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Search results

1000 results found for “Collagen”

Name

Description

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  • View Data Sheet

    Name :

    LMNA Human

    Description:

    Lamin A/C Human Recombinant

    Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.

    Product # :

    PRO-2666

    Price :

    Quantity :

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    Description

    LMNA Human Recombinant fused with a His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 614 amino acids and having a molecular mass of 68.0kDa. The LMNA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LMNA solution contains 20mM Tris-HCl pH 7.5, 1mM DTT, 0.5M NaCl, 1.5mM EDTA and 20%(v/v) glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
      Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
      Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.

    • Synonyms

      Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.

    • 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

      MAHHHHHHVG TGSNDDDDKS PDMETPSQRR ATRSGAQASS TPLSPTRITR LQEKEDLQEL NDRLAVYIDR VRSLETENAG LRLRITESEE VVSREVSGI KAAYEAELGD ARKTLDSVAK ERARLQLELS KVREEFKELK ARNTKKEGDL IAAQARLKDL EALLNSKEAA LSTALSEKRT LEGELHDLRG QVAKLEAALG EAKKQLQDEM LRRVDAENRL QTMKEELDFQ KNIYSEELRE TKRRHETRLV EIDNGKQREF ESRLADALQE LRAQHEDQVE QYKKELEKTY SAKLDNARQS AERNSNLVGA AHEELQQSRI RIDSLSAQLS QLQKQLAAKE AKLRDLEDSL ARERDTSRRL LAEKEREMAE MRARMQQQLD EYQELLDIKL ALDMEIHAYR KLLEGEEERL RLSPSPTSQR SRGRASSHSS QTQGGGSVTK KRKLESTESR SSFSQHARTS GRVAVEEVDE EGKFVRLRNK SNEDQSMGNW QIKRQNGDDP LLTYRFPPKF TLKAGQVVTI WAAGAGATHS PPTDLVWKAQ NTWGCGNSLR TALINSTGEE VAMRKLVRSV TVVEDDEDED GDDLLHHHHG SHCSSSGDPA EYNLRSRTVL CGTCGQPADK ASASGSGAQS PQNCSIM

    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.

    Lmna Human
  • View Data Sheet

    Name :

    Insulin Human (20-110)

    Description:

    Insulin (20-110 a.a) Human Recombinant

    Product # :

    CYT-1237

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    Description

    The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN

    • Background

      Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.

    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.

    Insulin Recombinant
  • View Data Sheet

    Name :

    Leptin qA Ovine, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Ovine Recombinant

    Product # :

    CYT-1246

    Price :

    Quantity :

    Shipping Method :

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    • More Info

    Description

    Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Background

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

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Antagonist Peg Ovine
  • View Data Sheet

    Name :

    PCSK1N Human

    Description:

    Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant

    ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    Product # :

    PRO-1819

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.

    • Synonyms

      ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    • 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 MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP P.

    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.

    Pcsk1N Human
  • View Data Sheet

    Name :

    NEFL Bovine

    Description:

    Neurofilament Light Bovine

    Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    Product # :

    PRO-2786

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NEFL Bovine having a calculated molecular mass of 68 kDa, pI-5.0.

    Source

    Bovine spinal cord.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized NEFL between 2-8°C, do not freeze. Upon reconstitution NEFL should be stored at -20°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Neurofilament light chain (NEFL) is a critical component of the neuronal cytoskeleton, primarily found in neurons of the central and peripheral nervous systems. While extensive research has been conducted on NEFL in human and rodent models, the study of NEFL in bovine nervous tissues is an emerging area with potential for advancing our understanding of neuronal biology in larger mammals and its applications in veterinary medicine and neurobiology.

      Bovine nervous tissues, such as the brain and spinal cord, are of particular interest due to their relevance in cattle health and the food industry. This research aims to provide a comprehensive exploration of NEFL in bovine nervous tissues, elucidating its functions, structural significance, and potential applications.

      The primary objective of this research is to elucidate the role of NEFL in bovine nervous tissues, particularly in maintaining the structural integrity of neurons and axons. In vitro and ex vivo experiments, utilizing bovine neuronal cell cultures and tissue specimens, will be conducted to investigate how NEFL contributes to neuronal morphology, axonal transport, and neuronal resilience. Understanding these mechanisms is fundamental for deciphering the complexities of neuronal biology in bovine species.

      The second objective is to assess the relevance of bovine NEFL in veterinary medicine. Studies involving bovine models will be conducted to evaluate the impact of NEFL mutations or variations on neuronal health, disease susceptibility, and neurodegenerative conditions. These investigations may provide valuable insights into potential applications in cattle health and the development of diagnostic tools for neurological disorders.

      The third objective is to explore the potential applications of bovine NEFL in neurobiology and biotechnology. Research will investigate the use of bovine NEFL-expressing cells as models for studying neuronal-related diseases and for developing tissue engineering approaches for veterinary medicine and biotechnology.

      By delving into the functions and roles of NEFL in bovine nervous tissues, this research aims to expand our knowledge of neuronal biology, its implications for veterinary medicine, and its potential applications in neurobiology and cattle health

    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.

    Nefl Bovine
  • View Data Sheet

    Name :

    GDF3 Human

    Description:

    Growth Differentiation Factor-3 Human Recombinant

    Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

    Product # :

    CYT-694

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    Description

    GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated solution (0.5mg/ml) containing 30mM Acetate buffer pH-4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.

    • Synonyms

      Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF3 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 GDF3 in sterile 100mM Acetate buffer pH-4 at a concentration of 0.5mg/ml. For the dilution into higher pH values, it is recommended to dilute the protein to a concentration of 10μg/ml. Please note that in higher concentrations the solubility of GDF3 is limited. The protein is not sterile! Please sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

    • Background

      What is the molecular weight/Mw of GDF3 HUMAN Protein?
      GDF3 HUMAN Protein has a total Mw of 14.15XkDa.

      What is the source or expression system of GDF3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GDF3 HUMAN Protein?
      GDF3 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF3 HUMAN Protein?
      The biological functionality of GDF3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GDF3 HUMAN Protein?
      MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

      What applications can GDF3 HUMAN Protein be used in?
      GDF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF3 HUMAN Protein?
      The endotoxin level is minimal, GDF3 HUMAN Protein was purified using conventional chromatography techniques.

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

    Gdf3 Human
  • View Data Sheet

    Name :

    ENHO Human

    Description:

    Energy Homeostasis Associated Human Recombinant

    Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    Product # :

    PRO-1569

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    Description

    ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.

    • Synonyms

      Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

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

    • Amino Acid Sequence

      MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

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    Enho Human
  • View Data Sheet

    Name :

    Inhibin a Human

    Description:

    Inhibin Alpha Human Recombinant

    Product # :

    HOR-303

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    Description

    Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE analysis.

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      Alpha chain:
      STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

      Beta Chain:
      GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
      GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    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.

    Inhibin A Human
  • View Data Sheet

    Name :

    RPAIN Human

    Description:

    RPA Interacting Protein Human Recombinant

    HRIP, RIP, RPA-interacting protein, hRIP, RPAIN.

    Product # :

    PRO-1661

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    Description

    RPAIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106 a.a.) and having a molecular mass of 14.7kDa.RPAIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RPAIN protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RPA-interacting protein isoform d (RPAIN) is a single-stranded-DNA binding protein which participates in various eukaryotic DNA processes such as replication, repair and recombination. RPAIN interacting protein has been indicated as an adapter protein that is involved in RPA nuclear import instead of the prototypical importin proteins that normally mediate nuclear import. RPAIN is mainly expressed in pancreas, kidney, muscle, liver, lung, placenta, brain, heart, leukocytes, colon, intestine, ovary, testis, prostate, thymus and spleen.

    • Synonyms

      HRIP, RIP, RPA-interacting protein, hRIP, RPAIN.

    • 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 MGSMAESLRS PRRSLYKLVG SPPWKEAFRQ RCLERMRNSR DRLLNRYRQA GSSGPGNSQN SFLVQEVMEE EWNALQSVEN CPEDLAQLEE LIDMAVLEEI QQELINQGL.

    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.

    Rpain Human
  • View Data Sheet

    Name :

    RALY Human

    Description:

    RALY Human Recombinant

    RALY Heterogeneous Nuclear Ribonucleoprotein, RNA-Binding Protein (Autoantigenic, HnRNP-Associated With Lethal Yellow), HnRNP Associated With Lethal Yellow Protein Homolog, Heterogeneous Nuclear Ribonucleoprotein C-Like 2, HnRNP Core Protein C-Like 2, Autoantigen P542, HNRPCL2, P542, RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog (Mouse)), RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog), RNA-Binding Protein (Autoantigenic), RNA-Binding Protein Raly, RNA-binding protein Raly.

    Product # :

    PRO-2095

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    Description

    RALY 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 34.9kDa. RALY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RALY 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.

    More Info

    • Introduction

      RALY belongs to the heterogeneous nuclear ribonucleoprotein (hnRNP) gene family. RALY takes part in pre-mRNA splicing and also in embryonic development. Moreover, alternate splicing results in multiple transcript variants have been found for RALY.

    • Synonyms

      RALY Heterogeneous Nuclear Ribonucleoprotein, RNA-Binding Protein (Autoantigenic, HnRNP-Associated With Lethal Yellow), HnRNP Associated With Lethal Yellow Protein Homolog, Heterogeneous Nuclear Ribonucleoprotein C-Like 2, HnRNP Core Protein C-Like 2, Autoantigen P542, HNRPCL2, P542, RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog (Mouse)), RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog), RNA-Binding Protein (Autoantigenic), RNA-Binding Protein Raly, RNA-binding protein Raly.

    • 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 MGSMSLKLQA SNVTNKNDPK SINSRVFIGN LNTALVKKSD VETIFSKYGR VAGCSVHKGY AFVQYSNERH ARAAVLGENG RVLAGQTLDI NMAGEPKPDR PKGLKRAASA IYSGYIFDYD YYRDDFYDRL FDYRGRLSPV PVPRAVPVKR PRVTVPLVRR VKTNVPVKLF ARSTAVTTSS AKIKLKSSEL QAIKTELTQI KSNIDALLSR LEQIAAEQKA NPDGKKKGDG GGAGGGGGGG GSGGGGSGGG GGGGSSRPPA PQENTTSEAG LPQGEARTRD DGDEEGLLTH SEEELEHSQD TDADDGALQ.

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    Raly Human
  • View Data Sheet

    Name :

    MMP 8 Human

    Description:

    Matrix Metalloproteinase-8 Human Recombinant

    EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.

    Product # :

    ENZ-301

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    Description

    Matrix Metalloproteinase-8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 75 kDa.The MMP-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP-8 protein solution (100 units/ml) in 0.05M Tris-HCl buffer, pH 7.6, 0.2M NaCl, 5mM CaCl2, 0.0025% NaN3 and 0.1% BSA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    100 units/ml after activation with APMA by solution assay method.
    One unit of collagenolytic activity is defined as the cleavage of 1µg of collagen per minute by the solution method.

    More Info

    • Introduction

      Full-length recombinant human neutrophil MMP-8, latent form.
      Matrix metalloproteinase 8 (MMP-8), degrades interstitial collagens, acting preferentially on collagen type I.
      Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
      MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

    • Synonyms

      EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Applications

      Used as a standard for analyzing mammalian colagenase activity.

    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.

    Mmp8 Human
  • View Data Sheet

    Name :

    ANXA10 Human (1-162)

    Description:

    Annexin A10 (1-162 a.a.) Human Recombinant

    anxa-10.

    Product # :

    PRO-2837

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    Description

    The ANXA10 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ANXA10 His-Tagged Fusion Protein, produced in E. coli, is a 21kDa protein containing 162 amino acid residues of the ANXA10 Human, 1-162 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      anxa-10.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized ANXA10 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      Annexin A10 also known as ANXA10 is a part of the annexin family of calcium-binding proteins which members own a conserved core domain and a unique amino-terminal region which may convene binding specificity. The ANXA10 protein contains 4 annexin domains and plays a role in the regulation of cellular growth and signal transduction pathways throughout the cell.

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    Anxa10 Protein
  • View Data Sheet

    Name :

    RPS27A Human, Biotin

    Description:

    Ubiquitin Biotinylated Human Recombinant

    Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.

    Product # :

    PRO-629

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    Description

    Recombinant Human RPS27A protein biotinylated with NHS-biotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 76 amino acids and having a molecular mass of 8.6 kDa.

    Source

    Escherichia Coli.

    Formulation

    The RPS27A is supplied in 1x PBS and 0.05% PBS.

    Purity

    RPS27A Protein biotinilation is determined by Western Blotting and ELISA analysis using streptavidin–HRP conjugated as a detection reagent. Free biotin is eliminated by dialysis against PBS. Protein concentration is determined by 280nm absorbance.

    More Info

    • Introduction

      Recombinant Human Ubiquitin having the accession number of P62988 was conjugated to Biotin. RPS27A is a small protein composed of 76 amino acids. RPS27A is found only in eukaryotic organisms among which shows strong sequence conservation. The RPS27A protein is present in all cell types, thus giving rise to its name.
      RPS27A is found either in free form or conjugated to proteins through a covalent bond between the glycine at the C-terminal end and the side chains of lysine.
      The connection of multiple copies of RPS27A targets the proteins for degradation by the 26S proteosome. RPS27A ligation is an ATP-dependent multi-step process. RPS27A is activated by the E1 enzyme. The attachment of RPS27A to the target protein is catalyzed by the E2 enzyme acting in concert with E3 which is involved in the recognition of the substrate protein.

    • Synonyms

      Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.

    • 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. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

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    RPS27A Human, Biotin
  • View Data Sheet

    Name :

    SNX5 Human

    Description:

    Sorting Nexin 5 Human Recombinant

    Sorting nexin-5 isoform a, Sorting nexin-5, SNX5.

    Product # :

    PRO-786

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    Description

    SNX5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 427 amino acids (1-404 a.a) and having a molecular mass of 49.2kDa.SNX5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNX5 protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sorting nexin-5 (SNX5) belongs to the sorting nexin family, whose members contains a phox (PX) domain, (which is a phosphoinositide binding domain) and are involved in intracellular trafficking. SNX5 protein is a component of the mammalian retromer complex, which facilitates cargo recovery from endosomes to the trans-Golgi network. SNX5 binds to the Fanconi anemia, complementation group A protein.

    • Synonyms

      Sorting nexin-5 isoform a, Sorting nexin-5, SNX5.

    • 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 MGSMAAVPEL LQQQEEDRSK LRSVSVDLNV DPSLQIDIPD ALSERDKVKF TVHTKTTLPT FQSPEFSVTR QHEDFVWLHD TLIETTDYAG LIIPPAPTKP DFDGPREKMQ KLGEGEGSMT KEEFAKMKQE LEAEYLAVFK KTVSSHEVFL QRLSSHPVLS KDRNFHVFLE YDQDLSVRRK NTKEMFGGFF KSVVKSADEV LFTGVKEVDD FFEQEKNFLI NYYNRIKDSC VKADKMTRSH KNVADDYIHT AACLHSLALE EPTVIKKYLL KVAELFEKLR KVEGRVSSDE DLKLTELLRY YMLNIEAAKD LLYRRTKALI DYENSNKALD KARLKSKDVK LAEAHQQECC QKFEQLSESA KEELINFKRK RVAAFRKNLI EMSELEIKHA RNNVSLLQSC IDLFKNN.

    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.

    Snx5 Human
  • View Data Sheet

    Name :

    KLK5 Human, Sf9

    Description:

    Kallikrein-5 Human Recombinant, Sf9

    Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.

    Product # :

    ENZ-1021

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    Description

    Kallikrein-5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 236 amino acids (67-293 a.a.) and having a molecular mass of 26.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.

    • Synonyms

      Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.

    • 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

      ADLIINGSDC DMHTQPWQAA LLLRPNQLYC GAVLVHPQWL LTAAHCRKKV FRVRLGHYSL SPVYESGQQM FQGVKSIPHP GYSHPGHSND LMLIKLNRRI RPTKDVRPIN VSSHCPSAGT KCLVSGWGTT KSPQVHFPKV LQCLNISVLS QKRCEDAYPR QIDDTMFCAG DKAGRDSCQG DSGGPVVCNG SLQGLVSWGD YPCARPNRPG VYTNLCKFTK WIQETIQANS HHHHHH.

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    Klk5 Human Sf9
  • View Data Sheet

    Name :

    NCL Human

    Description:

    Nucleolin Human Recombinant

    Nucleolin, Protein C23, NCL, C23.

    Product # :

    PRO-1508

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    Description

    Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.

    • Synonyms

      Nucleolin, Protein C23, NCL, C23.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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    Ncl Human
  • View Data Sheet

    Name :

    BCAM Human

    Description:

    Basal Cell Adhesion Molecule (CD239) Human Recombinant

    Basal cell adhesion molecule isoform 1, BCAM, AU, CD239, LU, MSK19, Auberger B antigen, B-CAM cell surface glycoprotein, F8/G253 antigen, Lutheran antigen, Lutheran blood group glycoprotein, CD_antigen: CD239, LU, MSK19.

    Product # :

    PRO-2429

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    Description

    BCAM produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 755 amino acids (32-547a.a.) and having a molecular mass of 83.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). BCAM is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Basal Cell Adhesion Molecule (BCAM) which is a product of alternate splicing of the Lutheran blood group molecule is a part of the immunoglobulin superfamily. BCAM contains five extracellular immunoglobulin domains, a single transmembrane domain, and a short C-terminal cytoplasmic tail. BCAM protein is upregulated following malignant transformation of some cell types in vivo and in vitro. Furthermore, BCAM interacts with integrin in sickle red cells, and participates in vasoocclusive episodes.

    • Synonyms

      Basal cell adhesion molecule isoform 1, BCAM, AU, CD239, LU, MSK19, Auberger B antigen, B-CAM cell surface glycoprotein, F8/G253 antigen, Lutheran antigen, Lutheran blood group glycoprotein, CD_antigen: CD239, LU, MSK19.

    • 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

      EVRLSVPPLV EVMRGKSVIL DCTPTGTHDH YMLEWFLTDR SGARPRLASA EMQGSELQVT MHDTRGRSPP YQLDSQGRLV LAEAQVGDER DYVCVVRAGA AGTAEATARL NVFAKPEATE VSPNKGTLSV MEDSAQEIAT CNSRNGNPAP KITWYRNGQR LEVPVEMNPE GYMTSRTVRE ASGLLSLTST LYLRLRKDDR DASFHCAAHY SLPEGRHGRL DSPTFHLTLH YPTEHVQFWV GSPSTPAGWV REGDTVQLLC RGDGSPSPEY TLFRLQDEQE EVLNVNLEGN LTLEGVTRGQ SGTYGCRVED YDAADDVQLS KTLELRVAYL DPLELSEGKV LSLPLNSSAV VNCSVHGLPT PALRWTKDST PLGDGPMLSL SSITFDSNGT YVCEASLPTV PVLSRTQNFT LLVQGSPELK TAEIEPKADG SWREGDEVTL ICSARGHPDP KLSWSQLGGS PAEPIPGRQG WVSSSLTLKV TSALSRDGIS CEASNPHGNK RHVFHFGTVS PQTSQAVEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    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.

    Bcam Human
  • View Data Sheet

    Name :

    Omentin 298 a.a. Human

    Description:

    Omentin 298 a.a. Human Recombinant

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-061

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    Description

    Omentin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (17-313) and having a molecular mass of 33.2 kDa.The Omentin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Omentin protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.4M Urea and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • 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

      MWSTDEANTY FKEWTCSSSP SLPRSCKEIK DECPSAFDGL YFLRTENGVI YQTFCDMTSG GGGWTLVASV HENDMRGKCT VGDRWSSQQG SKAVYPEGDG NWANYNTFGS AEAATSDDYK NPGYYDIQAK DLGIWHVPNK SPMQHWRNSS LLRYRTDTGF LQTLGHNLFG IYQKYPVKYG EGKCWTDNGP VIPVVYDFGD AQKTASYYSP YGQREFTAGF VQFRVFNNER AANALCAGMR VTGCNTEHHC IGGGGYFPEA SPQQCGDFSG FDWSGYGTHV GYSSSREITE AAVLLFYR

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    Omentin 298 Aa Human
  • View Data Sheet

    Name :

    BIN1 Human

    Description:

    Bridging Integrator 1 Human Recombinant

    AMPH2, AMPHL, MGC10367, SH3P9, Amphiphysin II.

    Product # :

    PRO-546

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    Description

    BIN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 459 amino acids (1-439 a.a) and having a molecular mass of 50.4 kDa. The BIN1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BIN1 protein solution (1mg/ml) containing 20mM Tris buffer pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BIN1 is a nucleocytoplasmic adaptor protein, one of which was primarily identified as MYC-interacting protein having the characteristics of a tumor suppressor. BIN1 protein interacts with and inhibits the oncogenic activity of the myc oncoprotein that is a key player in many human cancers. The absence of Bin1 contributes to growth deregulation in cancer cells in carcinoma of the breast, colon, lung, cervix, prostate and liver.

    • Synonyms

      AMPH2, AMPHL, MGC10367, SH3P9, Amphiphysin II.

    • 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 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE KQHGSNTFTV KAQPSDNAPA KGNKSPSPPD GSPAATPEIR VNHEPEPAGG ATPGATLPKS PSQPAEASEV AGGTQPAAGA QEPGETAASE AASSSLPAVV VETFPATVNG TVEGGSGAGR LDLPPGFMFK VQAQHDYTAT DTDELQLRAG DVVLVIPFQN PEEQDEGWLM GVKESDWNQH KELEKCRGVF PENFTERVP.

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    Bin1 Human
  • View Data Sheet

    Name :

    BMP 7 Human

    Description:

    Bone Morphogenetic Protein-7 Human Recombinant

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-333

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    Description

    Bone Morphogenetic Protein-7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 139 amino acids and having a molecular mass of 15679.97 Dalton. The BMP-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-7 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM sodium citrate pH=3.5.

    Purity

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

    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

      It is recommended to briefly centrifuge the vial prior to opening to bring the contents to the bottom. Reconstitute in 20mM-100mM acetic acid at a concentration of 0.1-0.5mg per ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Thr-Gly-Ser-Lys.

    • Background

      Bone Morphogenetic Protein-7 Human Recombinant: A Comprehensive Review

      Abstract:

      Bone Morphogenetic Protein-7 (BMP-7) is a crucial member of the transforming growth factor-beta (TGF-β) superfamily with diverse roles in development, tissue repair, and regeneration.

      This research paper provides a comprehensive review of BMP-7 Human Recombinant, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the therapeutic potential of BMP-7 modulation.

      Introduction:

      BMP-7 is a multifunctional growth factor that plays a significant role in skeletal development and tissue homeostasis. This paper aims to provide an extensive review of BMP-7 Human Recombinant, highlighting its importance in various biological processes and its potential therapeutic applications.

      Structure and Function of BMP-7:

      BMP-7 is a disulfide-linked homodimeric protein composed of two subunits. It binds to specific cell surface receptors, activating downstream signaling pathways, including the Smad pathway and non-Smad signaling cascades. These pathways regulate cellular processes such as proliferation, differentiation, and apoptosis.

      Skeletal Development and Regeneration:

      BMP-7 is a key regulator of bone formation and remodeling. It promotes osteoblast differentiation and bone mineralization, contributing to skeletal development and repair. BMP-7 also plays a role in cartilage formation and chondrogenesis.

      Tissue Repair and Regeneration:

      Beyond its skeletal functions, BMP-7 is involved in tissue repair and regeneration in various organs, including the kidney, liver, and heart. It promotes the regeneration of damaged tissues by stimulating cell proliferation, angiogenesis, and extracellular matrix remodeling.

      Therapeutic Potential:

      Due to its regenerative and reparative properties, BMP-7 has attracted significant attention as a potential therapeutic agent. It has been investigated for its applications in bone regeneration, cartilage repair, and the treatment of kidney and liver diseases. Clinical trials exploring the therapeutic efficacy of BMP-7 are ongoing.

      Challenges and Future Perspectives:

      Despite the promising therapeutic potential of BMP-7, challenges remain, including optimizing its delivery systems, understanding its dosage and duration of treatment, and managing potential side effects. Future research should focus on unraveling the intricate mechanisms of BMP-7 signaling, developing targeted therapies, and enhancing its clinical applications.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 15kDa.

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

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The biological functionality of BMP7 Protein will be determined in the future.

      What is the amino acid sequence of BMP7 Protein?
      BMP7 Protein is composed from 139 amino acids.

      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
  • View Data Sheet

    Name :

    CALML3 Human

    Description:

    Calmodulin Like 3 Human Recombinant

    Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.

    Product # :

    PRO-1323

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    Description

    CALML3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-149 a.a.) and having a molecular mass of 19kDa.CALML3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CALML3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calmodulin Like 3 (CALML3) is a member of the calmodulin family and contains 4 EF-hand domains. The CALML3 protein may be similar to that of genuine calmodulin and may in fact compete with calmodulin by binding, with different affinities, to cellular substrates. CALML3 protein is expressed in normal mammary, prostate, cervical, and epidermal tissues.

    • Synonyms

      Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.

    • 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 MGSHMADQLT EEQVTEFKEA FSLFDKDGDG CITTRELGTV MRSLGQNPTE AELRDMMSEI DRDGNGTVDF PEFLGMMARK MKDTDNEEEI REAFRVFDKD GNGFVSAAEL RHVMTRLGEK LSDEEVDEMI RAADTDGDGQ VNYEEFVRVL VSK.

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    Calml3 Human
  • View Data Sheet

    Name :

    CCL16 Human

    Description:

    LEC/NCC-4 Human Recombinant

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

    Product # :

    CHM-237

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL16 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CCL16in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

    • Background

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

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

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

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

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

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

      What is the endotoxin level for CCL16 HUMAN Protein?
      The endotoxin level is minimal, CCL16 HUMAN Protein was purified using conventional chromatography techniques.


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    Ccl16 Human
  • View Data Sheet

    Name :

    CX3CL1 Rat

    Description:

    Fractalkine Rat Recombinant (CX3CL1)

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

    Product # :

    CHM-005

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    Description

    Fractalkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa.The Fractalkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG

    • Background

      What is the molecular weight/Mw of CX3CL1 RAT Protein?
      CX3CL1 RAT Protein has a total Mw of 8.7kDa.

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

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

      What is the Biological Activity of CX3CL1 RAT Protein?
      Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

      What is the amino acid sequence of CX3CL1 RAT Protein?
      QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG

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

      What is the endotoxin level for CX3CL1 RAT Protein?
      The endotoxin level is minimal, CX3CL1 RAT Protein was purified using conventional chromatography techniques.


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

    Fractalkine Rat
  • View Data Sheet

    Name :

    FURIN Human

    Description:

    Furin Human Recombinant

    Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    Product # :

    PRO-2199

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.

    • Synonyms

      Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.

    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.

    Furin Human
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