human Recombinant

    ARP3 Actin-Related Protein 3 Homolog (Yeast), ARP3, Actin-Like Protein 3, ARP3 (Actin-Related Protein 3, Yeast) Homolog, Actin-Related Protein 3.

    Product # :

    PRO-2096

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    Description

    ACTR3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 441 amino acids (1-418 a.a) and having a molecular mass of 49.8kDa. ACTR3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACTR3 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARP3 Actin-Related Protein 3, also known as ACTR3, belongs to the actin family. The specific function of ACTR3 has not been established yet. On the other hand, ACTR3 is identified as being a major constituent of the ARP2/3 complex. In addition, this complex is located at the cell surface and vital to cell shape & motility through lamellipodial actin assembly and protrusion. 3 transcript variants encoding 2 different isoforms have been discovered for ACTR3.

    • Synonyms

      ARP3 Actin-Related Protein 3 Homolog (Yeast), ARP3, Actin-Like Protein 3, ARP3 (Actin-Related Protein 3, Yeast) Homolog, Actin-Related Protein 3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAGRLPA CVVDCGTGYT KLGYAGNTEP QFIIPSCIAI KESAKVGDQA QRRVMKGVDD LDFFIGDEAI EKPTYATKWP IRHGIVEDWD LMERFMEQVI FKYLRAEPED HYFLLTEPPL NTPENREYTA EIMFESFNVP GLYIAVQAVL ALAASWTSRQ VGERTLTGTV IDSGDGVTHV IPVAEGYVIG SCIKHIPIAG RDITYFIQQL LRDREVGIPP EQSLETAKAV KERYSYVCPD LVKEFNKYDT DGSKWIKQYT GINAISKKEF SIDVGYERFL GPEIFFHPEF ANPDFTQPIS EVVDEVIQNC PIDVRRPLYK NIVLSGGSTM FRDFGRRLQR DLKRTVDARL KLSEELSGGR LKPKPIDVQV ITHHMQRYAV WFGGSMLAST PEFYQVCHTK KDYEEIGPSI CRHNPVFGVM S.

    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.

    Actr3 Human
  • View Data Sheet

    Name :

    PRNP Human

    Description:

    Prion Protein Human Recombinant

    ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, Major prion protein, PRNP.

    Product # :

    PRO-1400

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    Description

    PRNP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (23-230a.a) and having a molecular mass of 25kDa. GOSR2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PRNP protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prion protein (PRNP) is a ubiquitous membrane glycoprotein whose abnormal self-replicating, misfolded form is widely believed to cause several central nervous system disorders, together known as Transmissible Spongiform Encephalopathies (TSE). PRNP contains a highly unstable region of five tandem octapeptide repeat. Mutations in PRNP protein’s repeat region as well as elsewhere have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru.

    • Synonyms

      ASCR, CD230, CJD, GSS, MGC26679, prion, PRIP, PrP, PrP27-30, PrP33-35C, PrPc, Major prion protein, PRNP.

    • 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 MKKRPKPGGW NTGGSRYPGQ GSPGGNRYPP QGGGGWGQPH GGGWGQPHGG GWGQPHGGGW GQPHGGGWGQ GGGTHSQWNK PSKPKTNMKH MAGAAAAGAV VGGLGGYVLG SAMSRPIIHF GSDYEDRYYR ENMHRYPNQV YYRPMDEYSN QNNFVHDCVN ITIKQHTVTT TTKGENFTET DVKMMERVVE QMCITQYERE SQAYYQRGS.

    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.

    Prnp Human
  • View Data Sheet

    Name :

    LIN28B Human

    Description:

    LIN28B Human Recombinant

    Lin-28 Homolog B (C. Elegans), Protein Lin-28 Homolog B, CSDD2, Lin-28B, Lin-28.2, FLJ16517.

    Product # :

    PRO-1249

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    Description

    LIN28B Human Recombinant produced in E. coli is a single polypeptide chain containing 273 amino acids (1-250) and having a molecular mass of 29.5 kDa. LIN28B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The LIN28B solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lin28B is a member of the lin-28 family. LIN28 protein is a microRNA-binding protein that binds to and enhances the translation of the IGF-2 mRNA. Lin28B acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. LIN28 is highly expressed in testis, fetal liver, placenta, and in primary human tumors and cancer cell lines.

    • Synonyms

      Lin-28 Homolog B (C. Elegans), Protein Lin-28 Homolog B, CSDD2, Lin-28B, Lin-28.2, FLJ16517.

    • 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 MGSMAEGGAS KGGGEEPGKL PEPAEEESQV LRGTGHCKWF NVRMGFGFIS MINREGSPLD IPVDVFVHQS KLFMEGFRSL KEGEPVEFTF KKSSKGLESI RVTGPGGSPC LGSERRPKGK TLQKRKPKGD RCYNCGGLDH HAKECSLPPQ PKKCHYCQSI MHMVANCPHK NVAQPPASSQ GRQEAESQPC TSTLPREVGG GHGCTSPPFP QEARAEISER SGRSPQEASS TKSSIAPEEQ SKKGPSVQKR KKT.

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    Lin28B Human
  • View Data Sheet

    Name :

    FHL3 Human

    Description:

    Four And A Half LIM Domains 3 Human Recombinant

    Four And A Half LIM Domains 3, SLIM2, Skeletal Muscle LIM-Protein 2, FHL-3, SLIM-2, Four And A Half LIM Domains Protein 3, LIM-Only Protein FHL3.

    Product # :

    PRO-1757

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    Description

    FHL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 33.6kDa. FHL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FHL3 protein solution (1mg/ml) containing 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

      Four and a half LIM domains 3 (FHL3) belongs to a family of proteins containing a four-and-a-half LIM domain, which is a highly conserved double zinc finger motif. FHL3 has been shown to interact with the cancer developmental regulators SMAD2, SMAD3, and SMAD4, the skeletal muscle myogenesis protein MyoD, and the high-affinity IgE beta chain regulator MZF-1. FHL3 is involved in tumor suppression, repression of MyoD expression, and repression of IgE receptor expression. Two transcript variants encoding different isoforms have been found for this gene.

    • Synonyms

      Four And A Half LIM Domains 3, SLIM2, Skeletal Muscle LIM-Protein 2, FHL-3, SLIM-2, Four And A Half LIM Domains Protein 3, LIM-Only Protein FHL3.

    • 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 MGSMSESFDC AKCNESLYGR KYIQTDSGPY CVPCYDNTFA NTCAECQQLI GHDSRELFYE DRHFHEGCFR CCRCQRSLAD EPFTCQDSEL LCNDCYCSAF SSQCSACGET VMPGSRKLEY GGQTWHEHCF LCSGCEQPLG SRSFVPDKGA HYCVPCYENK FAPRCARCSK TLTQGGVTYR DQPWHRECLV CTGCQTPLAG QQFTSRDEDP YCVACFGELF APKCSSCKRP IVGLGGGKYV SFEDRHWHHN CFSCARCSTS LVGQGFVPDG DQVLCQGCSQ AGP.

    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.

    Fhl3 Human
  • View Data Sheet

    Name :

    PAEP Human

    Description:

    Progesterone-Associated Endometrial Protein Human Recombinant

    GD, GdA, GdF, GdS, PAEG, PEP, PP14, Glycodelin, Placental protein 14, Pregnancy-associated endometrial alpha-2 globulin, PEG, Progestagen-associated endometrial protein.

    Product # :

    PRO-1397

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    Description

    PAEP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (19-180a.a) and having a molecular mass of 21kDa. PAEP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PAEP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Progesterone-Associated Endometrial Protein (PAEP) is a member of the kernel lipocalin super family whose members share rather low sequence similarity but have highly conserved exon/intron structure and three-dimensional protein folding. Most lipocalins are clustered on the long arm of chromosome 9. PAEP protein has been previously referred to as pregnancy-associated endometrial alpha-2-globulin, placental protein 14, and glycodelin.

    • Synonyms

      GD, GdA, GdF, GdS, PAEG, PEP, PP14, Glycodelin, Placental protein 14, Pregnancy-associated endometrial alpha-2 globulin, PEG, Progestagen-associated endometrial protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDIPQTK QDLELPKLAG TWHSMAMATN NISLMATLKA PLRVHITSLL PTPEDNLEIV LHRWENNSCV EKKVLGEKTE NPKKFKINYT VANEATLLDT DYDNFLFLCL QDTTTPIQSM MCQYLARVLV EDDEIMQGFI RAFRPLPRHL WYLLDLKQME EPCRF.

    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.

    Paep Human
  • View Data Sheet

    Name :

    CALML5 Human

    Description:

    Calmodulin Like 5 Human Recombinant

    CLSP, Calmodulin-like skin protein, CALML5, Calmodulin-like protein 5. 

    Product # :

    PRO-2475

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    Description

    CALML5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-146) containing 155 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 17.0kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    CALML5 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calmodulin Like 5, also known as CALML5 is a part of the calmodulin family of calcium binding proteins. CALML5 undergoes a conformational change as a result of binding calcium. CALML5 is taking part in terminal differentiation of keratinocytes and encodes a calcium binding protein expressed in the epidermis.

    • Synonyms

      CLSP, Calmodulin-like skin protein, CALML5, Calmodulin-like protein 5.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. CALML5 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS AGELTPEEEA QYKKAFSAVD TDGNGTINAQ ELGAALKATG KNLSEAQLRK LISEVDSDGD GEISFQEFLT AAKKARAGLE DLQVAFRAFD QDGDGHITVD ELRRAMAGLG QPLPQEELDA MIREADVDQD GRVNYEEFAR MLAQE.

    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.

    Calml5 Human
  • View Data Sheet

    Name :

    CCL6 Mouse

    Description:

    C-10 Mouse Recombinant (CCL6)

    Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.

    Product # :

    CHM-307

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    Description

    C-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.7kDa.The CCL6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCL6 Mouse was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    The Biological activity was determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25µg/ml.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 6 (CCL6) is a small cytokine belonging to the CC chemokine family that has only been identified in rodents.
      In mice, CCL6 is expressed in cells from neutrophil and macrophage lineages, and can be greatly induced under conditions suitable for myeloid cell differentiation. It is highly expressed in bone marrow cultures that have been stimulated with the cytokine GM-CSF. Some low levels of gene expression also occur in certain cell lines of myeloid origin (e.g. the immature myeloid cell lines DA3 and 32D cl3, and the macrophage cell line P388D) that can also be greatly induced in culture with GM-CSF. However, in activated T cell lines, expression of CCL6 is greatly reduced. CCL6 can also be induced in the mouse lung by the cytokine interleukin 13. Mouse CCL6 is located on chromosome 11. The cell surface receptor for CCL6 is believed to be the chemokine receptor CCR1.

    • Synonyms

      Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized C10 protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL6 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 C10 protein in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GLIQEIEKED RRYNPPIIHQ GFQDTSSDCC FSYATQIPCK RFIYYFPTSG GCIKPGIIFI SRRGTQVCAD PSDRRVQRCL STLKQGPRSG NKVIA.

    • Background

      What is the molecular weight/Mw of CCL6 MOUSE Protein?
      CCL6 MOUSE Protein has a total Mw of 10.7kDa.

      What is the source or expression system of CCL6 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL6 MOUSE Protein?
      CCL6 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL6 MOUSE Protein?
      The Biological activity was determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25µg/ml.

      What is the amino acid sequence of CCL6 MOUSE Protein?
      GLIQEIEKED RRYNPPIIHQ GFQDTSSDCC FSYATQIPCK RFIYYFPTSG GCIKPGIIFI SRRGTQVCAD PSDRRVQRCL STLKQGPRSG NKVIA.

      What applications can CCL6 MOUSE Protein be used in?
      CCL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL6 MOUSE Protein?
      The endotoxin level is minimal, CCL6 MOUSE 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.

    C 10 Mouse
  • View Data Sheet

    Name :

    PFN4 Human

    Description:

    Profilin-4 Human Recombinant

    PFN-4, Profilin-IV, Profilin4.

    Product # :

    PRO-818

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    Description

    PFN4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-129 a.a.) and having a molecular mass of 16.4 kDa. PFN4 protein is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN4 Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFN4 is a small actin-binding protein that participates in the dynamic turnover and restructuring of the actin cytoskeleton. PFN4 is localized in all eukaryotic organisms in the majority of cells. PFN4 is crucial for spatially and temporally controlled growth of actin microfilaments, which is a necessary process in cellular locomotion and cell shape changes.

    • Synonyms

      PFN-4, Profilin-IV, Profilin4.

    • 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 MSHLQSLLLD TLLGTKHVDS AALIKIQERS LCVASPGFNV TPSDVRTLVN GFAKNPLQAR REGLYFKGKD YRCVRADEYS LYAKNENTGV VVVKTHLYLL VATYTEGMYP SICVEATESL GDYLRKKGS.

    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.

    Pfn4 Human
  • View Data Sheet

    Name :

    ATXN3 Human

    Description:

    Ataxin-3 Human Recombinant

    Ataxin-3, Machado-Joseph disease protein 1, Spinocerebellar ataxia type 3 protein, ATXN3, ATX3, MJD, MJD1, SCA3, AT3, JOS.

    Product # :

    PRO-708

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    Description

    ATXN3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 370 amino acids (1-370 a.a.) and having a molecular mass of 42.4kDa.ATXN3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ATXN3 protein solution contains 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ataxin 3 is otherwise known as Machado-Joseph disease protein 1. Machado–Joseph disease is a hereditary autosomal dominant neurodegenerative disorder. ATXN3 contains trinucleotide CAG repeats in the coding region, and the expansion of these repeats from the normal 13-36 to 68-79 causes the Machado-Joseph disease. ATXN3 is a poly-ubiquitin-binding protein whose cellular turnover is regulated by its catalytic activity.
      In addition, ATXN3 is a proteasome-associated factor which mediates the degradation of ubiquitinated proteins. ATXN3 folds reversibly using a single intermediate; partial destabilization of ATXN3 by chemical denaturation causes the formation of fibrillar aggregates by the non-pathological variant.
      Ataxin-3 interacts with the major histone acetyltransferases cAMP-response-element binding protein (CREB)-binding protein, p300, and p300/CREB-binding protein-associated factor and hinders transcription by these coactivators.

    • Synonyms

      Ataxin-3, Machado-Joseph disease protein 1, Spinocerebellar ataxia type 3 protein, ATXN3, ATX3, MJD, MJD1, SCA3, AT3, JOS.

    • 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

      MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE GGVTSEDYRT FLQQPSGNMD DSGFFSIQVI SNALKVWGLELILFNSPEYQ RLRIDPINER SFICNYKEHW FTVRKLGKQW FNLNSLLTGP ELISDTYLAL FLAQLQQEGY SIFVVKGDLP DCEADQLLQM IRVQQMHRPK LIGEELAQLK EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI DMEDEEADLR RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ QQQQQQQQQQ QQQQGDLSGQ SSHPCERPAT SSGALGSDLG DAMSEEDMLQ AAVTMSLETV RNDLKTEGKK.

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    Atxn3 Human
  • View Data Sheet

    Name :

    RTN4IP1 Human

    Description:

    Reticulon 4 Interacting Protein 1 Human Recombinant

    Reticulon-4-interacting protein 1 mitochondrial, NOGO-interacting mitochondrial protein, RTN4IP1, NIMP.

    Product # :

    PRO-1014

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    Description

    RTN4IP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 379 amino acids (41-396 a.a.) and having a molecular mass of 41.4kDa. RTN4IP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RTN4IP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      RTN4IP1 is a unique mitochondrial protein that interacts with reticulon 4, which is an effective inhibitor of regeneration ensuing spinal cord injury. The reticulon 4 interaction with mitochondrial proteins may offer insight into the mechanisms for reticulon-induced inhibition of neurite growth.

    • Synonyms

      Reticulon-4-interacting protein 1 mitochondrial, NOGO-interacting mitochondrial protein, RTN4IP1, NIMP.

    • 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 MGSTVMPAWV IDKYGKNEVL RFTQNMMMPI IHYPNEVIVK VHAASVNPID VNMRSGYGAT ALNMKRDPLH VKIKGEEFPL TLGRDVSGVV MECGLDVKYF KPGDEVWAAV PPWKQGTLSE FVVVSGNEVS HKPKSLTHTQ AASLPYVALT AWSAINKVGG LNDKNCTGKR VLILGASGGV GTFAIQVMKA WDAHVTAVCS QDASELVRKL GADDVIDYKS GSVEEQLKSL KPFDFILDNV GGSTETWAPD FLKKWSGATY VTLVTPFLLN MDRLGIADGM LQTGVTVGSK ALKHFWKGVH YRWAFFMASG PCLDDIAELV DAGKIRPVIE QTFPFSKVPE AFLKVERGHA RGKTVINVV.

    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.

    Rtn4Ip1 Human
  • View Data Sheet

    Name :

    CNTFR Human

    Description:

    Ciliary Neurotrophic Factor Receptor Human Recombinant

    Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha, Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.

    Product # :

    CYT-883

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    • sds-page

    Description

    CNTFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (23-342 a.a) and having a molecular mass of 38.1kDa. CNTFR is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    CNTF-sds-page - Product image 1

    More Info

    • Introduction

      Ciliary Neurotrophic Factor Receptor, also known as CNTFR is a member of the type I cytokine receptor family. CNTFR binds to CNTF. The alpha subunit provides the receptor specificity. Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.

    • Synonyms

      Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha, Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.

    • Physical Appearance

      Sterile Filtered colorless 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 MQRHSPQEAP HVQYERLGSD VTLPCGTANW DAAVTWRVNG TDLAPDLLNG SQLVLHGLEL GHSGLYACFH RDSWHLRHQV LLHVGLPPRE PVLSCRSNTY PKGFYCSWHL PTPTYIPNTF NVTVLHGSKI MVCEKDPALK NRCHIRYMHL FSTIKYKVSI SVSNALGHNA TAITFDEFTI VKPDPPENVV ARPVPSNPRR LEVTWQTPST WPDPESFPLK FFLRYRPLIL DQWQHVELSD GTAHTITDAY AGKEYIIQVA AKDNEIGTWS DWSVAAHATP WTEEPRHLTT EAQAAETTTS TTSSLAPPPT TKICDPGELG S.

    • Background

      Unveiling the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Insights and Applications

      Abstract:

      The Ciliary Neurotrophic Factor Receptor (CNTFR) holds a crucial role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper discusses the significance of Human Recombinant CNTFR, its production methods, and its potential applications in neurobiology and therapeutic interventions. The review sheds light on the pivotal role of CNTFR in neuroprotection and neuroregeneration research.

      Introduction:

      CNTFR, a transmembrane protein, plays a pivotal role in transmitting CNTF-mediated signals to the cell. The availability of Human Recombinant CNTFR allows researchers to investigate its role in neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's involvement in modulating neuronal health and promoting regeneration makes it an essential component in neurobiology.

      Role in CNTF Signaling:

      CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and initiate downstream signaling pathways. Activation of intracellular signaling cascades, such as JAK/STAT and MAPK, contributes to the neuroprotective and growth-promoting effects of CNTF.

      Production Methods:

      Human Recombinant CNTFR is produced through gene expression in suitable host cells, often employing bacterial or mammalian systems. Ensuring proper folding and post-translational modifications is essential to maintain its functionality and binding affinity for CNTF.

      Therapeutic Applications:

      The availability of Human Recombinant CNTFR offers potential therapeutic applications in neurodegenerative diseases like amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-mediated signaling presents opportunities to enhance neuronal survival and regeneration, ultimately improving patient outcomes.

      Challenges and Future Directions:

      While promising, challenges include optimizing the interaction between CNTFR and CNTF, ensuring efficient delivery to target tissues, and understanding potential off-target effects. Ongoing research is essential to unravel the complete mechanisms of CNTFR-mediated signaling and its implications for therapy.

      Conclusion:

      Human Recombinant Ciliary Neurotrophic Factor Receptor serves as a crucial tool in advancing our understanding of neuroprotection and regeneration. Its potential to modulate CNTF-mediated effects opens avenues for innovative therapeutic strategies targeting neurodegenerative disorders, exemplifying the intersection of molecular biology and clinical application.

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 38.1kDa.

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

      What is the Purity of CNTF Protein?
      CNTF Protein is >85% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CNTF Protein?
      MGSSHHHHHH SSGLVPRGSH MQRHSPQEAP HVQYERLGSD VTLPCGTANW DAAVTWRVNG TDLAPDLLNG SQLVLHGLEL GHSGLYACFH RDSWHLRHQV LLHVGLPPRE PVLSCRSNTY PKGFYCSWHL PTPTYIPNTF NVTVLHGSKI MVCEKDPALK NRCHIRYMHL FSTIKYKVSI SVSNALGHNA TAITFDEFTI VKPDPPENVV ARPVPSNPRR LEVTWQTPST WPDPESFPLK FFLRYRPLIL DQWQHVELSD GTAHTITDAY AGKEYIIQVA AKDNEIGTWS DWSVAAHATP WTEEPRHLTT EAQAAETTTS TTSSLAPPPT TKICDPGELG S.

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

      What is the endotoxin level for CNTF Protein?
      The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography tech

    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.

    Cntfr Human
  • View Data Sheet

    Name :

    SOSTDC1 Human

    Description:

    Sclerostin Domain Containing 1 Human Recombinant

    Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    Product # :

    PRO-426

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    Description

    SOSTDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (24-206 a.a) and having a molecular mass of 23kDa.SOSTDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOSTDC1 protein solution (1mg/ml) containing 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

      Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.

    • Synonyms

      Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    • 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 MGSFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF SNTGLDRNTR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE SMSPAKPVQH HRERKRASKS SKHSMS.

    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.

    Sostdc1 Human
  • View Data Sheet

    Name :

    Clusterin Mouse

    Description:

    Apolipoprotein-J Mouse Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    Product # :

    CYT-1172

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    Description

    Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.

    Source

    HEK293

    Formulation

    Clusterin filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Clusterin also known as Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      Clusterin is up/down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 50.2kDa.

      What is the source or expression system of CLUSTERIN Protein?
      HEK293

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

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

      What is the amino acid sequence of CLUSTERIN Protein?
      EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

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

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

    Clusterin Mouse
  • View Data Sheet

    Name :

    STRADA Human

    Description:

    STE20-Related Kinase Adaptor Alpha Human Recombinant

    LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.

    Product # :

    PRO-1992

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    Description

    STRADA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314a.a) and having a molecular mass of 37kDa. STRADA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STRADA protein solution (1mg/ml) containing 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

      STE20-Related Kinase Adaptor Alpha (STRADA) is a part of the STE- 20 like kinase family which stimulates MAPK pathways by activating MAPKKK. STRADA is an upstream activator of LKB1 and also leads the sub-cellular localization of LKB1 by fixing it in the cytoplasm. The interaction between STRADA-LKB1 leads to phosphorylation of STRADA and enhanced autophosphorylation of LKB1.

    • Synonyms

      LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.

    • 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 MGSMSFLVSK PERIRTNDAS SESIASFSKQ EVMSSFLPEG GCYELLTVIG KGFEDLMTVN LARYKPTGEY VTVRRINLEA CSNEMVTFLQ GELHVSKLFN HPNIVPYRAT FIADNELWVV TSFMAYGSAK DLICTHFMDG MNELAIAYIL QGVLKALDYI HHMGYVHRSV KASHILISVD GKVYLSGLRS NLSMISHGQR QRVVHDFPKY SVKVLPWLSP EVLQQNLQGY DAKSDIYSVG ITACELANGH VPFKDMPATQ MLLEKLNGTV PCLLDTSTIP AEELTMSPSR SVANSGLSDS LTTSTPRPSN GPVPAPS.

    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.

    Strada Human
  • View Data Sheet

    Name :

    TCEAL7 Human

    Description:

    Transcription Elongation Factor A (SII)-Like 7 Human Recombinant

    Transcription elongation factor A (SII)-like 7, TCEA-like protein 7, transcription elongation factor A protein-like 7, MGC23947, MPMGp800C04260Q003.

    Product # :

    PRO-1147

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    Description

    TCEAL7 Human Recombinant produced in E. coli is a single polypeptide chain containing 124 amino acids (1-100) and having a molecular mass of 14.8 kDa.TCEAL7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TCEAL7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription Elongation Factor A (SII)-Like 7 (TCEAL7) has a role in the negative regulation of NF-kappa-B signaling at the basal level by controlling transcriptional activity of NF-kappa-B on its target gene promoters. TCEAL7 links with cyclin D1 promoter containing Myc E-box sequence and transcriptionally inhibits cyclin D1 expression. TCEAL7 regulates telomerase reverse transcriptase expression and telomerase activity in both alternative lengthening of telomeres (ALT) and telomerase-positive cell lines. TCEAL7 is highly expressed in normal and fetal brain tissues, and weakly expressed in the uterus and ovary. TCEAL7 is down-regulated in epithelial ovarian, cervical, prostate, breast, brain and lung cancer cell lines and in the brain and ovarian tumors.

    • Synonyms

      Transcription elongation factor A (SII)-like 7, TCEA-like protein 7, transcription elongation factor A protein-like 7, MGC23947, MPMGp800C04260Q003.

    • 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 MGSHMQKPCK ENEGKPKCSV PKREEKRPYG EFERQQTEGN FRQRLLQSLE EFKEDIDYRH FKDEEMTREG DEMERCLEEI RGLRKKFRAL HSNHRHSRDR PYPI

    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.

    Tceal7 Human
  • View Data Sheet

    Name :

    BMP 7 Human, Plant

    Description:

    Bone Morphogenetic Protein-7 Human Recombinant, Plant

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-039

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    • More Info

    Description

    Bone Morphogenetic Protein-7 Human Recombinant produced in Plant is a monomeric, glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 16.5kDa, and fused to a 6xHis-tag at the N-terminus. The BMP-7 is purified by proprietary chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    BMP-7 was lyophilized from a solution containing Tris-HCl 0.05M buffer at pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of BMP-7 was measured by its ability to induce alkaline phosphatase production by ATDC5 cells, ED50 is less than 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, BMP-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP 7 Human 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

      Lyophilized BMP-7 protein should be reconstituted in distilled water to a concentration of 50 ng/µl.

    • Amino Acid Sequence

      HHHHHHSTGSKQRSQNRSKTPKNQEALRMANVAEN
      SSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAY
      YCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
      CCAPTQLNAISVLYFDDSSVILKKYRNMVVRACGCH.

    • Background

      Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, Plant, Monomer, HEK

      Abstract:

      Welcome to our research paper exploring the incredible world of Bone Morphogenetic Protein-7 Human Recombinant, Plant, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this study, we embark on a captivating journey to unravel the wonders of BMP-7 HR and its significance in cellular differentiation. As a key member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR plays a pivotal role in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells, while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).

      Introduction:

      Step into the fascinating world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its crucial role in guiding cellular differentiation. Meet our trusted companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.

      BMP-7 HR Signaling in HEK Cells:

      Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, paving the way for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.

      Influential Role in Cellular Differentiation:

      BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatility, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.

      Interplay with Key Cytokines:

      Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.

      Therapeutic Implications and Tissue Regeneration:

      The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.

      Conclusion:

      As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR from plant sources opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 16.5kDa.

      What is the source or expression system of BMP7 Protein?
      Escherichia Coli.

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The biological activity of BMP-7 was measured by its ability to induce alkaline phosphatase production by ATDC5 cells, ED50 is less than 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

      What is the amino acid sequence of BMP7 Protein?
      HHHHHHSTGSKQRSQNRSKTPKNQEALRMANVAEN
      SSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAY
      YCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
      CCAPTQLNAISVLYFDDSSVILKKYRNMVVRACGCH.

      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.

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

    Bmp 7 Human Plant
  • View Data Sheet

    Name :

    POU5F1 Human

    Description:

    POU Class 5 Homeobox 1 Human Recombinant

    POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.

    Product # :

    PRO-088

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    Description

    POU5F1 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-265) and having a molecular mass of 32.2 kDa.POU5F1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The POU5F1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.

    • Synonyms

      POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.

    • 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 MHFYRLFLGA TRRFLNPEWK GEIDNWCVYV LTSLLPFKIQ SQDIKALQKE LEQFAKLLKQ KRITLGYTQA DVGLTLGVLF GKVFSQTTIC RFEALQLSFK NMCKLRPLLQ KWVEEADNNE NLQEICKAET LVQARKRKRT SIENRVRGNL ENLFLQCPKP TLQQISHIAQ QLGLEKDVVR VWFCNRRQKG KRSSSDYAQR EDFEAAGSPF SGGPVSFPLA PGPHFGTPGY GSPHFTALYS SVPFPEGEAF PPVSVTTLGS PMHSN.

    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.

    Pou5F1 Human
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