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Search results

1000 results found for “parkinson disease protein”

Name

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  • View Data Sheet

    Name :

    REG1B Human

    Description:

    Regenerating Islet-Derived 1 Beta Human Recombinant

    Lithostathine-1-beta, Regenerating protein I beta, REG1B, REGL.

    Product # :

    PRO-391

    Price :

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    Description

    The Recombinant Human REG 1 beta manufactured with N-terminal fusion of His Tag. The Human REG 1 beta His-Tagged Fusion Protein, produced in E. coli, is 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 beta and 12 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      Lithostathine-1-beta, Regenerating protein I beta, REG1B, REGL.

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

    • Amino Acid Sequence

      MKHHHHHHAS HMQESQTELP NPRISCPEGT NAYRSYCYYF NEDPETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SSTDDSNVWI GLHDPKKNRR WHWSSGSLVS YKSWDTGSPS SANAGYCASL TSCSGFKKWK DESCEKKFSF VCKFKN.

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

    Reg1B Human
  • View Data Sheet

    Name :

    SNAP25 Human, His

    Description:

    Synaptosomal-associated protein 25kDa Human Recombinant, His Tag

    Super-Protein, SUP, RIC4, SEC9, SNAP, RIC-4, SNAP25, SNAP-25, Synaptosomal-associated protein 25, Synaptosomal-associated 25 kDa protein, FLJ23079, bA416N4.2, dJ1068F16.2.

    Product # :

    PRO-573

    Price :

    Quantity :

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    • More Info

    Description

    SNAP25 Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids and having a molecular mass of 25.4 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5, 1mM EDTA, 50mM NaCl and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, SNAP25 product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. The synaptosomal-associated protein (SNAP-25) is an essential component of the core complex that mediates presynaptic vesicle trafficking. Thus, SNAP-25 is directly involved in the release of neurotransmitters.

    • Synonyms

      Super-Protein, SUP, RIC4, SEC9, SNAP, RIC-4, SNAP25, SNAP-25, Synaptosomal-associated protein 25, Synaptosomal-associated 25 kDa protein, FLJ23079, bA416N4.2, dJ1068F16.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR IMEKADSNKT RIDEANQRAT KMLGSG.

    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.

    Snap25 Human
  • View Data Sheet

    Name :

    MANF Human

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant

    Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    Product # :

    CYT-141

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    MANF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids and having a molecular mass of 18.1 kDa. The MANF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4.

    Purity

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

    Biological Activity

    The ED50 was determined by its ability to stimulate the proliferation of rat C6 cells is typically 15-25 µg/ml.

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIENELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDKQ IDLSTVDLKK LRVKELKKIL DDWGETCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.

    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.

    Manf Human Recombinant
  • View Data Sheet

    Name :

    GFRA1 Human

    Description:

    GDNF Family Receptor Alpha 1 Human Recombinant

    GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.

    Product # :

    CYT-1026

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
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    • More Info

    Description

    GFRA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-423) containing 409 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 46.0kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    GFRA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline pH 7.5 containing 5 % (w/v) trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.

    • Synonyms

      GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.

    • 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. GFRA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.

    • Background

      What is the molecular weight/Mw of GFRA1 Protein?
      GFRA1 Protein has a total Mw of 46kDa.

      What is the source or expression system of GFRA1 Protein?
      HEK293 cells.
      What is the Purity of GFRA1 Protein?
      GFRA1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA1 Protein?
      The biological functionality of GFRA1 Protein will be determined in the future.

      What is the amino acid sequence of GFRA1 Protein?
      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.

      What applications can GFRA1 Protein be used in?
      GFRA1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA1 Protein?
      The endotoxin level is minimal, GFRA1 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.

    Gfra1 Human
  • View Data Sheet

    Name :

    DNAJC19 Human

    Description:

    DnaJ (Hsp40) Homolog, Subfamily C, Member 19 Human Recombinant

    Mitochondrial import inner membrane translocase subunit TIM14, DnaJ homolog subfamily C member 19, DNAJC19, TIM14, TIMM14, Pam18.

    Product # :

    HSP-039

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    Description

    DNAJC19 Human Recombinant fused with a 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids (19-116 a.a.) and having a molecular mass of 15.1kDa. The DNAJC19 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DNAJC19 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DNAJC19 is part of a complex involved in the ATP-dependent transport of transit peptide-containing proteins from the inner cell membrane to the mitochondrial matrix. DNAJC19 is a single-pass membrane protein which contains a J domain and is localized to the inner membrane of the mitochondrion. Expressed ubiquitously, DNAJC19 acts as a component of the mitochondrial DNAJC19 complex that is responsible for the ATP-dependent translocation of select proteins from the inner mitochondrial membrane to the mitochondrial matrix. Defects in the DNAJC19 gene are the cause of 3-methylglutaconic aciduria type 5 (MGA5), otherwise known as dilated cardiomyopathy with ataxia (DCMA).

    • Synonyms

      Mitochondrial import inner membrane translocase subunit TIM14, DnaJ homolog subfamily C member 19, DNAJC19, TIM14, TIMM14, Pam18.

    • 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 KDRWGSMGRY VLQAMKHMEP QVKQVFQSLP KSAFSGGYYR GGFEPKMTKR EAALILGVSP TANKGKIRDA HRRIMLLNHP DKGGSPYIAA KINEAKDLLE GQAKK.

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    Dnajc19 Human
  • View Data Sheet

    Name :

    SSBP1 Human, His

    Description:

    Single-Stranded DNA Binding Protein 1 Human Recombinant, His Tag

    Mt-SSB, mtSSB, SOSS-B1, SSBP, PWP1-interacting protein 17, Single-stranded DNA-binding protein, mitochondrial.

    Product # :

    PRO-1408

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    Description

    SSBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (17-148 a.a.) and having a molecular mass of 17kDa.SSBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SSBP1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Single-Stranded DNA Binding Protein 1 (SSBP) participates in mitochondrial biogenesis. SSBP binds preferentially and cooperatively to ss-DNA. The SSBP protein is involved in mitochondrial DNA replication and associates with mitochondrial DNA.

    • Synonyms

      Mt-SSB, mtSSB, SOSS-B1, SSBP, PWP1-interacting protein 17, Single-stranded DNA-binding protein, mitochondrial.

    • 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 MGSESETTTS LVLERSLNRV HLLGRVGQDP VLRQVEGKNP VTIFSLATNE MWRSGDSEVY QLGDVSQKTT WHRISVFRPG LRDVAYQYVK KGSRIYLEGK IDYGEYMDKN NVRRQATTII ADNIIFLSDQ TKEKE.

    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.

    Ssbp1 Human His
  • View Data Sheet

    Name :

    S100A8 Human, His-Myc

    Description:

    S100 Calcium Binding Protein A8, His-Myc Tag Human Recombinant

    S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.

    Product # :

    PRO-2329

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    Description

    S100A8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids (1-93) and having a molecular mass of 14.5kDa. S100A8 is fused to a 24 aa His-tag at N-terminus and to a 10 aa Myc-tag at C-terminus.

    Source

    Escherichia Coli.

    Formulation

    The S100A8 solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.

    • 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 MGSHMLTELE KALNSIIDVY HKYSLIKGNF HAVYRDDLKK LLETECPQYI RKKGADVWFK ELDINTDGAV NFQEFLILVI KMGVAAHKKS HEESHKEEQK LISEEDL.

    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.

    S100A8 His Myc Human
  • View Data Sheet

    Name :

    FABP4 Human, His

    Description:

    Fatty Acid Binding Protein 4 Human Recombinant, His Tag

    Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.

    Product # :

    PRO-566

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    Description

    FABP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 18 kDa. FABP4 is fused to His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP4 His-Tag is supplied in 20mM Tris HCL pH=8, 0.5mM DTT and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
      In mice, targeted mutations in FABP4 provide significant protection from hyperinsulinemia and insulin resistance in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages.

    • Synonyms

      Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

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

    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.

    Fabp4 Human His
  • View Data Sheet

    Name :

    IMPAD1 Human, Active

    Description:

    Inositol Monophosphatase Domain Containing 1 Human Recombinant, BioActive

    Inositol monophosphatase 3, IMP 3, IMPase 3, EC 3.1.3.25, EC 3.1.3.7, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3, IMPAD1, IMPA3, GPAPP, IMP-3

    Product # :

    PRO-2638

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    Description

    IMPAD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (34-359 a.a.) and having a molecular mass of 37.6kDa.IMPAD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IMPAD1 solution (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3300pmol/min/ug, and is defined as its ability to dephosphorylate adenosine 3'5'-diphosphate sodium slat at pH7.5, 25˚C.

    More Info

    • Introduction

      Inositol Monophosphatase Domain Containing 1 or IMPAD1 is a protein, part of the inositol monophosphatase group of proteins. The protein is found in Golgi apparatus and enhances phosphoadenosine phosphate hydrolysis to adenosine monophosphate. When Mutation in the IMPAD1 gene occurs leads to GRAPP type chondrodysplasia and therefore joint dislocations. On long arm chromosome 1 a pseudogene can be found.

    • Synonyms

      Inositol monophosphatase 3, IMP 3, IMPase 3, EC 3.1.3.25, EC 3.1.3.7, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3, IMPAD1, IMPA3, GPAPP, IMP-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 MGSGRFSLFG LGGEPGGGAA GPAAAADGGT VDLREMLAVS VLAAVRGGDE VRRVRESNVL HEKSKGKTRE GAEDKMTSGD VLSNRKMFYL LKTAFPSVQI NTEEHVDAAD QEVILWDHKI PEDILKEVTT PKEVPAESVT VWIDPLDATQ EYTEDLRKYV TTMVCVAVNG KPMLGVIHKP FSEYTAWAMV DGGSNVKARS SYNEKTPRIV VSRSHSGMVK QVALQTFGNQ TTIIPAGGAG YKVLALLDVP DKSQEKADLY IHVTYIKKWD ICAGNAILKA LGGHMTTLSG EEISYTGSDG IEGGLLASIR MNHQALVRKL PDLEKTGHK

    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.

    Impad1 Protein
  • View Data Sheet

    Name :

    FGF 9 Rat

    Description:

    Fibroblast Growth Factor-9 Rat Recombinant

    GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    Product # :

    CYT-558

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    Description

    Rat FGF9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.3kDa.The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF-9 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM NaP, pH-7.5 &, 75mM Ammonium Sulfate.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.

    More Info

    • Introduction

      Rat and mouse FGF-9 show a very high homology to human FGF-9. The transcripts for FGF-9 have been found in brain and in kidney tissue. Fibroblast Growth Factor-9 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling. Mice lacking the homolog gene displayed a male-to-female sex reversal phenotype, which suggested a role in testicular embryogenesis Fibroblast Growth Factor 9 may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.

    • Synonyms

      GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rat Fibroblast Growth Factor-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF9 Rat Recombinant 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 Rat FGF-9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.

    • Background

      What is the molecular weight/Mw of FGF9 Protein?
      FGF9 Protein has a total Mw of 23.3kDa.

      What is the source or expression system of FGF9 Protein?
      Escherichia Coli.

      What is the Purity of FGF9 Protein?
      FGF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF9 Protein?
      The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.

      What is the amino acid sequence of FGF9 Protein?
      MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.

      What applications can FGF9 Protein be used in?
      FGF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF9 Protein?
      The endotoxin level is minimal, FGF9 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.

    Fgf9 Rat
  • View Data Sheet

    Name :

    PEDF Human

    Description:

    Pigment Epithelium-Derived Factor Human Recombinant

    Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    Product # :

    CYT-580

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    Description

    PEDF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 400 amino acids and having a molecular mass of 44.5 kDa. The Human PEDF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated (1mg/ml) protein solution was lyophilized with 20mM sodium phosphate buffer & 150mM NaCl pH-7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.

    • Synonyms

      Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    • Amino Acid Sequence

      MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.

    • Background

      About PEDF Human

      Also known as “Pigment Epithelium-Derived Factor” or “SERPINF1,” PEDF is a
      multifunctional protein found in vertebrates. It has anti-tumorigenic, anti-angiogenic, and
      neurotrophic functions. Currently, it’s being researched as a candidate for treatment for
      several conditions, including heart disease and cancer.

      What’s the Function of PEDF Human Recombinant?

      PEDF is created/secreted in several tissues across the body. It has a unique anti-angiogenic
      action because of its induction of apoptosis in proliferating endothelial cells. Also, PEDF
      can inhibit many angiogenic factors, including VEGF and FGF-2. PEDF-R is currently the
      only known signaling receptor to be used by a serpin family member.


      What’s the Application of PEDF Human Recombinant?

      This version of PEDF is produced in E. Coli. It’s a single, non-glycosylated, polypeptide
      chain that contains 400 amino acids. It has a molecular mass of 44.5 kDa, and it’s purified
      by proprietary chromatographic techniques.

      The main purpose of PEDF human recombinant is for research. It has the potential to
      become a potential treatment for different angiogenesis-related diseases, including
      various cancers. Moreover, it can become crucial during the recovery from vasculature-
      related neurodegenerative illness.

      Such a discovery could be revolutionary for the world, which is why more research is
      needed to determine the effect of this non-inhibitory serpin on the body.

    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.

    Serpinf1 Human
  • View Data Sheet

    Name :

    Transferrin Human

    Description:

    Transferrin Human Recombinant

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

    Product # :

    PRO-747

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    Description

    Recombinant Human Transferrin produced in Plant is a non-glycosylated, polypeptide chain containing 679 amino acids and having a molecular mass of 76 kDa. The Recombinant Human Transferrin is purified by proprietary chromatographic techniques.

    Source

    Oryza sativa (rice).

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Purity as determined by SDS-PAGE is 97%.

    Biological Activity

    One mg of Recombinant Human Transferrin will bind to approximately 2 micrograms of Fe.

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    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

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

      Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 5mg/ml to 20 mg/ml in PBS, though others can be used as well. Please try to avoid the formation of bubbles when dissolving the protein. Sterile filter through 0.2µm filter.

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    Transferrin Human
  • View Data Sheet

    Name :

    MTCP1 Human

    Description:

    Mature T-Cell Proliferation 1 Human Recombinant

    Mature T-Cell Proliferation 1, Mature T-Cell Proliferation-1 Type B1, MTCP-1 Type B1, P13MTCP1, Mature T-Cell Proliferation 1 Isoform P13, p8MTCP1, Protein P13 MTCP-1, C6.1B, p13MTCP1.

    Product # :

    PRO-1748

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    Description

    MTCP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107a.a) and having a molecular mass of 15.0kDa.MTCP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MTCP1 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

      Mature T-Cell Proliferation 1, also known as MTCP1 was recognized by involvement in some t(X;14) translocations linked with mature T-cellproliferations. This region has a complex gene structure, with a common promoter and 5' exon spliced to two dissimilar sets of 3' exons which encode two different proteins. It represents the upstream 13 kDa protein which belongs to the TCL1 family. In addition, MTCP1 enhances the phosphorylation and activation of AKT1 and AKT2. MTCP1 is involved in leukemogenesis.Among the diseases associated with MTCP1 are queensland tick typhus, and african tick-bite fever.

    • Synonyms

      Mature T-Cell Proliferation 1, Mature T-Cell Proliferation-1 Type B1, MTCP-1 Type B1, P13MTCP1, Mature T-Cell Proliferation 1 Isoform P13, p8MTCP1, Protein P13 MTCP-1, C6.1B, p13MTCP1.

    • 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 MGSMAGEDVG APPDHLWVHQ EGIYRDEYQR TWVAVVEEET SFLRARVQQI QVPLGDAARP SHLLTSQLPL MWQLYPEERY MDNNSRLWQI QHHLMVRGVQ ELLLKLLPDD

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    Mtcp1 Human
  • View Data Sheet

    Name :

    JTB Human

    Description:

    Jumping Translocation Breakpoint Human Recombinant

    Protein JTB, Jumping translocation breakpoint protein, Prostate androgen-regulated protein, PAR protein, Jumping Translocation Breakpoint, JTB, Jumping translocation breakpoint, hJT, HJTB, HSPC222, PAR.

    Product # :

    PRO-2059

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    Description

    JTB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (31-105 a.a.) and having a molecular mass of 10.7kDa.JTB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    JTB protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Jumping Translocation Breakpoint (JTB) takes part in the regulation of cell proliferation and is essential for cytokinesis during mitosis. JTB inhibits apoptosis induced by TGFB1 and increases AURKB activity. JTB is also a part of the chromosomal passenger complex (CPC) which is a key regulator of mitosis.

    • Synonyms

      Protein JTB, Jumping translocation breakpoint protein, Prostate androgen-regulated protein, PAR protein, Jumping Translocation Breakpoint, JTB, Jumping translocation breakpoint, hJT, HJTB, HSPC222, PAR.

    • 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 MGSEAPVQEE KLSASTSNLP CWLVEEFVVA EECSPCSNFR AKTTPECGPT GYVEKITCSS SKRNEFKSCR SALMEQRL.

    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.

    Jtb Human
  • View Data Sheet

    Name :

    LDOC1L Human

    Description:

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

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

    Product # :

    PRO-1153

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Ldoc1L Human
  • View Data Sheet

    Name :

    VAPA Human

    Description:

    VAMP Associated Protein A 33kDa Human Recombinant

    hVAP-33, VAP-33, VAP-A, VAP33, Vesicle-associated membrane protein-associated protein A, VAMP-associated protein A, VAMP-A, 33 kDa VAMP-associated protein, VAPA.

    Product # :

    PRO-779

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    Description

    VAPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 264 amino acids (1-227 a.a.) and having a molecular mass of 29.8 kDa. VAPA is fused to 37 amino acid His Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VAPA solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      VAPA is involved in vesicle traficking. VAPA is a type IV membrane protein. It is localized in the plasma membrane and intracellular vesicles. VAPA is related with the cytoskeleton. VAPA functions membrane fusion, protein complex assembly and cell motility. VAPA is an essential regulator both of the subcellular localization of protrudin and of its ability to stimulate neurite outgrowth.

    • Synonyms

      hVAP-33, VAP-33, VAP-A, VAP33, Vesicle-associated membrane protein-associated protein A, VAMP-associated protein A, VAMP-A, 33 kDa VAMP-associated protein, VAPA.

    • 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

      RGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAS ASGAMAKHEQ ILVLDPPTDL KFKGPFTDVV TTNLKLRNPS DRKVCFKVKT TAPRRYCVRP NSGIIDPGST VTVSVMLQPF DYDPNEKSKH KFMVQTIFAP PNTSDMEAVW KEAKPDELMD SKLRCVFEMP NENDKLNDME PSKAVPLNAS KQDGPMPKPH SVSLNDTETR KLMEECKRLQ GEMMKLSEEN RHLRDEGLRL RKVAHSDKPG STSTASFRDN VTSP.

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    Vapa Human
  • View Data Sheet

    Name :

    CHMP6 Human

    Description:

    Charged Multivesicular Body Protein 6 Human Recombinant

    Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6.

    Product # :

    PRO-1085

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    Description

    CHMP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-201 a.a) and having a molecular mass of 26.1kDa (Molecular size on SDS-PAGE will appear higher).CHMP6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHMP6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Charged multivesicular body protein 6 (CHMP6) is a member of the SNF7 family. The CHMP6 protein is a core component of the endosomal sorting necessary for transport complex III (ESCRT-III) that is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) which are produced by invagination and scission from the limiting membrane of the endosome and generally are transported to lysosomes facilitating degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids.

    • Synonyms

      Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6.

    • 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 MGSHMGNLFG RKKQSRVTEQ DKAILQLKQQ RDKLRQYQKR IAQQLERERA LARQLLRDGR KERAKLLLKK KRYQEQLLDR TENQISSLEA MVQSIEFTQI EMKVMEGLQF GNECLNKMHQ VMSIEEVERI LDETQEAVEY QRQIDELLAG SFTQEDEDAI LEELSAITQE QIELPEVPSE PLPEKIPENV PVKARPRQAE LVAAS.

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    Chmp6 Human
  • View Data Sheet

    Name :

    CUEDC1 Human

    Description:

    CUE Domain Containing 1 Human Recombinant

    CUE Domain Containing 1, CUE Domain-Containing Protein 1.

    Product # :

    PRO-1822

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    Description

    CUEDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386 a.a) and having a molecular mass of 44.6kDa.CUEDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CUEDC1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUE Domain Containing 1, also know as CUEDC1 contains 1 CUE domain. The CUE domain is structurally associated to the ubiquitin-binding UBA domain and exists as a domain-swapped dimer which makes additional contacts with ubiquitin, and as a result, binds ubiquitin with higher affinity. The CUE domain is discovered in proteins with diverse functions including protein sorting and degradation of misfolded proteins in the endoplasmic reticulum.

    • Synonyms

      CUE Domain Containing 1, CUE Domain-Containing Protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.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 MGSMTSLFRR SSSGSGGGGT AGARGGGGGT AAPQELNNSR PARQVRRLEF NQAMDDFKTM FPNMDYDIIE CVLRANSGAV DATIDQLLQM NLEGGGSSGG VYEDSSDSED SIPPEILERT LEPDSSDEEP PPVYSPPAYH MHVFDRPYPL APPTPPPRID ALGSGAPTSQ RRYRNWNPPL LGNLPDDFLR ILPQQLDSIQ GNAGGPKPGS GEGCPPAMAG PGPGDQESRW KQYLEDERIA LFLQNEEFMK ELQRNRDFLL ALERDRLKYE SQKSKSSSVA VGNDFGFSSP VPGTGDANPA VSEDALFRDK LKHMGKSTRR KLFELARAFS EKTKMRKSKR KHLLKHQSLG AAASTANLLD DVEGHACDED FRGRRQEAPK VEEGLREGQ

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    Cuedc1 Human
  • View Data Sheet

    Name :

    TRIP10 Human

    Description:

    Thyroid Hormone Receptor Interactor 10 Human Recombinant

    Cdc42-interacting protein 4, Protein Felic, Salt tolerant protein, hSTP, Thyroid receptor-interacting protein 10, TR-interacting protein 10, TRIP-10,TRIP10, CIP4, STOT, STP, HSTP.

    Product # :

    PRO-1811

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    Description

    TRIP10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (260-545) and having a molecular mass of 34.6 kDa.TRIP10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TRIP10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol, 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thyroid Hormone Receptor Interactor 10 (TRIP10) is a part of the F-BAR family of proteins which is expressed in a variety of tissues, including kidney, brain, liver, lung, heart and pancreas. The F-BAR family of proteins contains an N-terminal, alpha-helical, region which is hydrophobic and related to the Bin Amphiphysin Rvs (BAR) protein family. TRIP10 is vital for the coordination of membrane tubulation with Actin cytoskeletal reorganization during endocytosis.

    • Synonyms

      Cdc42-interacting protein 4, Protein Felic, Salt tolerant protein, hSTP, Thyroid receptor-interacting protein 10, TR-interacting protein 10, TRIP-10,TRIP10, CIP4, STOT, STP, HSTP.

    • 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 MGSDPKNDSH VLIELHKSGF ARPGDVEFED FSQPMNRAPS DSSLGTPSDG RPELRGPGRS RTKRWPFGKK NKTVVTEDFS HLPPEQQRKR LQQQLEERSR ELQKEVDQRE ALKKMKDVYE KTPQMGDPAS LEPQIAETLS NIERLKLEVQ KYEAWLAEAE SRVLSNRGDS LSRHARPPDP PASAPPDSSS NSASQDTKES SEEPPSEESQ DTPIYTEFDE DFEEEPTSPI GHCVAIYHFE GSSEGTISMA EGEDLSLMEE DKGDGWTRVR RKEGGEGYVP TSYLRVTLN.

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    Trip10 Human
  • View Data Sheet

    Name :

    GFAP Human

    Description:

    Glial Fibrillary Acidic Protein Human Recombinant

    Glial fibrillary acidic protein, GFAP

    Product # :

    PRO-2802

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    Description

    GFAP Human produced in E.coli is a single, non-glycosylated polypeptide chain (60-383 a.a.) and having a molecular mass of 37906 Dalton.

    Source

    Escherichia Coli.

    Formulation

    GFAP was lyophilized from 50mM Tris-HCl pH-7.5, 4M Urea 150mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Glial fibrillary acidic protein, GFAP

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GFAP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Glial Fibrillary Acidic Protein should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Glial Fibrillary Acidic Protein (GFAP), a key intermediate filament protein predominantly found in astrocytes, plays a fundamental role in the central nervous system. Initially recognized for its structural functions, GFAP has emerged as a multifaceted molecule with implications in neural development, synaptic plasticity, and various neurological disorders. This research delves into the realm of GFAP human recombinant protein, shedding light on its structural properties, physiological significance, and its diverse roles in both health and disease.

      Structural Complexity of GFAP:

      GFAP belongs to the family of intermediate filament proteins, conferring structural support to astrocytes. Its unique structure comprises a central α-helical rod domain flanked by non-helical head and tail domains. This structural complexity allows GFAP to form stable filaments, providing structural integrity to astrocytes and contributing to the architecture of the central nervous system.

      Physiological Functions in Glial Cells:

      Beyond its structural role, GFAP participates in various physiological processes within glial cells. It is involved in the regulation of astrocyte morphology, motility, and migration, crucial for their interactions with neurons and blood vessels. Additionally, GFAP contributes to the formation and maintenance of the blood-brain barrier, highlighting its significance in the brain's homeostasis.

      Implications in Neurological Disorders:

      Aberrant GFAP expression and aggregation are associated with several neurological disorders. In Alexander disease, a rare neurodegenerative disorder, mutations in the GFAP gene lead to the formation of GFAP aggregates, contributing to disease pathology. Moreover, elevated levels of GFAP in cerebrospinal fluid serve as a biomarker for various neurological conditions, including traumatic brain injury, Alzheimer's disease, and multiple sclerosis, indicating its involvement in the brain's response to injury and neuroinflammation.

      GFAP in Neural Regeneration:

      Recent studies have unveiled GFAP’s role in neural regeneration and repair processes. In response to brain injury, GFAP-expressing astrocytes become reactive, forming a glial scar that isolates damaged areas. While this scar formation initially limits tissue damage, persistent scar formation can impede neural regeneration. Understanding the dynamics of GFAP expression in reactive astrocytes is crucial for developing therapies that promote neural regeneration following brain injuries or neurodegenerative diseases.

      GFAP human recombinant protein, once thought of as a structural element in astrocytes, has proven to be a pivotal player in the complex landscape of glial biology and neurological disorders. Its intricate functions extend beyond providing structural support, encompassing roles in neural development, disease pathology, and tissue repair. As research continues to uncover the nuances of GFAP’s involvement in health and disease, it offers promising avenues for developing targeted therapies and diagnostic tools, emphasizing its significance in the intricate workings of the central nervous system.

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    Gfap Human
  • View Data Sheet

    Name :

    AIDA Human

    Description:

    Axin Interactor Dorsalization Associated Human Recombinant

    C1orf80, RP11-378J18.7, Axin interactor, dorsalization-associated protein, Axin interaction partner and dorsalization antagonist, AIDA.

    Product # :

    PRO-1370

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    Description

    AIDA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-306 a.a) and having a molecular mass of 37.4kDa. AIDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    AIDA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.2M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Axin interactor, dorsalization-associated (AIDA) operates as a ventralizing factor during embryogenesis. AIDA inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. That in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling.

    • Synonyms

      C1orf80, RP11-378J18.7, Axin interactor, dorsalization-associated protein, Axin interaction partner and dorsalization antagonist, AIDA.

    • 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 MGSMSEVTRS LLQRWGASFR RGADFDSWGQ LVEAIDEYQI LARHLQKEAQ AQHNNSEFTE EQKKTIGKIA TCLELRSAAL QSTQSQEEFK LEDLKKLEPI LKNILTYNKE FPFDVQPVPL RRILAPGEEE NLEFEEDEEE GGAGAGSPDS FPARVPGTLL PRLPSEPGMT LLTIRIEKIG LKDAGQCIDP YITVSVKDLN GIDLTPVQDT PVASRKEDTY VHFNVDIELQ KHVEKLTKGA AIFFEFKHYK PKKRFTSTKC FAFMEMDEIK PGPIVIELYK KPTDFKRKKL QLLTKKPLYL HLHQTLHKE.

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    Aida Human
  • View Data Sheet

    Name :

    GDF5 Mouse, His

    Description:

    Growth differentiation factor 5 Mouse Recombinant, His Tag

    Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.

    Product # :

    CYT-852

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    • More Info
    • sds-page

    Description

    GDF5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (376-495 a.a) and having a molecular mass of 16kDa.GDF5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    GDF5-sds-page - Product image 1

    More Info

    • Introduction

      GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.

    • Synonyms

      Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.

    • 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 MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.

    • Background

      What is the molecular weight/Mw of GDF5 MOUSE Protein?
      GDF5 MOUSE Protein has a total Mw of 16kDa.

      What is the source or expression system of GDF5 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GDF5 MOUSE Protein?
      GDF5 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF5 MOUSE Protein?
      The biological functionality of GDF5 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of GDF5 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.

      What applications can GDF5 MOUSE Protein be used in?
      GDF5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF5 MOUSE Protein?
      The endotoxin level is minimal, GDF5 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.

    Gdf5 Mouse
  • View Data Sheet

    Name :

    VAT1 Human

    Description:

    Vesicle Amine Transport Protein 1 Homolog Human Recombinant

    Synaptic vesicle membrane protein VAT-1 homolog, VAT1, VATI.

    Product # :

    PRO-1011

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
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    Description

    VAT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-393 a.a.) and having a molecular mass of 44.1kDa. VAT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    VAT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Synaptic vesicle membrane protein VAT-1 homolog (VAT1) is a member of the quinone oxidoreductase subfamily of zinc-containing alcohol dehydrogenase proteins. Synaptic vesicles are in charge of regulating the storage and release of neurotransmitters in the nerve terminal. VAT1 has an increased calcium ion-dependent expression in glioblastomas and on wounding, in basal keratinocytes. VAT1 is an abundant integral membrane protein of cholinergic synaptic vesicles and is believed to be involved in vesicular transport.

    • Synonyms

      Synaptic vesicle membrane protein VAT-1 homolog, VAT1, VATI.

    • 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 MSDEREVAEA ATGEDASSPP PKTEAASDPQ HPAASEGAAA AAASPPLLRC LVLTGFGGYD KVKLQSRPAA PPAPGPGQLT LRLRACGLNF ADLMARQGLY DRLPPLPVTP GMEGAGVVIA VGEGVSDRKA GDRVMVLNRS GMWQEEVTVP SVQTFLIPEA MTFEEAAALL VNYITAYMVL FDFGNLQPGH SVLVHMAAGG VGMAAVQLCR TVENVTVFGT ASASKHEALK ENGVTHPIDY HTTDYVDEIK KISPKGVDIV MDPLGGSDTA KGYNLLKPMG KVVTYGMANL LTGPKRNLMA LARTWWNQFS VTALQLLQAN RAVCGFHLGY LDGEVELVSG VVARLLALYN QGHIKPHIDS VWPFEKVADA MKQMQEKKNV GKVLLVPGPE KEN.

    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.

    Vat1 Human
  • View Data Sheet

    Name :

    APOE4 Human

    Description:

    Apolipoprotein E4 Human Recombinant

    Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.

    Product # :

    CYT-968

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    Shipped at Room temp

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    • description
    • source
    • formulation
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    • More Info

    Description

    Apolipoprotein E4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 299 amino acids and having a molecular mass of 34.4kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 20mM PBS, pH7.8 and 5% trehalose.

    Purity

    Greater than 95% as determined by:

    (a) Analysis by RP-HPLC.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.

    More Info

    • Introduction

      Apolipoprotein E (APOE) is a chylomicron lipoprotein which is essential for the metabolism of lipoproteins and lipid transport. The APOE gene has 3 alleles, designated APOE2, APOE3, and APOE4. The APOE allelic proteins differ by only one or two amino acids, however have different biological structures and functions. APOE3 is the most common and neutral allele. The APOE4 allele is linked with an increased risk for Alzheimer's Disease (AD) and coronary artery disease (CAD). The APOE4 protein morphology decreases the ability of APOE4 to clear beta-amyloid protein from the brain, resulting in AD progression. The APOE2 allele is linked with type III hyperlipoproteinemia, which is characterized by defects in the clearance of plasma lipoproteins, however APOE2 may have a protective effect against AD.

    • Synonyms

      Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized APOE4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOE4 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 APOE4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.

    • Background

      What is the molecular weight/Mw of APOE4 Protein?
      APOE4 Protein has a total Mw of 34.4kDa.

      What is the source or expression system of APOE4 Protein?
      Escherichia Coli.

      What is the Purity of APOE4 Protein?
      APOE4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOE4 Protein?
      When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.

      What is the amino acid sequence of APOE4 Protein?
      KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.

      What applications can APOE4 Protein be used in?
      APOE4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOE4 Protein?
      The endotoxin level is minimal, APOE4 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.

    Apoe4 Human
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