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Search results

1000 results found for “myelin basic protein”

Name

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  • View Data Sheet

    Name :

    CEA Protein

    Description:

    Carcinoembryonic Antigen Human

    CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    Product # :

    PRO-2801

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    Description

    CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.

    Source

    Liver tissue.

    Formulation

    CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    • 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.

    • Applications

      Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.

    • Background

      Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.

      Structural Complexity of CEA:

      CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.

      CEA in Cancer Biology:

      CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.

      Beyond Cancer: CEA in Development and Inflammation:

      While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.

      CEA as a Diagnostic and Therapeutic Target:

      The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.

    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.

    Cea Human
  • View Data Sheet

    Name :

    METRN Mouse

    Description:

    Meteorin Mouse Recombinant

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

    Product # :

    PRO-2241

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Metrn Mouse
  • View Data Sheet

    Name :

    FABP4 Protein

    Description:

    Fatty Acid Binding Protein 4 Human Recombinant

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

    Product # :

    PRO-416

    Price :

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    Description

    14.7kDa protein containing 132 amino acid residues.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH4.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered 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

      0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDVI TIKSESTFKN TEISFILGQE FDEVTADDRK VKSTITLDGG VLVHVQKWDG KSTTIKRKRE DDKLVVECVM KGVTSTRVYE RA.

    • Specificity

      The amino acid sequence of the recombinant human FABP4 is 100% homologous to the amino acid sequence of the human FABP4.

    • Purification Method

      Two-step procedure using size exclusion chromatography before and after refolding.

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

    Fabp4 Human
  • View Data Sheet

    Name :

    RBP4 Protein

    Description:

    Retinol Binding Protein-4 Human

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

    Product # :

    CYT-1218

    Price :

    Quantity :

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    Description

    RBP4 Human produced in Pooled human plasma can be used as a calibrator in immunoassays. Immunoreactivity was checked using monoclonal antibodies specific to RBP4.

    Source

    Human Plasma.

    Formulation

    RBP4 was lyophilized from PBS, 150mM NaCl, and 10mM K-phosphate, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Retinol Binding Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RBP4 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 RBP4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Retinol Binding Protein 4 (RBP4) is a multifunctional protein that plays a crucial role in the transport of retinol (vitamin A) in the bloodstream. Beyond its traditional role in vitamin A metabolism, RBP4 has emerged as a key player in various physiological processes and pathological conditions. This research endeavors to explore the diverse facets of RBP4 in human biology, shedding light on its physiological functions, regulatory mechanisms, and implications in health and disease.

      Physiological Functions:

      At its core, RBP4 acts as a carrier protein, shuttling retinol from the liver, where it is stored, to peripheral tissues where it is utilized. Retinol is vital for vision, immune function, growth, and development, making RBP4 an essential component in these processes. By regulating the availability of retinol, RBP4 contributes significantly to maintaining normal vision, immune responses, and cellular differentiation, particularly in epithelial tissues.

      Metabolic Significance:

      Research has unveiled RBP4’s role in metabolic regulation. It has been associated with insulin resistance, a hallmark of type 2 diabetes mellitus. Elevated RBP4 levels are observed in individuals with obesity and insulin resistance, implicating its involvement in metabolic disorders. Understanding the interplay between RBP4, insulin signaling, and glucose metabolism is crucial for deciphering the complexities of diabetes and metabolic syndrome.

      Immunological Implications:

      Beyond its metabolic functions, RBP4 has been implicated in immune responses. Studies have suggested its involvement in modulating inflammatory processes and immune cell functions. By influencing immune cell differentiation and cytokine production, RBP4 may play a role in both immune defense and autoimmune disorders. Investigating these immunological implications provides insights into the crosstalk between metabolic and immune pathways.

      Genetic and Environmental Influences:

      Genetic variations and environmental factors, such as diet and lifestyle, can impact RBP4 levels and functions. Research into these influences is essential for understanding individual susceptibility to metabolic disorders and inflammatory conditions. Genetic studies shed light on the hereditary aspects of RBP4 regulation, providing valuable information for personalized medicine approaches.

      Clinical Relevance:

      RBP4’s involvement in various diseases, including diabetes, cardiovascular diseases, and certain cancers, underscores its clinical relevance. It serves as a potential biomarker for metabolic dysregulation and a target for therapeutic interventions. Moreover, RBP4-targeted therapies are being explored for their potential in managing metabolic disorders and related complications.

      Conclusion:

      RBP4, once primarily recognized for its role in vitamin A transport, has evolved into a multifaceted protein with intricate roles in metabolism, immunity, and disease. Its functions extend far beyond being a mere carrier of retinol, influencing diverse physiological processes and serving as a nexus between metabolic health and immunological responses. Unraveling the complexities of RBP4 opens avenues for understanding diseases like diabetes and offers promising prospects for innovative therapies, emphasizing its significance in human biology and 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.

    Rbp4 Protein
  • View Data Sheet

    Name :

    MYBPC3 Human

    Description:

    Myosin Binding Protein C, Cardiac Human Recombinant

    Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.

    Product # :

    PRO-2292

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    Description

    MYBPC3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Phe271) containing 281 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 29.6kDa.

    Source

    Escherichia Coli.

    Formulation

    MYBPC3 was filtered (0.4µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin Binding Protein C, Cardiac (MYBPC3) is the cardiac isoform of myosin-binding protein C expressed exclusively in heart muscle. Myosin-binding protein C is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. Regulatory phosphorylation of the cardiac isoform in vivo by cAMP-dependent protein kinase upon adrenergic stimulation may be associated with modulation of cardiac contraction. MYBPC3 gene mutations are one of the causes of familial hypertrophic cardiomyopathy. In vitro MYBPC3 binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. MYBPC3 may modulate muscle contraction or it may have a more structural role.

    • Synonyms

      Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.

    • 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. MYBPC3 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASMPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS ASNKYGLATE GTRHTLTVRE VGPADQGSYA VIAGSSKVKF DLKVIEAEKA EPMLAPAPAP AEATGAPGEA PAPAAELGES APSPKGSSSA ALNGPTPGAP DDPIGLFVMR PQDGEVTVGG SITFSARVAG ASLLKPPVVK WFKGKWVDLS SKVGQHLQLH DSYDRASKVY LFELHITDAQ PAFTGSYRCE VSTKDKFDCS NFNLTVHEAM GTGDLDLLSA F.

    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.

    Mybpc3 Human
  • View Data Sheet

    Name :

    GADD45B Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Beta Human Recombinant

    MYD118, GADD45BETA, GADD45B, Growth arrest and DNA-damage-inducible protein GADD45 beta, Myeloid differentiation primary response protein MyD118, Negative growth regulatory protein MyD118, DKFZp566B133.

    Product # :

    PRO-563

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    Description

    GADD45B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 17.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    The GADD45B protein solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GADD45B is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45B reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45B is involved in the regulation of growth and apoptosis. GADD45b takes part during chondrocyte terminal differentiation and mediates MMP-13 gene expression. GADD45 in B cells is induced by CD40 via a mechanism that involves NF-kappa B and that induction suppresses Fas-mediated killing. GADD45b is down-regulated in most cases of hepatocellular carcinoma (HCC), and is a molecular marker in the diagnosis of HCC and as a possible therapeutic target.

    • Synonyms

      MYD118, GADD45BETA, GADD45B, Growth arrest and DNA-damage-inducible protein GADD45 beta, Myeloid differentiation primary response protein MyD118, Negative growth regulatory protein MyD118, DKFZp566B133.

    • 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

      MTLEELVACD NAAQKMQTVT AAVEELLVAA QRQDRLTVGV YESAKLMNVD PDSVVLCLLA IDEEEEDDIA LQIHFTLIQS FCCDNDINIV
      RVSGMQRLAQ LLGEPAETQG TTEARDLHCL LVTNPHTDAW KSHGLVEVAS YCEESRGNNQ WVPYISLQER.

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    Gadd45B Human
  • View Data Sheet

    Name :

    MECOM Human

    Description:

    MDS1 And EVI1 Complex Locus Human Recombinant

    MDS1 And EVI1 Complex Locus, Ecotropic Virus Integration Site 1 Protein Homolog, Myelodysplasia Syndrome-Associated Protein 1, AML1-EVI-1, MDS1-EVI1, EVI1, MDS1, PRDM3, AML1-EVI-1 Fusion Protein, MDS1 And EVI1 Complex Locus Protein EVI1, MDS1 And EVI1 Complex Locus Protein MDS1, Oncogene EVI1, Zinc Finger Protein Evi1.

    Product # :

    PRO-1766

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    Description

    MECOM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-169 a.a) and having a molecular mass of 21.1kDa.MECOM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MECOM protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      MDS1 is a transcriptional regulator and oncoprotein which takes part in hematopoiesis, development, cell differentiation, apoptosis and proliferation. MDS1 is able to interact with CTBP1, SMAD3, CREBBP, KAT2B, MAPK8, and MAPK9. Overexpression, as a result of translocation with the AML1 gene, is known to cause leukemia. A number of transcript variants encoding several different isoforms were found.

    • Synonyms

      MDS1 And EVI1 Complex Locus, Ecotropic Virus Integration Site 1 Protein Homolog, Myelodysplasia Syndrome-Associated Protein 1, AML1-EVI-1, MDS1-EVI1, EVI1, MDS1, PRDM3, AML1-EVI-1 Fusion Protein, MDS1 And EVI1 Complex Locus Protein EVI1, MDS1 And EVI1 Complex Locus Protein MDS1, Oncogene EVI1, Zinc Finger Protein Evi1.

    • 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 MGSMRSKGRA RKLATNNECV YGNYPEIPLE EMPDADGVAS TPSLNIQEPC SPATSSEAFT PKEGSPYKAP IYIPDDIPIP AEFELRESNM PGAGLGIWTK RKIEVGEKFG PYVGEQRSNL KDPSYGWEVH LPRSRRVSVH SWLYLGKRSS DVGIAFSQAD VYMPGLQCAF LS

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    Mecom Human
  • View Data Sheet

    Name :

    BATF Human

    Description:

    Basic Leucine Zipper Transcription Factor Human Recombinant

    Basic leucine zipper transcriptional factor ATF-like, B-cell-activating transcription factor, B-ATF, SF-HT-activated gene 2 protein, SFA-2, BATF, SFA2, BATF1.

    Product # :

    PRO-119

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    Description

    BATF Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids (1-125 a.a.) and having a molecular mass of 16.2kDa. The BATF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BATF solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl and 40% glycerol.

    Purity

    BATF purity was found to be greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BATF is a nuclear basic leucine zipper protein which is a member of the AP-1/ATF superfamily of transcription factors. BATF is intensely expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I. BATF acts as a tissue-specific modulator of the AP-1 transcription complex in human cells. Furthermore, BATF connects with IFP35 which is a leucine zipper protein that translocates to the nucleus following IFN treatment.

    • Synonyms

      Basic leucine zipper transcriptional factor ATF-like, B-cell-activating transcription factor, B-ATF, SF-HT-activated gene 2 protein, SFA-2, BATF, SFA2, BATF1.

    • Physical Appearance

      BATF is supplied as a 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 MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK ADTLHLESED LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST PSPPEVVYSA HAFHQPHVSS PRFQP.

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    Batf Human
  • View Data Sheet

    Name :

    GYPA Human

    Description:

    Glycophorin A Human Recombinant

    Glycophorin A (MNS Blood Group), Glycophorin A (MN Blood Group), Sialoglycoprotein Alpha, MN Sialoglycoprotein, PAS-2, GPA, Erythroid-Lineage-Specific Membrane Sialoglycoprotein, Recombinant Glycophorin A-B Miltenberger-DR, Glycophorin A (Includes MN Blood Group),  Mi.V Glycoprotein (24 AA), Glycophorin Sta Type C, Glycophorin A, GPA, Glycophorin Erik, Glycophorin MiV, Glycophorin SAT, CD235a Antigen, Glycophorin-A, HGpSta(C),  HGpMiXI, CD235a, GPErik, HGpMiV, GPSAT, MNS, MN.

    Product # :

    PRO-2426

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    Description

    GYPA Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 81 amino acids (20-91a.a.) and having a molecular mass of 9.1kDa. (Molecular size on SDS-PAGE under reducing conditions 18-28kDa).GYPA is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    GYPA protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycophorins A & B (GYPA &GYPB) are the main sialoglycoproteins of the human erythrocyte membrane which carry the antigenic determinants for the MN and Ss blood groups. Along with the M or N and S or s antigens which normally occur in all populations, approximately 40 related variant phenotypes were identified. These variants comprise all the variants of the Miltenberger complex and some isoforms of Sta, as well as Dantu, Sat, He, Mg, and deletion variants Ena, S-s-U- and Mk. GYPA is significant for the function of SLC4A1 and is necessary for high activity of SLC4A1. GYPA is involved in translocation of SLC4A1 to the plasma membrane. GYPA is also a receptor for: the influenza virus, Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans and is also a receptor for Hepatitis A virus (HAV).

    • Synonyms

      Glycophorin A (MNS Blood Group), Glycophorin A (MN Blood Group), Sialoglycoprotein Alpha, MN Sialoglycoprotein, PAS-2, GPA, Erythroid-Lineage-Specific Membrane Sialoglycoprotein, Recombinant Glycophorin A-B Miltenberger-DR, Glycophorin A (Includes MN Blood Group), Mi.V Glycoprotein (24 AA), Glycophorin Sta Type C, Glycophorin A, GPA, Glycophorin Erik, Glycophorin MiV, Glycophorin SAT, CD235a Antigen, Glycophorin-A, HGpSta(C), HGpMiXI, CD235a, GPErik, HGpMiV, GPSAT, MNS, MN.

    • 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

      ADPLSTTEVA MHTSTSSSVT KSYISSQTND THKRDTYAAT PRAHEVSEIS VRTVYPPEEE TGERVQLAHH FSEPEHHHHH H

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    Gypa Human
  • View Data Sheet

    Name :

    MYL7 Human

    Description:

    Myosin Light Chain 7 Human Recombinant

    Myosin light chain 7 regulatory, myosin light polypeptide 7 regulatory, Myosin light chain 2a myosin regulatory light chain 2 atrial isoform, MYL2A, MYLC2A.

    Product # :

    PRO-1109

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    Description

    MYL7 Human Recombinant produced in E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.0kDa.MYL7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MYL7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      MYL7 protein is an atrial isoform of myosin regulatory light chain 2 (MYL2). Myosin is a hexamer containing 4 light chains and 2 heavy chains. MYL7 is mainly expressed in adult atrial muscle.

    • Synonyms

      Myosin light chain 7 regulatory, myosin light polypeptide 7 regulatory, Myosin light chain 2a myosin regulatory light chain 2 atrial isoform, MYL2A, MYLC2A.

    • 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 MGSHMASRKA GTRGKVAATK QAQRGSSNVF SMFEQAQIQE FKEAFSCIDQ NRDGIICKAD LRETYSQLGK VSVPEEELDA MLQEGKGPIN FTVFLTLFGE KLNGTDPEEA ILSAFRMFDP SGKGVVNKDE FKQLLLTQAD KFSPAEVEQM FALTPMDLAG NIDYKSLCYI ITHGDEKEE

    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.

    Myl7 Human
  • View Data Sheet

    Name :

    HAND1 Human

    Description:

    Heart and Neural Crest Derivatives Expressed 1 Human Recombinant

    Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.

    Product # :

    PRO-1231

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    Description

    HAND1 Human Recombinant produced in E. coli is a single polypeptide chain containing 238 amino acids (1-215) and having a molecular mass of 26.0 kDa.HAND1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HAND1 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

      HAND1 is a member of the basic helix-loop-helix family of transcription factors. HAND1 is one of two HAND proteins, two closely related family members that are irregularly expressed in the emerging ventricular chambers and have a key part in cardiac morphogenesis. Operating in a complementary manner, they work in the development of the right ventricle and aortic arch arteries, implicating them as mediators of congenital heart disease. Furthermore, HAND1 is obligatory for early trophoblast differentiation.

    • Synonyms

      Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.

    • 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 MGSMNLVGSY AHHHHHHHPH PAHPMLHEPF LFGPASRCHQ ERPYFQSWLL SPADAAPDFP AGGPPPAAAA AATAYGPDAR PGQSPGRLEA LGGRLGRRKG SGPKKERRRT ESINSAFAEL RECIPNVPAD TKLSKIKTLR LATSYIAYLM DVLAKDAQSG DPEAFKAELK KADGGRESKR KRELQQHEGF PPALGPVEKR IKGRTGWPQQ VWALELNQ

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    Hand1 Human
  • View Data Sheet

    Name :

    TNNI1 Human Native

    Description:

    Troponin I Skeletal Muscle Human

    DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.

    Product # :

    PRO-2789

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    Description

    TNNI1 Native produced in Human skeletal is Immunological identity confirmed by reaction with monoclonal antibody that is specific for the Human Troponin I Skeletal Muscle. TNNI1 Native is purified by proprietary chromatographic technique.

    Source

    Human skeletal muscle.

    Formulation

    TNNI1 was lyophilized from 0.01M HCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Troponin I Skeletal Muscle although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI1 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 TNNI1 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Troponin I, specifically the skeletal muscle isoform encoded by the TNNI1 gene, is a crucial regulator of muscle contraction. It functions as part of the troponin complex, which controls the interaction between actin and myosin filaments during muscle contraction. While extensive research has been conducted on troponin I in the context of cardiac muscle and cardiac diseases, the study of native human skeletal muscle troponin I remains an important but relatively understudied area. This research aims to provide a comprehensive exploration of native human skeletal muscle troponin I (TNNI1), elucidating its functions, structural significance, and potential applications in musculoskeletal research and clinical medicine.

      The primary objective of this research is to elucidate the physiological role of native human skeletal muscle TNNI1 in muscle contraction. Experiments involving human skeletal muscle tissue samples and isolated muscle fibers will be conducted to investigate how TNNI1 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of skeletal muscle physiology and its implications for musculoskeletal health.

      The second objective is to assess the clinical relevance of native TNNI1 in muscle-related diseases. Clinical studies involving patients with various neuromuscular and muscle-wasting conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI1 as a biomarker. These investigations may provide valuable insights into the use of native TNNI1 in the early detection and management of muscle disorders.

      The third objective is to explore the potential applications of native TNNI1 in musculoskeletal research and therapeutic development. Research will investigate the use of native TNNI1-expressing cells and tissues as models for studying muscle disorders and for developing novel therapeutic interventions targeting the troponin complex.

      By delving into the functions and roles of native human skeletal muscle TNNI1, this research aims to expand our knowledge of skeletal muscle physiology, its implications for muscle-related diseases, and its potential applications in musculoskeletal research and clinical medicine.

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    Troponin 1 Skeletal Muscle
  • View Data Sheet

    Name :

    SNCA Delta-NAC Human

    Description:

    Alpha Synuclein Delta-NAC 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-161

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    Description

    A-Synuclein Delta-NAC Human Recombinant which is a deletion mutant of the a-synuclein that lacks the NAC region (amino acid 61-95), produced in E.Coli is a single, non-glycosylated polypeptide chain of 111 amino acids having a molecular mass of 11.9kDa (molecular size on SDS-PAGE will appear higher), with 6 amino acids added as a linker. The Recombinant Human a-Synuclein Delta-NAC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA Delta-NAC protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • 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 GTEIWMKKDQ LGKNEEGAPQ EGILEDMPVD PDNEAYEMPS EEGYQDYEPE A.

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    Snca Delta Nac Human
  • View Data Sheet

    Name :

    TAC3 Human

    Description:

    Tachykinin-3 Human Recombinant

    Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

    Product # :

    PRO-716

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    Description

    TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
      During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy.

    • Synonyms

      Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

    • 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 QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.

    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.

    Tac3 Human
  • View Data Sheet

    Name :

    MYL4 Human

    Description:

    Myosin Light Chain 4 Human Recombinant

    Myosin light chain 4 alkali atrial embryonic, ALC1, AMLC, GT1, Myosin light chain 1 embryonic muscle/atrial isoform, Myosin light chain alkali GT-1 isoform, PRO1957, MLC1.

    Product # :

    PRO-992

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    Description

    MYL4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (1-197 a.a.) and having a molecular mass of 22.6kDa.MYL4 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    MYL4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 150mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MYL4 is a hexameric ATPase cellular motor protein which is composed of two nonphosphorylatable alkali light chains, two heavy chains and two phosphorylatable regulatory light chains. MYL4 encodes a myosin alkali light chain which is located in embryonic muscle and adult atria. Two alternatively spliced transcript variants encoding the same protein were found for this gene.

    • Synonyms

      Myosin light chain 4 alkali atrial embryonic, ALC1, AMLC, GT1, Myosin light chain 1 embryonic muscle/atrial isoform, Myosin light chain alkali GT-1 isoform, PRO1957, MLC1.

    • 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

      MAPKKPEPKK EAAKPAPAPA PAPAPAPAPA PEAPKEPAFD PKSVKIDFTA DQIEEFKEAF SLFDRTPTGE MKITYGQCGD VLRALGQNPT NAEVLRVLGK PKPEEMNVKM LDFETFLPIL QHISRNKEQG TYEDFVEGLR VFDKESNGTV MGAELRHVLA TLGEKMTEAE VEQLLAGQED ANGCINYEAF VKHIMSGLEH HHHHH.

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    Myl4 Human
  • View Data Sheet

    Name :

    Streptavidin

    Description:

    Streptavidin Recombinant

    Product # :

    PRO-791

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    Description

    Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized in 10mM potassium phosphate buffer pH 6.5.

    Purity

    Greater than 98.0% as determined by SDS-PAGE and HPLC.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.

    • Solubility

      It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
      GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
      EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS.

    • Proteolytic Activity

      < 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).

    • Specific Activity

      > 17U/mg (one unit binds 1 μg D-biotin).

    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.

    Streptavidin Recombinant
  • View Data Sheet

    Name :

    MLANA Human

    Description:

    Melan-A Human Recombinant

    MART-1, MART1, Melanoma antigen recognized by T-cells 1, Antigen LB39-AA, Antigen SK29-AA, Protein Melan-A, MLANA.

    Product # :

    PRO-1498

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    Description

    MLANA Human Recombinant produced in E. coli is a single polypeptide chain containing 94 amino acids (48-118) and having a molecular mass of 10.4kDa. MLANA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Melan-A (MLANA), is engaged in melanosome biogenesis by ensuring the stability of GPR143. MLANA takes part in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is essential to the formation of stage II melanosomes.

    • Synonyms

      MART-1, MART1, Melanoma antigen recognized by T-cells 1, Antigen LB39-AA, Antigen SK29-AA, Protein Melan-A, MLANA.

    • 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 MGSCRRRNGY RALMDKSLHV GTQCALTRRC PQEGFDHRDS KVSLQEKNCE PVVPNAPPAY EKLSAEQSPP PYSP.

    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.

    Mlana Human
  • View Data Sheet

    Name :

    FABP1 Mouse, His

    Description:

    Fatty Acid Binding Protein-1, His Tag Mouse Recombinant

    Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein, Fatty acid-binding protein, liver.

    Product # :

    PRO-2512

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    Description

    FABP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 150 amino acids (1-127 a.a.) and having a molecular mass of 16.6 kDa. The FABP1 is fused to a 23 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FABP1 solution (0.25mg/ml) contains PBS (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.

    • Synonyms

      Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein, Fatty acid-binding protein, liver.

    • 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 MGSMNFSGKY QLQSQENFEP FMKAIGLPED LIQKGKDIKG VSEIVHEGKK IKLTITYGPK VVRNEFTLGE ECELETMTGE KVKAVVKLEG DNKMVTTFKG IKSVTELNGD TITNTMTLGD IVYKRVSKRI.

    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.

    Fabp 1 Mouse
  • View Data Sheet

    Name :

    GMFB Human

    Description:

    Glia Maturation Factor Beta Human Recombinant

    Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

    Product # :

    CYT-565

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    Description

    Glia Maturation Factor-Beta (GMF-Beta) Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.5 kDa. Glia Maturation Factor-Beta, GMF-Beta, Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMF-beta protein was lyophilized after dialysis against 20mM PBS pH=7.4 and 130mM NaCl.

    Purity

    Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
      Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
      GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
      GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.

    • Synonyms

      Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
      ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
      KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.

    • Background

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

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

      What is the Purity of GMFB HUMAN Protein?
      GMFB HUMAN Protein is >98% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of GMFB HUMAN Protein?
      SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
      ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
      KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.

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

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


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

    Gmfb Human
  • View Data Sheet

    Name :

    NREP Human

    Description:

    Neuronal Regeneration Related Protein Human Recombinant

    Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.

    Product # :

    PRO-1780

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    Description

    NREP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (1-68) and having a molecular mass of 10.3kDa.NREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NREP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuronal Regeneration Related Protein (NREP) has roles in neural function. NREP promotes axonal regeneration. In addition, NREP has functions in cellular differentiation. NREP protein induces differentiation of fibroblast into myofibroblast and increases retinoic-acid regulation of lipid-droplet biogenesis. NREP down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3. NREP has a role in the regulation of alveolar generation.

    • Synonyms

      Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related 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 MGSMVYYPEL FVWVSQEPFP NKDMEGRLPK GRLPVPKEVN RKKNDETNAA SLTPLGSSEL RSPRISYLHF F.

    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.

    Nrep Human
  • View Data Sheet

    Name :

    PARK7 Mouse

    Description:

    Parkinson Disease Protein 7 Mouse Recombinant

    Protein deglycase DJ-1, Parkinson disease protein 7 homolog.

    Product # :

    PRO-2226

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    Description

    PARK7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189 a.a) and having a molecular mass of 22.4kDa. PARK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PARK7 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).

    • Synonyms

      Protein deglycase DJ-1, Parkinson disease protein 7 homolog.

    • 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 MGSMASKRAL VILAKGAEEM ETVIPVDVMR RAGIKVTVAG LAGKDPVQCS RDVMICPDTS LEDAKTQGPY DVVVLPGGNL GAQNLSESPM VKEILKEQES RKGLIAAICA GPTALLAHEV GFGCKVTTHP LAKDKMMNGS HYSYSESRVE KDGLILTSRG PGTSFEFALA IVEALVGKDM ANQVKAPLVL KD.

    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.

    Park7 Mouse
  • View Data Sheet

    Name :

    MAPRE3 Human

    Description:

    Microtubule-Associated Protein, RP/EB Family, Member 3 Human Recombinant

    RP3, EB3, EBF3, End-binding protein 3, EBF3-S, APC binding protein.

    Product # :

    PRO-264

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    Description

    MAPRE3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (1-281a.a.) and having a molecular mass of 34.1kDa.MAPRE3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAPRE3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 2mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPRE3 is a microtubule related protein that cooperates with the colorectal adenomatous polyposis coli tumor suppressor protein and takes a curtail part in regulating microtubule dynamics, cell polarity, and chromosome stability. MAPRE3 protein is related to MAPRE1 and also associates with the microtubule cytoskeleton. MAPRE3 is expressed mainly in the central nervous system and specially associates with APCL, a homolog of the adenomatous polyposis coli tumor suppressor protein.

    • Synonyms

      RP3, EB3, EBF3, End-binding protein 3, EBF3-S, APC binding protein.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM LFPGCVHLRK VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK FQDNFEFIQW FKKFFDANYD GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP PCILRKNPPS ARNGGHETDA QILELNQQLV DLKLTVDGLE KERDFYFSKL RDIELICQEH ESENSPVISG IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y

    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.

    Mapre3 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 :

    MANF Mouse

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Mouse Recombinant

    Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    Product # :

    CYT-827

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    • More Info

    Description

    MANF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18.2kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 98.0% 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 rat C6 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

    More Info

    • Introduction

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

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIEEELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDNQ IDLSTVDLKK LRVKELKKIL DDWGEMCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.

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

    Manf Mouse
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