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Search results

1000 results found for “noggin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    JOSD1 Human

    Description:

    Josephin Domain Containing 1 Human Recombinant

    Josephin-1, Josephin domain-containing 1, JOSD1, JSPH1, KIAA0063, dJ508I15.2.

    Product # :

    PRO-1251

    Price :

    Quantity :

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    • More Info

    Description

    JOSD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202 a.a.) and having a molecular mass of 25.6kDa.JOSD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    JOSD1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Josephin-1 (JOSD1) has minimal protease activity towards poly-ubiquitin chains (in vitro). JOSD1 functions as a deubiquitinating enzyme. Ubiquitin-binding sites in the Josephin domain are a factor in ubiquitin chain binding and cleavage.

    • Synonyms

      Josephin-1, Josephin domain-containing 1, JOSD1, JSPH1, KIAA0063, dJ508I15.2.

    • 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 MGSMSCVPWK GDKAKSESLE LPQAAPPQIY HEKQRRELCA LHALNNVFQD SNAFTRDTLQ EIFQRLSPNT MVTPHKKSML GNGNYDVNVI MAALQTKGYE AVWWDKRRDV GVIALTNVMG FIMNLPSSLC WGPLKLPLKR QHWICVREVG GAYYNLDSKL KMPEWIGGES ELRKFLKHHL RGKNCELLLV VPEEVEAHQS WRTDV.

    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.

    Josd1 Human
  • 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

    Price :

    Quantity :

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    • 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
  • View Data Sheet

    Name :

    GNAZ Human

    Description:

    Guanine Nucleotide Binding Protein Alpha Z Polypeptide Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.

    Product # :

    PRO-1225

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    GNAZ Human Recombinant produced in E. coli is a single polypeptide chain containing 375 amino acids (1-355) and having a molecular mass of 43.0 kDa.GNAZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Guanine nucleotide-binding protein G(z) subunit alpha (GNAZ) belongs to the G protein subfamily which mediates signal transduction in pertussis toxin-insensitive systems. GNAZ has a role in maintaining the ionic balance of perilymphatic and endolymphatic cochlear fluids. G proteins are involved as modulators or transducers in a variety of transmembrane signaling systems.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.

    • 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 MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR AYDAVQLFAL TGPAESKGEI TPELLGVMRR LWADPGAQAC FSRSSEYHLE DNAAYYLNDL ERIAAADYIP TVEDILRSRD MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC

    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.

    Gnaz Human
  • View Data Sheet

    Name :

    Leptin Human, PEG

    Description:

    Leptin Human Recombinant, PEG

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1108

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • biological activity
    • More Info

    Description

    Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.

    More Info

    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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 Pegylated leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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 Mutant
  • View Data Sheet

    Name :

    CAPG Human

    Description:

    Capping Protein Gelsolin-Like Human Recombinant

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

    Product # :

    PRO-759

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    Description

    CAPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-348 a.a.) and having a molecular mass of 38.5 kDa. The CAPG protein is purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • 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

      MYTAIPQSGS PFPGSVQDPG LHVWRVEKLK PVPVAQENQG VFFSGDSYLV LHNGPEEVSH LHLWIGQQSS RDEQGACAVL AVHLNTLLGE RPVQHREVQG NESDLFMSYF PRGLKYQEGG VESAFHKTST GAPAAIKKLY QVKGKKNIRA TERALNWDSF NTGDCFILDL GQNIFAWCGG KSNILERNKA RDLALAIRDS ERQGKAQVEI VTDGEEPAEM IQVLGPKPAL KEGNPEEDLT ADKANAQAAA LYKVSDATGQ MNLTKVADSS PFALELLISD DCFVLDNGLC GKIYIWKGRK ANEKERQAAL QVAEGFISRM QYAPNTQVEI LPQGRESPIF KQFFKDWK.

    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.

    Capg Human
  • View Data Sheet

    Name :

    Desmin Chicken

    Description:

    Desmin Chicken Gizzard

    Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    Product # :

    PRO-2783

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    Description

    Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.

    Source

    Chicken gizzard.

    Formulation

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

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Background

      Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.

      The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.

      The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.

      The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.

      By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.

    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.

    Desmin Chicken
  • View Data Sheet

    Name :

    OGG1 Mouse

    Description:

    8-Oxoguanine DNA Glycosylase Mouse Recombinant

    HMMH, HOGG1, MUTM, OGH1, AP lyase, OGG1, 8-Oxoguanine DNA Glycosylase, OGG1.

    Product # :

    ENZ-1048

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    Description

    OGG1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a) and having a molecular mass of 41.3kDa. OGG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OGG1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3 to the lesion.

    • Synonyms

      HMMH, HOGG1, MUTM, OGH1, AP lyase, OGG1, 8-Oxoguanine DNA Glycosylase, OGG1.

    • Physical Appearance

      Sterile filtered colourless 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 MGSMLFRSWL PSSMRHRTLS SSPALWASIP CPRSELRLDL VLASGQSFRW KEQSPAHWSG VLADQVWTLT QTEDQLYCTV YRGDDSQVSR PTLEELETLH KYFQLDVSLA QLYSHWASVD SHFQRVAQKF QGVRLLRQDP TECLFSFICS SNNNIARITG MVERLCQAFG PRLIQLDDVT YHGFPNLHAL AGPEAETHLR KLGLGYRARY VRASAKAILE EQGGPAWLQQ LRVAPYEEAH KALCTLPGVG AKVADCICLM ALDKPQAVPV DVHVWQIAHR DYGWHPKTSQ AKGPSPLANK ELGNFFRNLW GPYAGWAQAV LFSADLRQPS LSREPPAKRK KGSKRPEG.

    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.

    Ogg1 Mouse
  • View Data Sheet

    Name :

    CRYGN Human

    Description:

    Crystallin, Gamma N Human Recombinant

    Gamma-crystallin N, Gamma-N-crystallin, CRYGN.

    Product # :

    PRO-1152

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    Description

    CRYGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-182 a.a) and having a molecular mass of 23.1kDa.CRYGN is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crystallin gamma N (CRYGN) is a member of the Crystallins family. Crystallins are the main proteins of the vertebrate eye lens, where they preserve the transparency and refractive index of the lens. CRYGN is unique in the way that it has both beta and gamma crystallin protein motifs. The CRYGN is differentially controlled after early development, and is involved in cataract creation due to either age-related protein degradation or genetic mutation.

    • Synonyms

      Gamma-crystallin N, Gamma-N-crystallin, CRYGN.

    • 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 MGSHMAQRSG KITLYEGKHF TGQKLEVFGD CDNFQDRGFM NRVNSIHVES GAWVCFNHPD FRGQQFILEH GDYPDFFRWN SHSDHMGSCR PVGMHGEHFR LEIFEGCNFT GQCLEFLEDS PFLQSRGWVK NCVNTIKVYG DGAAWSPRSF GAEDFQLSSS LQSDQGPEEA TTKPATTQPP FLTANL.

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    Crygn Human
  • View Data Sheet

    Name :

    SCG5 Human

    Description:

    Secretogranin-V Human Recombinant

    7B2, SgV, P7B2, SGNE1, Secretogranin-5, Secretory granule endocrine protein I.

    Product # :

    PRO-467

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    Description

    SCG5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (27-212 a.a.) and having a molecular mass of 22 kDa. SCG5 is fused to a 8 amino acid His tag at C-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    SCG5 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 0.1mM PMSF, 1mM DTT, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SCG5 also called 7B2 protein is localized in neuroendocrine tissues. SCG5 functions as a chaperone protein for the proprotein convertase PC2 and is essential for the production of an active PC2 enzyme.

    • Synonyms

      7B2, SgV, P7B2, SGNE1, Secretogranin-5, Secretory granule endocrine protein I.

    • 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.

    • Amino Acid Sequence

      MYSPRTPDRV SEADIQRLLH GVMEQLGIAR PRVEYPAHQA MNLVGPQSIE GGAHEGLQHL GPFGNIPNIV AELTGDNIPK DFSEDQGYPD
      PPNPCPVGKT ADDGCLENTP DTAEFSREFQ LHQHLSDPEH DYPGLGKWNK KLLYEKMKGG ERRKRRSVNP YLQGQRLDNV VAKKSVPHFS
      DEDKDPELEH 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.

    Scg5 Human
  • View Data Sheet

    Name :

    OSM Rat

    Description:

    Oncostatin-M Rat Recombinant

    Oncostatin-M, OSM, OncoM.

    Product # :

    CYT-169

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    Description

    OSM Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids and having a molecular mass of 24.3kDa.The OSM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of rat C6 cells is < 5.0 µg/ml, corresponding to a specific activity of > 200 units/mg.

    More Info

    • Introduction

      Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

    • Synonyms

      Oncostatin-M, OSM, OncoM.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KRGCSSSSPK LLSQLKSQAN ITGNTASLLE PYILHQNLNT LTLRAACTEH PVAFPSEDML RQLSKPDFLS TVHATLGRVW HQLGAFRQQF PKIQDFPELE RARQNIQGIR NNVYCMARLL HPPLEIPEPT QADSGTSRPT TTAPGIFQIK IDSCRFLWGY HRFMGSVGRV FEEWGDGSRR SR RHSPLWAW LKGDHRIRPS RSSQSAMLRS LVPR.

    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.

    Osm Rat
  • View Data Sheet

    Name :

    ProNGF Human

    Description:

    Pro-Nerve Growth Factor Human Recombinant

    Human Pro-NGF, ProNGF, NGFB.

    Product # :

    CYT-426

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    Description

    Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.ProNGF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ProNGF was lyophilized from a 0.2 μM filtered solution of 20m Tris-HCL, 0.5M NaCl, 5% Trehalose, 5% Mannitol. 0.01% Tween-80 and 1mM EDTA pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Human Pro-NGF, ProNGF, NGFB.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
      TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
      SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
      KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
      VCVLSRKAVRRA.

    • Background

      Pro-Nerve Growth Factor Human Recombinant: Unveiling its Potential in Neuroregulation and Disease Pathogenesis

      Abstract:

      Pro-Nerve Growth Factor (Pro-NGF) human recombinant is a crucial precursor protein involved in neuronal development, survival, and degenerative processes. This research paper aims to provide a comprehensive analysis of Pro-NGF, including its characteristics, processing mechanisms, and implications in neuroregulation and disease pathogenesis. Additionally, innovative methodologies for the production and manipulation of Pro-NGF human recombinant are proposed, highlighting its potential as a therapeutic target for neurological disorders and neurodegenerative diseases.

      Introduction:

      Neuroregulation and maintenance of neuronal health are intricate processes governed by a network of signaling molecules. Pro-NGF, the precursor form of Nerve Growth Factor (NGF), acts as a key player in neuronal development, synaptic plasticity, and cell survival. This paper delves into the distinctive features of Pro-NGF and presents novel approaches for the production and manipulation of Pro-NGF human recombinant, aiming to unravel its role in neuroregulation and disease pathogenesis.

      Characteristics and Processing Mechanisms:

      Pro-NGF is initially synthesized as an inactive precursor, requiring proteolytic cleavage for conversion into mature NGF. The processing of Pro-NGF involves the action of proteases, such as furin, and the formation of distinct protein complexes. The balance between Pro-NGF and mature NGF levels plays a critical role in modulating neuronal function and fate, influencing processes such as neuronal survival, axonal growth, and synaptic plasticity.

      Production and Manipulation of Pro-NGF Human Recombinant:

      Efficient production methodologies and manipulation strategies are crucial for studying the role of Pro-NGF in neuroregulation and disease pathogenesis. Recombinant protein expression systems, including mammalian cell culture and bacterial expression systems, have been employed to produce functional Pro-NGF human recombinant. Techniques such as mutagenesis, protein purification, and specific inhibitors targeting Pro-NGF processing pathways enable the manipulation of Pro-NGF levels and investigation of its downstream effects.

      Implications in Neuroregulation and Disease Pathogenesis:

      Pro-NGF human recombinant holds significant potential in understanding the intricate mechanisms underlying neuroregulation and disease pathogenesis. Dysregulation of Pro-NGF processing and altered Pro-NGF/mature NGF ratios have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and ischemic stroke. Manipulating Pro-NGF levels and the balance between its mature form may offer therapeutic strategies for modulating neurotrophic signaling and promoting neuronal health in these conditions.

      Conclusion:

      Pro-NGF human recombinant emerges as a key regulator in neuroregulation and disease pathogenesis, offering promising avenues for therapeutic intervention. Enhancing our understanding of Pro-NGF processing mechanisms and its downstream signaling cascades will provide valuable insights into neurodevelopment, neurodegeneration, and potential therapeutic strategies. Targeting Pro-NGF as a therapeutic intervention may hold immense promise in treating neurological disorders and promoting neuronal health.

      What is the molecular weight / Mw of ProNGF Protein?
      ProNGF Protein has a total Mw of 25kDa.

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

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


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

      What is the amino acid sequence of ProNGF Protein?
      MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
      TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
      SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
      KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
      VCVLSRKAVRRA

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

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

    Pro Ngf Human
  • View Data Sheet

    Name :

    SNAPIN Human

    Description:

    SNAP Associated Protein Human Recombinant

    SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.

    Product # :

    PRO-663

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    Description

    SNAPIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-136) and having a molecular mass of 17 kDa. SNAPIN is fused to 20 amino acid His Tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH-8, 5mM DTT, 2mM EDTA, 0.2M NaCl, and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.

    • Synonyms

      SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.

    • 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 MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINEDQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK.

    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.

    Snapin Human
  • View Data Sheet

    Name :

    LCN2 Rat

    Description:

    Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Rat Recombinant

    Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.

    Product # :

    ENZ-920

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    Description

    LCN2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (21-198 a.a) and having a molecular mass of 22.9kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core. They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

    • Synonyms

      Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.

    • 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 MGSQDSTQNL IPAPPLISVP LQPGFWTERF QGRWFVVGLA ANAVQKERQS RFTMYSTIYE LQEDNSYNVT SILVRGQGCR YWIRTFVPSS RPGQFTLGNI HSYPQIQSYD VQVADTDYDQ FAMVFFQKTS ENKQYFKVTL YGRTKGLSDE LKERFVSFAK SLGLKDNNIV FSVPTDQCID N.

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    Lcn2 Rat
  • View Data Sheet

    Name :

    CHGA Human, Sf9

    Description:

    Chromogranin A Human Recombinant, Sf9

    CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.

    Product # :

    PRO-2513

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    Description

    CHGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-457 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 448 amino acids and having a molecular mass of 50kDa.CHGA shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CHGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol & 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chromogranin-A Isoform 1 Preproprotein or CHGA is part of the neuroendocrine secretory proteins of the chromogranin/secretogranin family. CHGA is a precursor of numerus enzymes such as pancreastatin, catestatin, vasostatin-1,vasostatin-2, and parastatin. The protein acts as a negative regulator the neuroendocrine activity of autocrine or nearby cells (paracrine). CHGA causes further production of secretory granules that contains insulin in pancreatic islet beta cells.

    • Synonyms

      CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.

    • 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

      ADLLPVNSPM NKGDTEVMKC IVEVISDTLS KPSPMPVSQE CFETLRGDER ILSILRHQNL LKELQDLALQ GAKERAHQQK KHSGFEDELS EVLENQSSQA ELKEAVEEPS SKDVMEKRED SKEAEKSGEA TDGARPQALP EPMQESKAEG NNQAPGEEEE EEEEATNTHP PASLPSQKYP GPQAEGDSEG LSQGLVDREK GLSAEPGWQA KREEEEEEEE EAEAGEEAVP EEEGPTVVLN PHPSLGYKEI RKGESRSEAL AVDGAGKPGA EEAQDPEGKG EQEHSQQKEE EEEMAVVPQG LFRGGKSGEL EQEEERLSKE WEDSKRWSKM DQLAKELTAE KRLEGQEEEE DNRDSSMKLS FRARAYGFRG PGPQLRRGWR PSSREDSLEA GLPLQVRGYP EEKKEEEGSA NRRPEDQELE SLSAIEAELE KVAHQLQALR RGHHHHHH.

    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.

    Chromogranin A
  • View Data Sheet

    Name :

    NRP1 Mouse

    Description:

    Neuropilin 1 Mouse Recombinant

    Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.

    Product # :

    CYT-971

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    Description

    NRP1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856 a.a.) and having a molecular mass of 94.7kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.

    • Synonyms

      Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.

    • 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

      FRSDKCGGTI KIENPGYLTS PGYPHSYHPS EKCEWLIQAP EPYQRIMINF NPHFDLEDRD CKYDYVEVID GENEGGRLWG KFCGKIAPSP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TAPTGVIKSP GFPEKYPNSL ECTYIIFAPK MSEIILEFES FDLEQDSNPP GGMFCRYDRL EIWDGFPEVG PHIGRYCGQK TPGRIRSSSG VLSMVFYTDS AIAKEGFSAN YSVLQSSISE DFKCMEALGM ESGEIHSDQITASSQYGTNW SVERSRLNYP ENGWTPGEDS YKEWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYRVD ISSNGEDWIS LKEGNKAIIF QGNTNPTDVV LGVFSKPLIT RFVRIKPVSW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITASN QADRNWMPEN IRLVTSRTGW ALPPSPHPYT NEWLQVDLGD EKIVRGVIIQ GGKHRENKVF MRKFKIAYSN NGSDWKTIMD DSKRKAKSFE GNNNYDTPEL RTFSPLSTRF IRIYPERATH SGLGLRMELL GCEVEAPTAG PTTPNGNPVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTIIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDSHAQL RWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQSSAHC MTFWYHMSGS HVGTLRVKLR YQKPEEYDQL VWMVVGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PTDLDKKNTE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH

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    Nrp1 Mouse
  • View Data Sheet

    Name :

    Vimentin Bovine

    Description:

    Bovine Vimentin

    Vimentin, Vim, FLJ36605.

    Product # :

    PRO-525

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    Description

    Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.

    Source

    Bovine Lens.

    Formulation

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

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

    • Synonyms

      Vimentin, Vim, FLJ36605.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Reconstitution to filaments

      After vimentin is dissolved in 6M urea buffer (see above), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.

    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.

    Vimentin Bovine
  • View Data Sheet

    Name :

    MREG Human

    Description:

    Melanoregulin Human Recombinant

    Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.

    Product # :

    PRO-1885

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    Description

    MREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 27.3kDa.MREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Melanoregulin (MREG) takes part in membrane fusion and in regulating the biogenesis of disk membranes of photoreceptor rods. MREG is expressed in photoreceptor cells as two isoforms as a result of alternative splicing. MREG interacts with Peripherin-2, a photoreceptor specific tetraspanin protein which is required to preserve normal cell structure during the renewal process of membrane fusion. Moreover, MREG plays a part in the incorporation of pigments into hair.

    • Synonyms

      Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMGLRDWL RTVCCCCGCE CLEERALPEK EPLVSDNNPY SSFGATLVRD DEKNLWSMPH DVSHTEADDD RTLYNLIVIR NQQAKDSEEW QKLNYDIHTL RQVRREVRNR WKCILEDLGF QKEADSLLSV TKLSTISDSK NTRKAREMLL KLAEETNIFP TSWELSERYL FVVDRLIALD AAEEFFKLAR RTYPKKPGVP CLADGQKELH YLPFPSP

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    Mreg Human
  • View Data Sheet

    Name :

    SCG3 Human

    Description:

    Secretogranin III Human Recombinant

    Secretogranin III, secretogranin-3, SGIII.

    Product # :

    PRO-1556

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    Description

    SCG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 472 amino acids (20-468) and having a molecular mass of 53.0kDa.SCG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SCG3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SCG3 belongs to the chromogranin/secretogranin family of neuroendocrine secretory proteins. Though, the function of SCG3 is unknown, Granins operate as precursors for biologically active peptides. Several granins are known to serve as helper proteins in sorting and proteolytic processing of prohormones.

    • Synonyms

      Secretogranin III, secretogranin-3, SGIII.

    • 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 MGSFPKPGGS QDKSLHNREL SAERPLNEQI AEAEEDKIKK TYPPENKPGQ SNYSFVDNLN LLKAITEKEK IEKERQSIRS SPLDNKLNVE DVDSTKNRKL IDDYDSTKSG LDHKFQDDPD GLHQLDGTPL TAEDIVHKIA ARIYEENDRA VFDKIVSKLL NLGLITESQA HTLEDEVAEV LQKLISKEAN NYEEDPNKPT SWTENQAGKI PEKVTPMAAI QDGLAKGEND ETVSNTLTLT NGLERRTKTY SEDNFEELQY FPNFYALLKS IDSEKEAKEK ETLITIMKTL IDFVKMMVKY GTISPEEGVS YLENLDEMIA LQTKNKLEKN ATDNISKLFP APSEKSHEET DSTKEEAAKM EKEYGSLKDS TKDDNSNPGG KTDEPKGKTE AYLEAIRKNI EWLKKHDKKG NKEDYDLSKM RDFINKQADA YVEKGILDKE EAEAIKRIYS SL.

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    Scg3 Human
  • View Data Sheet

    Name :

    DRG1 Human

    Description:

    Developmentally Regulated GTP Binding Protein 1 Human Recombinant

    Developmentally-regulated GTP-binding protein 1, DRG-1, Neural precursor cell expressed developmentally down-regulated protein 3, NEDD-3, DRG1, NEDD3.

    Product # :

    PRO-885

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    Description

    DRG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 42.7kDa.DRG1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DRG1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 1mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Developmentally-regulated GTP-binding protein 1 (DRG1) is a member of the GTP1/OBG family. DRG1 has a role in cell proliferation and differentiation, as well as in apoptosis, proposing a role in tumor formation and metastasis. Expression of the DRG1 was considerably reduced in breast tumor cells, particularly in patients with lymph node or bone metastasis as compared to those with localized breast cancer. The DRG1 protein is expressed at high levels in the heart, kidney and skeletal muscle and at lower levels in the brain, liver, placenta, lung, colon and spleen.

    • Synonyms

      Developmentally-regulated GTP-binding protein 1, DRG-1, Neural precursor cell expressed developmentally down-regulated protein 3, NEDD-3, DRG1, NEDD3.

    • 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 MSSTLAKIAE IEAEMARTQK NKATAHHLGL LKARLAKLRR ELITPKGGGG GGPGEGFDVA KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGVIRYKG AKIQLLDLPG IIEGAKDGKG RGRQVIAVAR TCNLILIVLD VLKPLGHKKI IENELEGFGI RLNSKPPNIG FKKKDKGGIN LTATCPQSEL DAETVKSILA EYKIHNADVT LRSDATADDL IDVVEGNRVY IPCIYVLNKI DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLK LVRIYTKPKG QLPDYTSPVV LPYSRTTVED FCMKIHKNLI KEFKYALVWG LSVKHNPQKV GKDHTLEDED VIQIVKK.

    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.

    Drg1 Human
  • View Data Sheet

    Name :

    NMB Human

    Description:

    Neuromedin B Human Recombinant

    Neuromedin-B, NMB, Neuromedin-B-32, Neuromedin B.

    Product # :

    PRO-1518

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    Description

    NMB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (25-121) and having a molecular mass of 13.2 kDa.NMB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NMB solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuromedin B (NMB) which is a part of the bombesin/neuromedin-B/ranatensin family and stimulates smooth muscle contraction in a way similar to that of bombesin.

    • Synonyms

      Neuromedin-B, NMB, Neuromedin-B-32, Neuromedin B.

    • 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 MGSAPLSWDL PEPRSRASKI RVHSRGNLWA TGHFMGKKSL EPSSPSPLGT APHTSLRDQR LQLSHDLLGI LLLKKALGVS LSRPAPQIQY RRLLVQILQK.

    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.

    Nmb Human
  • View Data Sheet

    Name :

    b NGF Mouse

    Description:

    Beta-Nerve Growth Factor Mouse

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-440

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    Description

    NGF beta Mouse produced in Submaxillary Gland of Grown Mouse is a homodimer, non-glycosylated, polypeptide chain containing 2 identical 120 amino acids and having a molecular mass of 13,471 Dalton each.The NGF beta Mouse is purified by advanced biology purification technology.

    Source

    Submaxillary Gland of Grown Mouse.

    Formulation

    The NGF beta Mouse was lyophilized from solution containing 5% mannitol and 1% HSA.

    Purity

    Greater than 98% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE .

    Biological Activity

    The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 13kDa.

      What is the source or expression system of B NGF Protein?
      Submaxillary Gland of Grown Mouse.

      What is the Purity of B NGF Protein?

      B NGF Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of B NGF Protein?
      The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of B NGF Protein?
      SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.

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

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

    Beta Ngf Mouse
  • View Data Sheet

    Name :

    CHGA Human, HEK

    Description:

    Chromogranin A Human Recombinant, HEK

    CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.

    Product # :

    PRO-2664

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    Description

    CHGA Human Recombinant is a single, glycosylated polypeptide chain containing 445 amino acids (19-457a.a) and having a molecular mass of 49.7kDa (calculated). CHGA is fused to a 6 a.a His tag at C-terminal.

    Source

    HEK293 cells.

    Formulation

    CHGA filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS, pH 7.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chromogranin A is a 439 amino acid protein which is encoded on chromosome 14 and is present in neuroendocrine cells throughout the body, including the neuroendocrine cells of the large and small intestine, adrenal medulla and pancreatic islets. It is an excellent marker for carcinoid tumors, phenochromocytomas, paragangliomas, and other neuroendocrine tumors.
      Coexpression of chromogranin A and neuron specific enolase (NSE) is common in neuroendocrine neoplasms.

    • Synonyms

      CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      LPVNSPMNKG DTEVMKCIVE VISDTLSKPS PMPVSQECFE TLRGDERILS ILRHQNLLKE LQDLALQGAK ERAHQQKKHS GFEDELSEVL ENQSSQAELK EAVEEPSSKD VMEKREDSKE AEKSGEATDG ARPQALPEPM QESKAEGNNQ APGEEEEEEE EATNTHPPAS LPSQKYPGPQ AEGDSEGLSQ GLVDREKGLS AEPGWQAKRE EEEEEEEEAE AGEEAVPEEE GPTVVLNPHP SLGYKEIRKG ESRSEALAVD GAGKPGAEEA QDPEGKGEQE HSQQKEEEEE MAVVPQGLFR GGKSGELEQE EERLSKEWED SKRWSKMDQL AKELTAEKRL EGQEEEEDNR DSSMKLSFRA RAYGFRGPGP QLRRGWRPSS REDSLEAGLP LQVRGYPEEK KEEEGSANRR PEDQELESLS AIEAELEKVA HQLQALRRGH HHHHH

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    Chga Human
  • View Data Sheet

    Name :

    LCN2 Human

    Description:

    Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant

    Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.

    Product # :

    ENZ-783

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    Description

    LCN2 Human Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains consisting of two 178 amino acids and having a molecular mass of 41.0kDa.

    Source

    Escherichia Coli.

    Formulation

    LCN2 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, with 0.05 % Tween-20.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 1,000,000 IU/mg.

    More Info

    • Introduction

      Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
      They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

    • Synonyms

      Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LCN2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCN2 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.

    • Amino Acid Sequence

      QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG LPENHIVFPV PIDQCIDG

    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.

    Human Lcn2
  • View Data Sheet

    Name :

    Periostin Human, HEK

    Description:

    Periostin Human Recombinant, HEK

    OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    Product # :

    CYT-835

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    Periostin was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% trehalose.

    Purity

    Greater than 38.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
      Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.

    • Synonyms

      OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    • 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.

    • Solubility

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

    • Amino Acid Sequence

      NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH H.

    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.

    Periostin Human Hek
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