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Search results

1000 results found for “Microfibrillar Associated Protein”

Name

Description

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  • View Data Sheet

    Name :

    NELFE Human

    Description:

    Negative Elongation Factor Complex Member E Human Recombinant

    Negative elongation factor E, NELF-E, RNA-binding protein RD, NELFE, RD, RDBP, Negative Elongation Factor Complex Member E, D6S45, RDP.

    Product # :

    PRO-1968

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    Description

    NELFE Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-380) and having a molecular mass of 45.6 kDa.NELFE is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NELFE solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NELFE is a vital component of NELF complex which represses RNA polymerase II transcript elongation. NELFE is similar to nuclear RNA-binding proteins but does not bind RNA. NELFE contains a tract of alternating basic and acidic residues, mainly arginine and aspartic acid.

    • Synonyms

      Negative elongation factor E, NELF-E, RNA-binding protein RD, NELFE, RD, RDBP, Negative Elongation Factor Complex Member E, D6S45, RDP.

    • 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 MGSMLVIPPG LSEEEEALQK KFNKLKKKKK ALLALKKQSS SSTTSQGGVK RSLSEQPVMD TATATEQAKQ LVKSGAISAI KAETKNSGFK RSRTLEGKLK DPEKGPVPTF QPFQRSISAD DDLQESSRRP QRKSLYESFV SSSDRLRELG PDGEEAEGPG AGDGPPRSFD WGYEERSGAH SSASPPRSRS RDRSHERNRD RDRDRERDRD RDRDRDRERD RDRDRDRDRD RERDRDRERD RDRDREGPFR RSDSFPERRA PRKGNTLYVY GEDMTPTLLR GAFSPFGNII DLSMDPPRNC AFVTYEKMES ADQAVAELNG TQVESVQLKV NIARKQPMLD AATGKSVWGS LAVQNSPKGC HRDKRTQIVY SDDVYKENLV DGF.

    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.

    Nelfe Human
  • View Data Sheet

    Name :

    NMM Human

    Description:

    Non-Muscle Myosin-II Regulatory Light Chain Human Recombinant

    Non-Muscle Myosin-II Regulatory Light Chain, NMM.

    Product # :

    PRO-366

    Price :

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    Description

    Non-Muscle Myosin-II Regulatory Light Chain Human Recombinant full length expressed in E.coli.The NMM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMM protein at 0.2mg/ml in 20mM HEPES-KOH, pH7, 50mM NaCl, 1mM EDTA and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Assayed for phosphorilation by MLCK.

    More Info

    • Introduction

      Non muscle Myosins are required for cytokinesis at the end of cell division, when a contractile ring near the plasmalemma divides the cytoplasm of the daughter cells. They are involved in cytoplasmic streaming movements in tissues, and especially in activation of motile cells such as fibroblasts and macrophages. Activation of non-muscle myosin-II is achieved by phosphorylation of Ser33 in the motif KKRPQRATSN by a dedicated, Ca +2 Calmodulin regulated light chain kinase (MLCK).

    • Synonyms

      Non-Muscle Myosin-II Regulatory Light Chain, NMM.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS LGKNPTDAYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEATGTIQE DYLRELLTTM GDRFTDEEVD ELYREAPIDK KGNFNYIEFT RILKHGAKDK DD.

    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.

    Nmm Human
  • View Data Sheet

    Name :

    Protein-A/G, His

    Description:

    Protein A/G Recombinant, His Tag

    Product # :

    PRO-1927

    Price :

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH HHH.

    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.

    Protein A G His
  • View Data Sheet

    Name :

    GFAP Bovine

    Description:

    Glial Fibrillary Acidic Protein Bovine

    Glial fibrillary acidic protein, GFAP.

    Product # :

    PRO-2784

    Price :

    Quantity :

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    Description

    GFAP Bovine having a calculated molecular mass of 52 kDa, pI-5.4.

    Source

    Bovine spinal cord.

    Formulation

    GFAP 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

      Glial fibrillary acidic protein, GFAP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Background

      Glial fibrillary acidic protein (GFAP) is a key intermediate filament protein found predominantly in astrocytes, a type of glial cell in the central nervous system. While extensive research has been conducted on GFAP in rodents and humans, the study of GFAP in bovine brain tissue is an emerging area with potential for advancing our understanding of astrocytic function and neurological health in larger mammals. Bovine brains provide a unique model system due to their size and complexity, making them valuable for investigating astrocyte-specific functions. This research aims to provide a comprehensive exploration of GFAP in bovine brain tissue, shedding light on its functions and implications for neurological health.

      The primary objective of this research is to elucidate the role of GFAP in bovine brain tissue, particularly in astrocyte structure and function. In vitro and ex vivo experiments, utilizing bovine astrocyte cultures and brain tissue slices, will be conducted to investigate how GFAP contributes to astrocytic morphology, intracellular signaling, and response to neuronal injury or disease. Understanding these mechanisms is fundamental for deciphering the complexities of astrocyte biology in large mammalian brains.

      The second objective is to assess the relevance of bovine GFAP in neurodegenerative diseases and brain injuries. Studies involving bovine brain models of neurodegenerative conditions such as Alzheimer's disease or traumatic brain injury will be conducted to evaluate the role of GFAP in disease progression, neuroinflammation, and tissue repair. These investigations may provide valuable insights into potential therapeutic strategies for neurological disorders.

      The third objective is to explore the potential applications of bovine GFAP in biotechnology and medical research. Research will investigate the use of bovine astrocyte cultures as models for studying astrocyte-neuron interactions and for developing tissue engineering approaches for neurological repair and regeneration.

      By delving into the functions and roles of GFAP in bovine brain tissue, this research aims to expand our knowledge of astrocyte biology, its implications for neurological health, and its potential applications in biotechnology and medical research.

    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.

    Gfap Bovine
  • View Data Sheet

    Name :

    APOC1 Human

    Description:

    Apolipoprotein C-I Human Recombinant

    Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.

    Product # :

    CYT-812

    Price :

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    • sds-page

    Description

    APOC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids (27-83 a.a.) and having a molecular mass of 9.0kDa. APOC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    APOC1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    APOC1-sds-page - Product image 1

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    • Introduction

      Apolipoprotein C-I (APOC1) which expressed mainly in the liver is a part of the apolipoprotein C family. APOC1 which is usually found in plasma and responsible for the activation of esterified lechitin cholesterol takes an important part in the exchange of esterified cholesterol among lipoproteins and in removal of cholesterol from tissues. APOC1 is activated when monocytes differentiate into macrophages. APOC1 protein’s main role is to inhibit CETP by altering the electric charge of HDL molecules. APOC1 is also binds free fatty acids and reduces their intracellular esterification.

    • Synonyms

      Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.

    • 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 MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.

    • Background

      Apolipoprotein C-I Human Recombinant: Unraveling the Complexity of Lipid Regulation

      Abstract:

      Apolipoprotein C-I (ApoC-I) is a remarkable protein that plays a significant role in lipid metabolism and cardiovascular health. It is primarily synthesized in the liver and is associated with lipoproteins involved in lipid transport. This research paper aims to provide a comprehensive overview of ApoC-I human recombinant, shedding light on its physiological functions, production methods, and potential therapeutic applications. By delving into the intricacies of ApoC-I, we can gain valuable insights into its role as a key player in lipid regulation and its potential as a therapeutic target.

      Introduction:

      The prevalence of lipid disorders and cardiovascular diseases necessitates a deeper understanding of the mechanisms governing lipid metabolism. ApoC-I, a critical component of lipoproteins, offers unique insights into the regulation of lipid levels and its implications for cardiovascular health.

      Structure and Function of Apolipoprotein C-I:

      ApoC-I exhibits a complex molecular structure, comprising functional domains that enable its interaction with lipoproteins. It plays a crucial role in regulating lipoprotein metabolism by inhibiting the activity of lipoprotein lipase and modulating the clearance of triglyceride-rich lipoproteins.

      Regulation of Apolipoprotein C-I Expression:

      The synthesis and secretion of ApoC-I are tightly regulated processes influenced by various factors, including nutritional status and hormonal signals. Understanding the regulatory mechanisms underlying ApoC-I expression can provide insights into its role in maintaining lipid homeostasis.

      Apolipoprotein C-I and Cardiovascular Diseases:

      Dysregulation of ApoC-I has been associated with various lipid disorders and cardiovascular diseases. Altered levels of ApoC-I have been observed in conditions such as hypertriglyceridemia and atherosclerosis, highlighting its potential as a biomarker for cardiovascular risk assessment.

      Production of Apolipoprotein C-I Human Recombinant:

      Recombinant ApoC-I can be produced using advanced biotechnological approaches, including recombinant DNA technology and protein expression systems. These methods enable large-scale production, purification, and characterization of ApoC-I, facilitating its potential therapeutic applications.

      Therapeutic Potential of Apolipoprotein C-I Human Recombinant:

      Targeting ApoC-I opens up exciting avenues for therapeutic interventions in lipid disorders and cardiovascular diseases. Modulating ApoC-I expression or function holds promise for restoring lipid balance and reducing the risk of cardiovascular complications.

      Conclusion:

      Apolipoprotein C-I human recombinant represents a fascinating area of research in the field of lipid metabolism and cardiovascular health. By unraveling the intricate interplay between ApoC-I, lipoproteins, and cardiovascular diseases, we can pave the way for novel therapeutic strategies and improved risk assessment. Further studies are required to fully understand the therapeutic potential of ApoC-I human recombinant and translate these findings into clinical applications.

      What is the molecular weight/Mw of APOC1 Protein?
      APOC1 Protein has a total Mw of 9kDa.

      What is the source or expression system of APOC1 Protein?
      Escherichia Coli.

      What is the Purity of APOC1 Protein?
      APOC1 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOC1 Protein?
      The biological functionality of APOC1 Protein will be determined in the future.

      What is the amino acid sequence of APOC1 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.

      What applications can APOC1 Protein be used in?
      APOC1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOC1 Protein?
      The endotoxin level is minimal, APOC1 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.

    Apoc1 Human
  • View Data Sheet

    Name :

    MAD2L1 Human

    Description:

    MAD2 Mitotic Arrest Deficient-Like 1 Human Recombinant

    Mitotic spindle assembly checkpoint protein MAD2A, HsMAD2, Mitotic arrest deficient 2-like protein 1, MAD2-like protein 1, MAD2L1, MAD2.

    Product # :

    PRO-934

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    Description

    MAD2L1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205 a.a.) and having a molecular mass of 25.7kDa.MAD2L1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAD2L1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAD2L1-binding protein (MAD2L1) is a component of the mitotic spindle assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. MAD2L1 is vital for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate.

    • Synonyms

      Mitotic spindle assembly checkpoint protein MAD2A, HsMAD2, Mitotic arrest deficient 2-like protein 1, MAD2-like protein 1, MAD2L1, MAD2.

    • 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 MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG LTLLVTTDLE LIKYLNNVVE QLKDWLYKCS VQKLVVVISN IESGEVLERW QFDIECDKTA KDDSAPREKS QKAIQDEIRS VIRQITATVT FLPLLEVSCS FDLLIYTDKD LVVPEKWEES GPQFITNSEE VRLRSFTTTI HKVNSMVAYK IPVND.

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    Mad2L1 Human
  • View Data Sheet

    Name :

    MIA Human

    Description:

    Melanoma Inhibitory Activity Human Recombinant

    Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

    Product # :

    CYT-310

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    Description

    Melanoma Inhibitory Activity Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain consisting of 108 amino having a total molecular mass of 12237 Dalton.The MIA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Potassium-phosphate pH=7 and 150mM potassium chloride.

    Purity

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

    Biological Activity

    The biological activity is calculated by the inhibiting effect on the invasion of Mel In Tumor cells and found active in Mel In assay.

    More Info

    • Introduction

      The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain.
      MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.

    • Synonyms

      Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Agrees with the sequence of native MIA human with an addition N-terminal Methionine residue.
      MGPMPKLADRKLCADQECSSHPISMAVALQDYMAPDCRFLTIHRGQVV
      YVFSLKGRGRFLWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKVDVKT
      DKWDFYCQ.

    • Protein content

      UV spectroscopy at 280 nm using the absorption coefficient of 19300 M-1cm-1.

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    Mia Human
  • View Data Sheet

    Name :

    SERPINA3 Human

    Description:

    Alpha-1 AntiChymotrypsin Human

    Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    Product # :

    PRO-378

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    Description

    Human Alpha-1 AntiChymotrypsin produced from normal human serum having a molecular mass of 68kDa.

    Source

    Human Serum.

    Formulation

    Lyophilized from 0.02M Tris-buffer,pH-7.5 and 0.15M Nacl.

    Purity

    Greater than 90.0%.

    More Info

    • Introduction

      Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1- ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
      Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT.

    • Synonyms

      Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Human SERPINA3 although stable at room temperature for 3 weeks, should be stored between 2-8°C. Do not freeze.

    • Solubility

      It is recommended to reconstitute the lyophilized human A1ACT in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.

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    Serpina3 Human
  • View Data Sheet

    Name :

    RBP4 Mouse

    Description:

    Retinol Binding Protein-4 Mouse Recombinant, BioActive

    Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    Product # :

    CYT-1158

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    Description

    RBP4 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 191 amino acids (19-201 a.a) and having a molecular mass of 22.4kDa. RBP4 is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The RBP4 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Retinol Binding Protein-4 or RBP4, is the retinol currier protein in the plasma. RBP4 takes part on the conversion of retinol to the stable and soluble retinol complex in the plasma. RBP4 carries retinol from the liver tissue where its store to peripheral tissues. RBP-retinol complex has interactions with transthyretin in the plasma, thus prevents its loss by filtration in the kidney.

    • Synonyms

      Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    • 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

      ERDCRVSSFR VKENFDKARF SGLWYAIAKK DPEGLFLQDN IIAEFSVDEK GHMSATAKGR VRLLSNWEVC ADMVGTFTDT EDPAKFKMKY WGVASFLQRG NDDHWIIDTD YDTFALQYSC RLQNLDGTCA DSYSFVFSRD PNGLSPETRR LVRQRQEELC LERQYRWIEH NGYCQSRPSR NSLLEHHHHH H.

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    Rbp4 Mouse
  • View Data Sheet

    Name :

    TOMM20 Human

    Description:

    Translocase Of Outer Mitochondrial Membrane 20 Human Recombinant

    Mmitochondrial import receptor subunit TOM20 homolog, TOMM20, MAS20, MOM19, KIAA0016, Outer mitochondrial membrane receptor Tom20, Mitochondrial 20 kDa outer membrane protein.

    Product # :

    PRO-1471

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    Description

    TOMM20 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (25-145) and having a molecular mass of 16.2 kDa. TOMM20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TOMM20 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mmitochondrial import receptor subunit TOMM20 homolog (TOMM20) is a member of the Tom20 family. The Tom machinery consists of import receptors for the initial binding of cytosolically synthesized preproteins and a general import pore (GIP) for the membrane translocation of various preproteins into the mitochondria. TOMM20 acts as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.

    • Synonyms

      Mmitochondrial import receptor subunit TOM20 homolog, TOMM20, MAS20, MOM19, KIAA0016, Outer mitochondrial membrane receptor Tom20, Mitochondrial 20 kDa outer membrane protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSDRKRRSD PNFKNRLRER RKKQKLAKER AGLSKLPDLK DAEAVQKFFL EEIQLGEELL AQGEYEKGVD HLTNAIAVCG QPQQLLQVLQ QTLPPPVFQM LLTKLPTISQ RIVSAQSLAE DDVE.

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    Tomm20 Human
  • View Data Sheet

    Name :

    EFNA1 Human

    Description:

    Ephrin A1 Human Recombinant

    Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    Product # :

    PRO-971

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    Description

    EFNA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (19-182) and having a molecular mass of 21.6 kDa.EFNA1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EFNA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

    • Synonyms

      Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    • 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 MDRHTVFWNS SNPKFRNEDY TIHVQLNDYV DIICPHYEDH SVADAAMEQY ILYLVEHEEY QLCQPQSKDQ VRWQCNRPSA KHGPEKLSEK FQRFTPFTLG KEFKEGHSYY YISKPIHQHE DRCLRLKVTV SGKITHSPQA HVNPQEKRLA ADDPEVRVLH SIGHS

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    Efna1 Human
  • View Data Sheet

    Name :

    JAZF1 Human

    Description:

    JAZF zinc finger 1 Human Recombinant

    Juxtaposed with another zinc finger protein 1 , TAK1-interacting protein 27, Zinc finger protein 802, JAZF1, TIP27, ZNF802, JAZF zinc finger 1, Juxtaposed With Another Zinc Finger Gene 1.

    Product # :

    PRO-1444

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    Description

    JAZF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (1-243 a.a) and having a molecular mass of 29.5kDa.JAZF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    JAZF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      JAZF zinc finger 1 (JAZF1) is a nuclear protein with 3 C2H2-type zinc fingers, which functions as a transcriptional repressor. Chromosomal anomalies involving the JAZF1 are linked with endometrial stromal tumors. Alternatively spliced variants which encode different protein isoforms have been described; though, not all variants have been fully characterized.

    • Synonyms

      Juxtaposed with another zinc finger protein 1 , TAK1-interacting protein 27, Zinc finger protein 802, JAZF1, TIP27, ZNF802, JAZF zinc finger 1, Juxtaposed With Another Zinc Finger Gene 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTGIAAA SFFSNTCRFG GCGLHFPTLA DLIEHIEDNH IDTDPRVLEK QELQQPTYVA LSYINRFMTD AARREQESLK KKIQPKLSLT LSSSVSRGNV STPPRHSSGS LTPPVTPPIT PSSSFRSSTP TGSEYDEEEV DYEESDSDES WTTESAISSE AILSSMCMNG GEEKPFACPV PGCKKRYKNV NGIKYHAKNG HRTQIRVRKP FKCRCGKSYK TAQGLRHHTI NFHPPVSAEI IRKMQQ

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    Jazf1 Human
  • View Data Sheet

    Name :

    WB123 Wuchereria

    Description:

    Wb123 Wuchereria Bancrofti Recombinant

    Product # :

    PRO-2820

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    Description

    The E.Coli derived Recombinant Wuchereria Bancrofti Wb123 is a 43kDa protein which is fused to a His tag in N-terminus.

    Source

    Escherichia Coli.

    Formulation

    25mM K2CO3 and PBS.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Background

      One of the key antigens associated with Wuchereria bancrofti is Wb123, a protein that has emerged as a potential diagnostic marker for early infection and a target for vaccine development. Wb123 is a highly immunogenic protein that elicits a strong antibody response in individuals infected with Wuchereria bancrofti. Recombinant Wb123 is utilized in serological assays to detect specific IgG4 antibodies, which are indicative of active infection, particularly in the early stages before clinical symptoms manifest. Studies using rWb123 have demonstrated its high sensitivity and specificity, making it a valuable tool for diagnosing lymphatic filariasis and monitoring the effectiveness of mass drug administration (MDA) programs aimed at eliminating the disease.

    • Specificity

      Immunoassay.

    • Purification Method

      Purified by proprietary chromatographic technique.

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    Wuchereria Bancrofti Wb123
  • View Data Sheet

    Name :

    DNAJC24 Human

    Description:

    DnaJ (Hsp40) Homolog, Subfamily C, Member 24 Human Recombinant

    DnaJ homolog subfamily C member 24, DNAJC24, DPH4, JJJ3, ZCSL3, CSL-type zinc finger-containing protein 3, Diphthamide biosynthesis protein 4.

    Product # :

    HSP-056

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    Description

    DNAJC24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-149 a.a.) and having a molecular mass of 19.5kDa. DNAJC24 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DNAJC24 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      DnaJ homolog subfamily C member 24 (DNAJC24) belongs to the ZCSL family of proteins and each contain one DPH-type zinc finger. DNAJC24 is involved in the synthesis of diphthamide, a protein found on translation elongation factor EF-2 which is the target of bacterial ADP-ribosylating toxins. DNAJC24 stimulates the ATPase activity of few Hsp70-type chaperones. DNAJC24 detected in heart, brain, spleen, lung, liver, kidney and testis.

    • Synonyms

      DnaJ homolog subfamily C member 24, DNAJC24, DPH4, JJJ3, ZCSL3, CSL-type zinc finger-containing protein 3, Diphthamide biosynthesis protein 4.

    • 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 MGSMMAVEQM PKKDWYSILG ADPSANISDL KQKYQKLILM YHPDKQSTDV PAGTVEECVQ KFIEIDQAWK ILGNEETKRE YDLQRCEDDL RNVGPVDAQV YLEEMSWNEG DHSFYLSCRC GGKYSVSKDE AEEVSLISCD TCSLIIELLH YN.

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    Dnajc24 Human
  • View Data Sheet

    Name :

    ARHGDIB Human

    Description:

    Rho GDP Dissociation Inhibitor (GDI) Beta Human Recombinant

    Rho GDP dissociation inhibitor (GDI) beta, Rho GDI 2, Rho-GDI beta, GDIA2, GDID4, Ly-GDI, RAP1GN1.

    Product # :

    PRO-1067

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    Description

    ARHGDIB Human Recombinant produced in E. coli is a single polypeptide chain containing 428 amino acids (1-201) and having a molecular mass of 49.4kDa.ARHGDIB is fused to a 227 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ARHGDIB solution (1mg/1ml) contains phosphate-buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Members of the Rho (or ARH) protein family and other Ras-related small GTP-binding proteins are involved in various cellular procedures, such as cell cytoskeletal organization, secretion, proliferation, and signaling. The GTPBPs are active only in the GTP-bound state. At least 3 types of proteins firmly regulate cycling between the GTP-bound and GDP-bound states: GDP-dissociation inhibitors (GDIs), GTPase-activating proteins (GAPs) and guanine nucleotide-releasing factors (GRFs). ARHGDIB and the other GDIs lower the level of GDP dissociation from Ras-like GTPases.

    • Synonyms

      Rho GDP dissociation inhibitor (GDI) beta, Rho GDI 2, Rho-GDI beta, GDIA2, GDID4, Ly-GDI, RAP1GN1.

    • 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

      MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSHMTE KAPEPHVEED DDDELDSKLN YKPPPQKSLK ELQEMDKDDE SLIKYKKTLL GDGPVVTDPK APNVVVTRLT LVCESAPGPI TMDLTGDLEA LKKETIVLKE GSEYRVKIHF KVNRDIVSGL KYVQHTYRTG VKVDKATFMV GSYGPRPEEY EFLTPVEEAP KGMLARGTYH NKSFFTDDDK QDHLSWEWNL SIKKEWTE

    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.

    Arhgdib Human
  • View Data Sheet

    Name :

    MCTS1 Human

    Description:

    Malignant T-Cell-Amplified Sequence 1 Human Recombinant

    MCT-1, MCT1, Malignant T-cell-amplified sequence 1, Multiple copies T-cell malignancies.

    Product # :

    PRO-1387

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    Description

    MCTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 204 amino acids (1-181 a.a.) and having a molecular mass of 22.9kDa. MCTF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    MCTF1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Malignant T cell amplified sequence 1 (MCTS1) is an Anti-oncogene which takes part in cell cycle regulation by means of decreasing cell doubling time and encouraging-dependent growth and also by shorting the duration of G1 transit time and G1/S transition. MCTS1 also plays a role as translation enhancer. MCTS1 recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, thereupon altering the mRNA translation profile; Up-regulates protein levels of BCL2L2, TFDP1, MRE11A, CCND1 and E2F1, while mRNA levels remains constant.

    • Synonyms

      MCT-1, MCT1, Malignant T-cell-amplified sequence 1, Multiple copies T-cell malignancies.

    • 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 MGSMFKKFDE KENVSNCIQL KTSVIKGIKN QLIEQFPGIE PWLNQIMPKK DPVKIVRCHE HIEILTVNGE LLFFRQREGP FYPTLRLLHK YPFILPHQQV DKGAIKFVLS GANIMCPGLT SPGAKLYPAA VDTIVAIMAE GKQHALCVGV MKMSAEDIEK VNKGIGIENI HYLNDGLWHM KTYK.

    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.

    Mcts1 Human
  • View Data Sheet

    Name :

    BMP8B Antibody

    Description:

    Bone Morphogenetic protein-8b, Mouse Anti Human

    Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

    Product # :

    ANT-558

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    Formulation

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

    More Info

    • Introduction

      Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.

    • Synonyms

      Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human BMP8B mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human BMP8B protein 264-402 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT13E6AT.

    • Applications

      BMP8B antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      BMP8B antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Bmp8B Antibody
  • View Data Sheet

    Name :

    MAP2K3 Human

    Description:

    Mitogen-Activated Protein Kinase Kinase 3 Human Recombinant

    Dual specificity mitogen-activated protein kinase kinase 3, MAP kinase kinase 3, MAPKK 3, MAPK/ERK kinase 3, MEK 3, MAP2K3, MEK3, MKK3, PRKMK3.

    Product # :

    PKA-004

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    Description

    MAP2K3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 338 amino acids (1-318) and having a molecular mass of 38.3kDa. MAP2K3 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAP2K3 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dual specificity mitogen-activated protein kinase kinase 3 (MAP2K3) is a dual specificity protein kinase which is a member of the MAP kinase kinase family. MAP2K3 is activated by mitogenic and environmental stress, and participates in the MAP kinase-mediated signaling cascade. MAP2K3 phosphorylates and consequently activates MAPK14/p38-MAPK.

    • Synonyms

      Dual specificity mitogen-activated protein kinase kinase 3, MAP kinase kinase 3, MAPKK 3, MAPK/ERK kinase 3, MEK 3, MAP2K3, MEK3, MKK3, PRKMK3.

    • 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 MSKPPAPNPT PPRNLDSRTF ITIGDRNFEV EADDLVTISE LGRGAYGVVE KVRHAQSGTI MAVKRIRATV NSQEQKRLLM DLDINMRTVD CFYTVTFYGA LFREGDVWIC MELMDTSLDK FYRKVLDKNM TIPEDILGEI AVSIVRALEH LHSKLSVIHR DVKPSNVLIN KEGHVKMCDF GISGYLVDSV AKTMDAGCKP YMAPERINPE LNQKGYNVKS DVWSLGITMI EMAILRFPYE SWGTPFQQLK QVVEEPSPQL PADRFSPEFV DFTAQCLRKN PAERMSYLEL MEHPFFTLHK TKKTDIAAFV KEILGEDS.

    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.

    Map2K3 Human
  • View Data Sheet

    Name :

    CREG1 Mouse

    Description:

    Cellular Repressor of E1A-Stimulated Genes 1 Mouse Recombinant

    Protein CREG1, Cellular repressor of E1A-stimulated genes 1, Creg1, Creg.

    Product # :

    PRO-2387

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    Description

    CREG1 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (32-220) and having a molecular mass of 24kDa. CREG1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CREG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.

    • Synonyms

      Protein CREG1, Cellular repressor of E1A-stimulated genes 1, Creg1, Creg.

    • 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 MGSMRGGRDH GDWDVDRRLP PLPPREDGPR VARFVTHVSD WGSLATISTI KEVRGWPFAD IISISDGPPG EGTGEPYMYL SPLQQAVSDL QENPEATLTM SLAQTVYCRN HGFDPQSPLC VHIMMSGTVT KVNKTEEDYA RDSLFVRHPE MKHWPSSHNW FFAKLKISRI WVLDYFGGPK VVTPEEYFNV TLQ.

    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.

    Creg1 Mouse
  • View Data Sheet

    Name :

    RNF181 Human

    Description:

    Ring Finger Protein 181 Human Recombinant

    Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    Product # :

    PRO-1218

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    Description

    RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RNF181 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).

    • Synonyms

      Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    • 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 MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.

    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.

    Rnf181 Human
  • View Data Sheet

    Name :

    SNCA 1-95, Human

    Description:

    Alpha-Synuclein 1-95 Human Recombinant

    SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.

    Product # :

    PRO-2625

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    Description

    SNCA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (1-95 a.a.) and having a molecular mass of 9.3kDa.SNCA is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SNCA protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 7.5) and 0.1 M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Alpha-synuclein or SNCA is a synuclein protein. SNCA mainly found in the brain, small concentration of the protein can also be located in other tissues such as heart and muscle. When looking in the brain tissue, SNCA is located in the end of the neuron, in an area called presynaptic terminal. In the presynaptic terminal SNCA has interaction with phospholipids & other proteins. Neurotransmitters are released from the synaptic vesicles in the Presynaptic terminals and act as messengers. Once released, the neurotransmitters send signals across the neurons that are crucial for the brain’s operation.

    • Synonyms

      SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFV

    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.

    Alpha Synuclein
  • View Data Sheet

    Name :

    MUC1 ( 47 a.a.) Human

    Description:

    Mucin-1 (47 a.a.) Human Recombinant

    KL-6, ADMCKD1, ADMCKD, Ca15-3, CD227.

    Product # :

    PRO-2829

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    Description

    The MUC1Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MUC1His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 47 amino acid residues of the MUC1Human, 1094-1140 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

      KL-6, ADMCKD1, ADMCKD, Ca15-3, CD227.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized MUC1at -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

      L R P G S V V V Q L T L A F R E G T I N V H D V E T Q F N Q Y K T E A A S R Y N L T I S D V

      S G

    • Background

      Human Mucin-1 also known as MUC1, is a glycoprotein with extensive O-linked glycosylation of its extracellular domain.

      MUC1 has alpha and beta subunits that form a heterodimeric complex.

      The N-terminal alpha subunit roles in cell-adhesion and the C-terminal beta subunit is involved in cell signaling.

      Mucins line the apical surface of epithelial cells in the stomach, lungs, intestines, eyes and other tissues.

      Mucins protect the body from infection by pathogen binding to oligosaccharides in the extracellular domain, preventing the pathogen from reaching the cell surface.

      Overexpression of MUC1 can be related to various cancers.

    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.

    Muc1 Human
  • View Data Sheet

    Name :

    CNOT8 Human

    Description:

    CCR4-NOT Transcription Complex, Subunit 8 Human Recombinant

    CCR4-NOT transcription complex subunit 8, CAF1, CALIF, hCAF1, POP2, CAF1-like protein, CAF2, CCR4-associated factor 8, Caf1b, CNOT8.

    Product # :

    PRO-1517

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    Description

    CNOT8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 35.9 kDa.CNOT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CNOT8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCR4-NOT Transcription Complex, Subunit 8 (CNOT8) is a part of the CAF1 family. CNOT8 is a ubiquitous transcription factor necessary for a varied set of processes and functions as part of the CCR-NOT complex. The CCR4-NOT complex which functions as general transcription regulation complex binds BTG2 and holds CHAF1A, CHAF1B, CNOT1, CNOT2, CNOT3, CNOT4, CNOT6 and CNOT8

    • Synonyms

      CCR4-NOT transcription complex subunit 8, CAF1, CALIF, hCAF1, POP2, CAF1-like protein, CAF2, CCR4-associated factor 8, Caf1b, CNOT8.

    • 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 MGSMPAALVE NSQVICEVWA SNLEEEMRKI REIVLSYSYI AMDTEFPGVV VRPIGEFRSS IDYQYQLLRC NVDLLKIIQL GLTFTNEKGE YPSGINTWQF NFKFNLTEDM YSQDSIDLLA NSGLQFQKHE EEGIDTLHFA ELLMTSGVVL CDNVKWLSFH SGYDFGYMVK LLTDSRLPEE EHEFFHILNL FFPSIYDVKY LMKSCKNLKG GLQEVADQLD LQRIGRQHQA GSDSLLTGMA FFRMKELFFE DSIDDAKYCG RLYGLGTGVA QKQNEDVDSA QEKMSILAII NNMQQ.

    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.

    Cnot8 Human
  • View Data Sheet

    Name :

    SNCA Human

    Description:

    Alpha Synuclein Human Recombinant

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

    Product # :

    PRO-393

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    Description

    a-Synuclein Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (Real molecular weight on SDS-PAGE will be shift up). The Recombinant Human a-Synuclein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl and 1mM MgCl2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.

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

    Snca Human
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