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Search results

1000 results found for “lipocalin”

Name

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  • View Data Sheet

    Name :

    APOM Human

    Description:

    Apolipoprotein-M Human Recombinant

    G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

    Product # :

    CYT-715

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    • sds-page

    Description

    APOM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (23-188 a.a.) and having a molecular mass of 20.9 kDa. APOM protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    APOM Human solution containing 20mM Tris-HCl pH-8 1mM DTT & 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    APOM-sds-page - Product image 1

    More Info

    • Introduction

      APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport. .

    • Synonyms

      G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

    • 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 MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.

    • Background

      Apolipoprotein-M Human Recombinant: Insights into its Role in Lipid Metabolism and Cardiovascular Health

      Abstract:


      Apolipoprotein-M (ApoM), a unique member of the apolipoprotein family, has gained significant attention in the field of lipid metabolism and cardiovascular health. This research paper provides a comprehensive analysis of ApoM human recombinant, exploring its structure, function, and potential implications in cardiovascular diseases. Understanding the intricate nature of ApoM sheds light on its significance as a potential biomarker and therapeutic target in cardiovascular disorders. This article presents a concise yet comprehensive examination of ApoM, highlighting its impact on human health.

      Introduction:


      Cardiovascular diseases remain a leading cause of global morbidity and mortality, underscoring the importance of understanding lipid metabolism and its association with cardiovascular health. ApoM, an intriguing apolipoprotein, has emerged as a key player in lipid metabolism and cardiovascular function. This paper delves into the intricate nature of ApoM, elucidating its structure, molecular interactions, and potential roles in cardiovascular diseases.

      Structure and Function of Apolipoprotein-M:


      ApoM exhibits a unique structural configuration, comprising a single membrane-bound alpha-helix and a lipocalin-like domain. It predominantly associates with high-density lipoproteins (HDL) and plays a critical role in HDL metabolism and cholesterol transport. Additionally, ApoM has been implicated in endothelial function, inflammation, and modulation of sphingolipid metabolism.

      Apolipoprotein-M and Cardiovascular Diseases:


      Studies have highlighted the potential involvement of ApoM in cardiovascular diseases, such as atherosclerosis and coronary artery disease. Genetic variations in the ApoM gene and alterations in ApoM levels have been associated with disease development and progression. Understanding the role of ApoM in cardiovascular diseases offers insights into potential therapeutic interventions and diagnostic strategies.

      Apolipoprotein-M Human Recombinant Production:


      The production of ApoM human recombinant is made possible through advanced biotechnological techniques, including recombinant DNA technology and protein expression systems. These methods facilitate large-scale production, purification, and characterization of ApoM, providing opportunities for further research and potential therapeutic applications.

      Therapeutic Potential of Apolipoprotein-M Human Recombinant:


      Exploring the therapeutic potential of ApoM holds promise in the field of cardiovascular disorders. Strategies aimed at modulating ApoM expression or function may contribute to the prevention or treatment of lipid metabolism-related diseases. Furthermore, ApoM may serve as a potential biomarker for risk assessment and monitoring of cardiovascular conditions.

      Conclusion:


      Apolipoprotein-M human recombinant represents a fascinating area of research, shedding light on the role of this protein in lipid metabolism and cardiovascular health. Understanding the structure, function, and genetic implications of ApoM is pivotal in advancing our knowledge and exploring its potential as a therapeutic target. Continued investigation into the mechanisms and signaling pathways involving ApoM will likely pave the way for innovative strategies in the diagnosis, prevention, and treatment of cardiovascular diseases.

      What is the molecular weight/Mw of APOM Protein?
      APOM Protein has a total Mw of 20.9kDa.

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

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

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

      What is the amino acid sequence of APOM Protein?
      MGSSHHHHHH SSGLVPRGSH MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.

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

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

    Apom Human
  • View Data Sheet

    Name :

    S100A6 Human

    Description:

    S100 Calcium Binding Protein A6 Human Recombinant

    Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

    Product # :

    PRO-148

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    Description

    S100A6 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 110 amino acids (1-90 a.a.) and having a molecular mass of 12.3kDa. The S100A6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A6 function in stimulation of prolactin secretion and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

    • Synonyms

      Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

    • 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 MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG.

    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.

    S100A6 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

    Price :

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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 :

    PFN4 Human

    Description:

    Profilin-4 Human Recombinant

    PFN-4, Profilin-IV, Profilin4.

    Product # :

    PRO-818

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    Description

    PFN4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-129 a.a.) and having a molecular mass of 16.4 kDa. PFN4 protein is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN4 Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFN4 is a small actin-binding protein that participates in the dynamic turnover and restructuring of the actin cytoskeleton. PFN4 is localized in all eukaryotic organisms in the majority of cells. PFN4 is crucial for spatially and temporally controlled growth of actin microfilaments, which is a necessary process in cellular locomotion and cell shape changes.

    • Synonyms

      PFN-4, Profilin-IV, Profilin4.

    • 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 MSHLQSLLLD TLLGTKHVDS AALIKIQERS LCVASPGFNV TPSDVRTLVN GFAKNPLQAR REGLYFKGKD YRCVRADEYS LYAKNENTGV VVVKTHLYLL VATYTEGMYP SICVEATESL GDYLRKKGS.

    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.

    Pfn4 Human
  • View Data Sheet

    Name :

    RBP7 Human

    Description:

    Retinol Binding Protein-7 Human Recombinant

    Retinoid-binding protein 7, Cellular retinoic acid-binding protein 4, CRABP4, CRBP4, Cellular retinoic acid-binding protein IV, CRABP-IV, RBP7, MGC70641.

    Product # :

    CYT-023

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    Description

    RBP7 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 154 amino acids (1-134 a.a.) and having a molecular mass of 17.6kDa. The RBP7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RBP7 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RBP7 is a member of a superfamily of small cytoplasmic proteins which interact with hydrophobic ligands. RBP7 is cytoplasmic protein which, like CRBP I and CRBP II, forms ?-barrel structures and participates in the intracellular transport of retinol. RBP7 is a newly identified cellular retinol carrier, which is expressed in the kidney, heart and transverse colon in humans.

    • Synonyms

      Retinoid-binding protein 7, Cellular retinoic acid-binding protein 4, CRABP4, CRBP4, Cellular retinoic acid-binding protein IV, CRABP-IV, RBP7, MGC70641.

    • 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 MPADLSGTWT LLSSDNFEGY MLALGIDFAT RKIAKLLKPQ KVIEQNGDSF TIHTNSSLRN YFVKFKVGEE FDEDNRGLDN RKCKSLVIWD NDRLTCIQKG EKKNRGWTHW IEGDKLHLEM FCEGQVCKQT FQRA.

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    Rbp7 Human
  • View Data Sheet

    Name :

    ARTN Human

    Description:

    Artemin Human Recombinant

    ART, ARTN , EVN, NBN.

    Product # :

    CYT-306

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    Description

    Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

    More Info

    • Introduction

      The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.

    • Synonyms

      ART, ARTN , EVN, NBN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

    • Background

      Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications

      Abstract:

      Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.

      Introduction:

      Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.

      Artemin Signaling and Mechanisms:

      Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.

      Artemin in Neurological Disorders:

      Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.

      Therapeutic Potential of Artemin Human Recombinant:

      Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.

      Challenges and Future Directions:

      While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.

      Conclusion:

      Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.

      What is the molecular weight/Mw of ARTN Protein?
      ARTN Protein has a total Mw of 24.2kDa.

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

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

      What is the Biological Activity of ARTN Protein?
      The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

      What is the amino acid sequence of ARTN Protein?
      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

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

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

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    Artemin 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

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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.

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    Rbp4 Protein
  • View Data Sheet

    Name :

    Activin-A Human Plant-Active

    Description:

    Activin-A Human Recombinant, Plant-Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-414

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    Description

    Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4

    Purity

    Greater than 98% as obsereved by SDS-PAGE.

    Biological Activity

    The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.

    • Solubility

      INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.

    • Amino Acid Sequence

      HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
      YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
      NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.

      What is the source or expression system of Activin A Protein?
      Nicotiana benthamiana.

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

      What is the Biological Activity of Activin A Protein?
      The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

      What is the endotoxin level for Activin A Protein?
      The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

      What applications can ACTIVIN-A Protein be used in?

      ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

       

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    Activin A Active
  • View Data Sheet

    Name :

    BGN Human, Sf9

    Description:

    Biglycan Human Recombinant, Sf9

    BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    Product # :

    PRO-2536

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    Description

    BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 340 amino acids (38-368 a.a.) and having a molecular mass of 38.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). BGN is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is ≤ 20 ug/ml. The specific activity is measured by inhibiting the cell growth using 3T3‑ L1 mouse embryonic  fibroblast  adipose-like cells.

    More Info

    • Introduction

      Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

    • Synonyms

      BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    • 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

      ADPDEEASGA DTSGVLDPDS VTPTYSAMCP FGCHCHLRVV QCSDLGLKSV PKEISPDTTL LDLQNNDISE LRKDDFKGLQ HLYALVLVNN KISKIHEKAF SPLRKLQKLY ISKNHLVEIP PNLPSSLVEL RIHDNRIRKV PKGVFSGLRN MNCIEMGGNP LENSGFEPGA FDGLKLNYLR ISEAKLTGIP KDLPETLNEL HLDHNKIQAI ELEDLLRYSK LYRLGLGHNQ IRMIENGSLS FLPTLRELHL DNNKLARVPS GLPDLKLLQV VYLHSNNITK VGVNDFCPMG FGVKRAYYNG ISLFNNPVPY WEVQPATFRC VTDRLAIQFG NYKKHHHHHH.

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    Biglycan Human
  • View Data Sheet

    Name :

    Cys-Protein-G

    Description:

    Cys-Protein G Recombinant

    Product # :

    PRO-1238

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    Description

    Cys-Protein G Recombinant produced in E.Coli, is a single non-glycosylated polypeptide chain containing 201 amino acids and having a cys on N-terminal. Cys-Protein G has a predicted molecular mass of approximately 21.9kDa but it migrates with an apparent molecular mass of 40kDa in SDS-PAGE. The Cys-Protein G is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized without any additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      CLPKTDTYKL ILNGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTKAVDAET AEKAFKQYAN DNGVDGVWTY DDATKTFTVT E.

    • Specificity

      The recombinant Protein G is a genetically engineered protein contains 3 IgG-binding regions of protein G.

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    Cys Protein G His
  • View Data Sheet

    Name :

    LBP Mouse

    Description:

    Lipopolysaccaride Mouse Recombinant

    Lipopolysaccharide-binding protein, LBP, Ly88.

    Product # :

    PRO-539

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    Description

    LBP is produced from mouse LBP transfected CHO-cells in serum free medium. For transfection we have cloned complete mouse LBP cDNA into expression vector pPOL-DHFR. Before transfection the complete mouse LBP cDNA was amplified by PCR and cloned into expression vector p-POL-DHFR. RmLBP was produced by his-tag by means of metal affinity purification with Talon and controlled by SDS page. Showing a 58kDa band on SDS-PAGE. Attention: His-tag at the c-terminal end of the LBP has no protease site and is not to split off.

    Source

    Chinese Hamster Ovarian Cells (CHO).

    Formulation

    Recombinant Mouse LBP was lyophilized from a protein solution (1 mg/ml) containing phosphate-buffered saline, pH 7.2.

    Biological Activity

    Up to 2µg/ml LBP mediates binding of FITC-LPS (0.5µg/ml) to CD14+CHO transfectants (2 x 106/ml).

    More Info

    • Introduction

      Lipopolysaccharides (LPS) are a type of glycolipids on the outer cell wall of Gram-negative bacteria. Lipopolysaccharide binding protein (aka LBP) is a plasma protein which facilitates the diffusion of bacterial LPS (endotoxin). LBP is involved in the acute-phase immunologic response to gram-negative bacterial infections. In cooperation with bactericidal permeability-increasing protein (BPI), LBP binds LPS and interacts with the CD14 receptor, most likely playing a role in regulating LPS-dependent monocyte responses. LBP belongs to a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). The LBP gene is found on chromosome 20, directly downstream of the BPI gene. LBP catalyzes the transfer of LPS monomers from LPS aggregates to HDL particles, to phospholipid bilayers, and to a binding site on soluble CD14 (sCD14). sCD14 is capable of speeding up the transfer by receiving an LPS monomer from an LPS aggregate, and then yielding it to an HDL particle, therefore acting as a soluble "shuttle" for an insoluble lipid.

    • Synonyms

      Lipopolysaccharide-binding protein, LBP, Ly88.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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    Lbp Mouse
  • View Data Sheet

    Name :

    BCAR1 Human

    Description:

    Breast Cancer Anti-Estrogen Resistance 1 Human Recombinant

    CAS, CAS1, CASS1, CRKAS, P130Cas, Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, BCAR1.

    Product # :

    PRO-1858

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    Description

    BCAR1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 407 amino acids (465-848) and having a molecular mass of 43.9kDa. BCAR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCAR1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Breast Cancer Anti-Estrogen Resistance 1 (BCAR1) is a Src family kinase substrate which takes part in a range of cellular events such as migration, survival, transformation, and invasion. BCAR1 plays a vital role for tyrosine kinase-based signaling related to cell adhesion.

    • Synonyms

      CAS, CAS1, CASS1, CRKAS, P130Cas, Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, BCAR1.

    • 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 MGSRLQQGVS ATVAHLLDLA GSAGATGSWR SPSEPQEPLV QDLQAAVAAV QSAVHELLEF ARSAVGNAAH TSDRALHAKL SRQLQKMEDV HQTLVAHGQA LDAGRGGSGA TLEDLDRLVA CSRAVPEDAK QLASFLHGNA SLLFRRTKAT APGPEGGGTL HPNPTDKTSS IQSRPLPSPP KFTSQDSPDG QYENSEGGWM EDYDYVHLQG KEEFEKTQKE LLEKGSITRQ GKSQLELQQL KQFERLEQEV SRPIDHDLAN WTPAQPLAPG RTGGLGPSDR QLLLFYLEQC EANLTTLTNA VDAFFTAVAT NQPPKIFVAH SKFVILSAHK LVFIGDTLSR QAKAADVRSQ VTHYSNLLCD LLRGIVATTK AAALQYPSPS AAQDMVE.

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    Bcar1 Human
  • View Data Sheet

    Name :

    CD68 Human, sf9

    Description:

    CD68 Human Recombinant, sf9

    Macrosialin, CD68, Gp110, Macrosialin isoform A, GP110, LAMP4, SCARD1.

    Product # :

    PRO-2375

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    Description

    CD68 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 307 amino acids (22-319) and having a molecular mass of 32.6kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa).CD68 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD68 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

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    • Introduction

      CD68 encodes a 110-kD transmembrane glycoprotein that is highly expressed by human monocytes and tissue macrophages. It is a member of the lysosomal/endosomal-associated membrane glycoprotein (LAMP) family. The protein primarily localizes to lysosomes and endosomes with a smaller fraction circulating to the cell surface. It is a type I integral membrane protein with a heavily glycosylated extracellular domain and binds to tissue- and organ-specific lectins or selectins. The protein is also a member of the scavenger receptor family. Scavenger receptors typically function to clear cellular debris, promote phagocytosis, and mediate the recruitment and activation of macrophages. Alternative splicing results in multiple transcripts encoding different isoforms.

    • Synonyms

      Macrosialin, CD68, Gp110, Macrosialin isoform A, GP110, LAMP4, SCARD1.

    • 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

      ADPNDCPHKK SATLLPSFTV TPTVTESTGT TSHRTTKSHK TTTHRTTTTG TTSHGPTTAT HNPTTTSHGN VTVHPTSNST ATSQGPSTAT HSPATTSHGN ATVHPTSNST ATSPGFTSSA HPEPPPPSPS PSPTSKETIG DYTWTNGSQP CVHLQAQIQI RVMYTTQGGG EAWGISVLNP NKTKVQGSCE GAHPHLLLSF PYGHLSFGFM QDLQQKVVYL SYMAVEYNVS FPHAAQWTFS AQNASLRDLQ APLGQSFSCS NSSIILSPAV HLDLLSLRLQ AAQLPHTGVF GQSFSCPSDR SHHHHHH.

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    Cd68 Human Sf9
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    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.

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    • 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

    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.

    Gypa Human
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    Name :

    SEPT5 Human

    Description:

    Septin-5 Human Recombinant

    Septin 5, PNUTL1, H5, HCDCREL-1, CDCREL-1, cell division control related protein 1, Peanut-like protein 1 (Drosophila), platelet glycoprotein Ib beta chain.

    Product # :

    PRO-879

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    Description

    SEPT5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 392 amino acids (1-369) and having a molecular mass of 45.2 kDa.The SEPT5 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SEPT5 protein (0.25mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.3M NaCl, 1mM DTT and 40% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      SEPT5 is a member of the septin gene family of nucleotide binding proteins which were initially defined in yeast as cell division cycle regulatory proteins. Septins are extremely conserved in yeast, Drosophila, and mouse and seem to regulate cytoskeletal organization. Interference of septin function disrupts cytokinesis and results in high multinucleate or polyploid cells.

    • Synonyms

      Septin 5, PNUTL1, H5, HCDCREL-1, CDCREL-1, cell division control related protein 1, Peanut-like protein 1 (Drosophila), platelet glycoprotein Ib beta chain.

    • 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 MGSMSTGLRY KSKLATPEDK QDIDKQYVGF ATLPNQVHRK SVKKGFDFTL MVAGESGLGK STLVHSLFLT DLYKDRKLLS AEERISQTVE ILKHTVDIEE KGVKLKLTIV DTPGFGDAVN NTECWKPITD YVDQQFEQYF RDESGLNRKN IQDNRVHCCL YFISPFGHGL RPVDVGFMKA LHEKVNIVPL IAKADCLVPS EIRKLKERIR EEIDKFGIHV YQFPECDSDE DEDFKQQDRE LKESAPFAVI GSNTVVEAKG QRVRGRLYPW GIVEVENQAH CDFVKLRNML IRTHMHDLKD VTCDVHYENY RAHCIQQMTS KLTQDSRMES PIPILPLPTP DAETEKLIRM KDEELRRMQE MLQRMKQQMQ DQ

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    Sept5 Human
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    Name :

    ANXA7 Human

    Description:

    Annexin A7 Human Recombinant

    Annexin A7, Annexin-7, Annexin VII, Synexin, ANXA7, ANX7, SNX.

    Product # :

    PRO-449

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    Description

    ANXA7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 490 amino acids (1-466 a.a.) and having a molecular mass of 52.9kDa.ANXA7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANXA7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 150mM NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins. Annexin VII has molecular weight of approximately 51 kDa with a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.

    • Synonyms

      Annexin A7, Annexin-7, Annexin VII, Synexin, ANXA7, ANX7, SNX.

    • 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 MGSHMSYPGY PPTGYPPFPG YPPAGQESSF PPSGQYPYPS GFPPMGGGAY PQVPSSGYPG AGGYPAPGGY PAPGGYPGAP QPGGAPSYPG VPPGQGFGVP PGGAGFSGYP QPPSQSYGGG PAQVPLPGGF PGGQMPSQYP GGQPTYPSQP ATVTQVTQGT IRPAANFDAI RDAEILRKAM KGFGTDEQAI VDVVANRSND QRQKIKAAFK TSYGKDLIKD LKSELSGNME ELILALFMPP TYYDAWSLRK AMQGAGTQER VLIEILCTRT NQEIREIVRC YQSEFGRDLE KDIRSDTSGH FERLLVSMCQ GNRDENQSIN HQMAQEDAQR LYQAGEGRLG TDESCFNMIL ATRSFPQLRA TMEAYSRMAN RDLLSSVSRE FSGYVESGLK TILQCALNRP AFFAERLYYA MKGAGTDDST LVRIVVTRSE IDLVQIKQMF AQMYQKTLGT MIAGDTSGDY RRLLLAIVGQ

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    Anxa7 Human
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    Name :

    BMP 7 Human

    Description:

    Bone Morphogenetic Protein-7 Human Recombinant

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-333

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

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    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, BMP-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Background

      Bone Morphogenetic Protein-7 Human Recombinant: A Comprehensive Review

      Abstract:

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

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

      Introduction:

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

      Structure and Function of BMP-7:

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

      Skeletal Development and Regeneration:

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

      Tissue Repair and Regeneration:

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

      Therapeutic Potential:

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

      Challenges and Future Perspectives:

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

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

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

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

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

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

      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.

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    Bmp 7 Human
  • View Data Sheet

    Name :

    FABP7 Human

    Description:

    Fatty Acid Binding Protein-7 Human Recombinant

    MRG, BLBP, FABPB, B-FABP, DKFZp547J2313, Fatty acid-binding protein brain, Fatty acid-binding protein 7, Brain lipid-binding protein, Mammary-derived growth inhibitor related, FABP7.

    Product # :

    PRO-628

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    Description

    FABP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 14 kDa.

    Source

    Escherichia Coli.

    Formulation

    The FABP7 protein solution contains 25mM Tris-HCl pH7.5, 2mM EDTA and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      FABP7 is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs are are inovlved in fatty acid uptake, transport, and metabolism. FABP7 is expressed in radial glia by the activation of Notch receptors and binds DHA with the highest affinity among all of FABPs. FABP7 plays an important role in transport of hydrophobic ligand with potential morphogenic activity during cns development. FABP7 is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (by similarity).

    • Synonyms

      MRG, BLBP, FABPB, B-FABP, DKFZp547J2313, Fatty acid-binding protein brain, Fatty acid-binding protein 7, Brain lipid-binding protein, Mammary-derived growth inhibitor related, FABP7.

    • 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

      MVEAFCATWK LTNSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGDKV VIRTLSTFKN TEISFQLGEE FDETTADDRN CKSVVSLDGD KLVHIQKWDG KETNFVREIK DGKMVMTLTF GDVVAVRHYE KA.

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    Fabp7 Human
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    Name :

    PEX26 Human

    Description:

    Peroxisomal Biogenesis Factor 26 Human Recombinant

    PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.

    Product # :

    PRO-1544

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    Description

    PEX26 Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-246) and having a molecular mass of 29.3kDa. PEX26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PEX26 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Peroxisomal Biogenesis Factor 26 (PEX26) which is a part of the peroxin-26 gene family is probably required for protein import into peroxisomes. PEX26 attaches PEX1 and PEX6 to peroxisome membranes to form heteromeric AAA ATPase complexes needed for the import of proteins into peroxisomes. Deficiencies in this gene are the cause of peroxisome biogenesis disorder complementation group 8. PBD is a group of peroxisomal disorders evolving from a failure of protein import into the peroxisomal membrane or matrix.

    • Synonyms

      PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.

    • 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 MGSMKSDSST SAAPLRGLGG PLRSSEPVRA VPARAPAVDL LEEAADLLVV HLDFRAALET CERAWQSLAN HAVAEEPAGT SLEVKCSLCV VGIQALAEMD RWQEVLSWVL QYYQVPEKLP PKVLELCILL YSKMQEPGAV LDVVGAWLQD PANQNLPEYG ALAEFHVQRV LLPLGCLSEA EELVVGSAAF GEERRLDVLQ AIHTARQQQK QEHSGSEEAQ KPNLEGSVSH KFLSLPMLVR QLWDSAVSH.

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    Pex26 Human
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    Name :

    LHRH Protein

    Description:

    Luteinizing Hormone Releasing Hormone Human Recombinant

    LHRH, GRH, GNRH, LNRH.

    Product # :

    HOR-268

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    Description

    LHRH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (24-92 a.a.) and having a molecular mass of 10.3kDa.LHRH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      GNRH1 also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
      At the pituitary, GNRH1 stimulates the synthesis and secretion of the follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
      There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
      GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male.

    • Synonyms

      LHRH, GRH, GNRH, LNRH.

    • 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 MGSQHWSYGL RPGGKRDAEN LIDSFQEIVK EVGQLAETQR FECTTHQPRS PLRDLKGALE SLIEEETGQK KI.

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    Lhrh Human Recombinant
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    Name :

    LUM Human

    Description:

    Lumican Human Recombinant

    Lumican, LDC, Lumican Proteoglycan, Keratan Sulfate Proteoglycan Lumican, SLRR2D, KSPG Lumican.

    Product # :

    PRO-1821

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    Description

    LUM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (19-338a.a) and having a molecular mass of 39kDa. LUM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Lumican also known as LUM belongs to the small leucine-rich proteoglycan (SLRP) family which comprises decorin, biglycan, fibromodulin, keratocan, epiphycan, and osteoglycin. Furthermore we can see that in these bifunctional molecules, the protein moiety binds collagen fibrils and the highly charged hydrophilic glycosaminoglycans regulate interfibrillar spacings. Lumican is the main keratan sulfate proteoglycan of the cornea however LUM is also distributed in interstitial collagenous matrices throughout the body. Lumican regulates collagen fibril organization and circumferential growth, corneal transparency, epithelial cell migration and tissue repair. Among the diseases associated with LUM is posterior amorphous corneal dystrophy.

    • Synonyms

      Lumican, LDC, Lumican Proteoglycan, Keratan Sulfate Proteoglycan Lumican, SLRR2D, KSPG Lumican.

    • 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 MGSQYYDYDF PLSIYGQSSP NCAPECNCPE SYPSAMYCDE LKLKSVPMVP PGIKYLYLRN NQIDHIDEKA FENVTDLQWL ILDHNLLENS KIKGRVFSKL KQLKKLHINH NNLTESVGPL PKSLEDLQLT HNKITKLGSF EGLVNLTFIH LQHNRLKEDA VSAAFKGLKS LEYLDLSFNQ IARLPSGLPV SLLTLYLDNN KISNIPDEYF KRFNALQYLR LSHNELADSG IPGNSFNVSS LVELDLSYNK LKNIPTVNEN LENYYLEVNQ LEKFDIKSFC KILGPLSYSK IKHLRLDGNR ISETSLPPDM YECLRVANEV TLN.

    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.

    Lum Human
  • View Data Sheet

    Name :

    APOL4 Human

    Description:

    Apolipoprotein L 4 Human Recombinant

    APOL-IV, APOLIV, Apolipoprotein L4, ApoL-IV.

    Product # :

    CYT-785

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    • sds-page

    Description

    APOH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (1-348 a.a.) and having a molecular mass of 41.1kDa.APOH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    APOL4-sds-page - Product image 1

    More Info

    • Introduction

      Apolipoprotein L 4 (APOL4) belongs to the apolipoprotein L family. APOL4 plays a role in lipid exchange and transport through the body, in addition to reverse cholesterol transport from peripheral cells to the liver. Two transcript variants encoding two different isoforms have been found for this gene. APOL4 is highly expressed in spinal cord, placenta, adrenal gland; also detected in spleen, bone marrow, uterus, trachea, mammary gland and testis

    • Synonyms

      APOL-IV, APOLIV, Apolipoprotein L4, ApoL-IV.

    • 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 MGSMGSWVQL ITSVGVQQNH PGWTVAGQFQ EKKRFTEEVI EYFQKKVSPV HLKILLTSDE AWKRFVRVAE LPREEADALY EALKNLTPYV AIEDKDMQQK EQQFREWFLK EFPQIRWKIQ ESIERLRVIA NEIEKVHRGC VIANVVSGST GILSVIGVML APFTAGLSLS ITAAGVGLGI ASATAGIASS IVENTYTRSA ELTASRLTAT STDQLEALRD ILRDITPNVL SFALDFDEAT KMIANDVHTL RRSKATVGRP LIAWRYVPIN VVETLRTRGA PTRIVRKVAR NLGKATSGVL VVLDVVNLVQ DSLDLHKGAK SESAESLRQW AQELEENLNE LTHIHQSLKA G.

    • Background

      Clusterin Human Recombinant: Unraveling the Molecular Chaperone's Multifaceted Roles in Health and Disease

      Abstract:


      Clusterin, a versatile molecular chaperone, is involved in diverse physiological and pathological processes, making it an intriguing target for biomedical research. This paper provides a comprehensive analysis of Clusterin human recombinant, exploring its structure, functions, and potential applications. Understanding the intricacies of Clusterin sheds light on its significance in various biological contexts and highlights its potential as a therapeutic agent. This article offers a concise yet comprehensive examination of Clusterin, emphasizing its impact on human health.

      Introduction:


      The multifunctional protein Clusterin has emerged as a fascinating molecule with diverse roles in cellular homeostasis, neuroprotection, and tissue repair. This paper delves into the intricate nature of Clusterin, unveiling its structural features, molecular interactions, and involvement in various physiological processes.

      Structure and Function of Clusterin:


      Clusterin exhibits a complex structure, comprising multiple isoforms and domains that enable its interactions with a wide range of ligands. It functions as a molecular chaperone, aiding in protein folding, clearance of cellular debris, and regulation of apoptosis. Clusterin also plays a role in lipid transport and immune modulation.

      Biological Implications of Clusterin:


      Clusterin's involvement in diverse biological processes highlights its significance in health and disease. It contributes to the maintenance of tissue homeostasis, participates in neuroprotection, and influences immune responses. Moreover, Clusterin has been implicated in various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases.

      Clusterin Human Recombinant Production:


      Cutting-edge biotechnological techniques, such as recombinant DNA technology and protein expression systems, allow for the production of Clusterin human recombinant. These methods facilitate large-scale production, purification, and characterization of Clusterin, offering opportunities for therapeutic applications.

      Therapeutic Potential of Clusterin Human Recombinant:


      Harnessing the therapeutic potential of Clusterin holds promise in various clinical scenarios. Its chaperone-like properties make it an attractive target for the development of therapies against protein misfolding diseases. Additionally, Clusterin's involvement in tissue repair and immune modulation opens avenues for therapeutic interventions in neurodegenerative diseases and cancer.

      Conclusion:


      Clusterin human recombinant represents a captivating field of research, unraveling the multifaceted roles of this molecular chaperone in health and disease. Understanding the structure, functions, and biological implications of Clusterin is essential in advancing our knowledge and exploring its potential therapeutic applications. Continued investigation into the mechanisms of Clusterin will likely pave the way for innovative therapeutic strategies in diverse fields of medicine.

      What is the molecular weight/Mw of APOL4 Protein?
      APOL4 Protein has a total Mw of 41.1kDa.

      What is the source or expression system of APOL4 Protein?
      Escherichia Coli.

      What is the Purity of APOL4 Protein?
      APOL4 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOL4 Protein?
      The biological functionality of APOL4 Protein will be determined in the future.

      What is the amino acid sequence of APOL4 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMGSWVQL ITSVGVQQNH PGWTVAGQFQ EKKRFTEEVI EYFQKKVSPV HLKILLTSDE AWKRFVRVAE LPREEADALY EALKNLTPYV AIEDKDMQQK EQQFREWFLK EFPQIRWKIQ ESIERLRVIA NEIEKVHRGC VIANVVSGST GILSVIGVML APFTAGLSLS ITAAGVGLGI ASATAGIASS IVENTYTRSA ELTASRLTAT STDQLEALRD ILRDITPNVL SFALDFDEAT KMIANDVHTL RRSKATVGRP LIAWRYVPIN VVETLRTRGA PTRIVRKVAR NLGKATSGVL VVLDVVNLVQ DSLDLHKGAK SESAESLRQW AQELEENLNE LTHIHQSLKA G.

      What applications can APOL4 Protein be used in?
      APOL4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOL4 Protein?
      The endotoxin level is minimal, APOL4 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.

    Apol4 Human
  • View Data Sheet

    Name :

    SORBS3 Human

    Description:

    Sorbin And SH3 Domain Containing 3 Human Recombinant

    Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.

    Product # :

    PRO-1829

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    Description

    SORBS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329) and having a molecular mass of 39.1 kDa. SORBS3 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The SORBS3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

    • Synonyms

      Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADGGSP FLGRRDFVYP SSTRDPSASN GGGSPARREE KKRKAARLKF DFQAQSPKEL TLQKGDIVYI HKEVDKNWLE GEHHGRLGIF PANYVEVLPA DEIPKPIKPP TYQVLEYGEA VAQYTFKGDL EVELSFRKGE HICLIRKVNE NWYEGRITGT GRQGIFPASY VQVSREPRLR LCDDGPQLPT SPRLTAAARS ARHPSSPSAL RSPADPIDLG GQTSPRRTGF SFPTQEPRPQ TQNLGTPGPA LSHSRGPSHP LDLGTSSPNT SQIHWTPYRA MYQYRPQNED ELELREGDRV DVMQQCDDGW FVGVSRRTQK FGTFPGNYVA PV

    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.

    Sorbs3 Human
  • View Data Sheet

    Name :

    LMNA Human

    Description:

    Lamin A/C Human Recombinant

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

    Product # :

    PRO-2666

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Lmna Human
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