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1000 results found for “cebp”

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  • View Data Sheet

    Description:

    Corticotropin Releasing Hormone Binding Protein (22-322 a.a.) Human Recombinant

    Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

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    HOR-025

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    Description

    CRHBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (22-322 a.a) and having a molecular mass of 36.1kDa.CRHBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CRHBP protein (1mg/ml) contains 10% glycerol, 0.4M urea and 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Corticotropin Releasing Hormone Binding Protein or CRHBP is a hormone that stimulates the preopiomelanocortin-derived peptides secretion & synthesis. In general, the levels of CRHBP in the human plasma are relatively low. There are times when we can find high levels of the hormone, mainly in pregnancy, after parturition the levels drop back, the high levels are thought to be derived from the placenta. CRH-binding protein can be found in the plasma, this protein inactivates CRH, in order to avoid inappropriate pituitary-adrenal stimulation during gestation.

    • Synonyms

      Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding 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 MGSESRYLEL REAADYDPFL LFSANLKREL AGEQPYRRAL RCLDMLSLQG QFTFTADRPQ LHCAAFFISE PEEFITIHYD QVSIDCQGGD FLKVFDGWIL KGEKFPSSQD HPLPSAERYI DFCESGLSRR SIRSSQNVAM IFFRVHEPGN GFTLTIKTDP NLFPCNVISQ TPNGKFTLVV PHQHRNCSFS IIYPVVIKIS DLTLGHVNGL QLKKSSAGCE GIGDFVELLG GTGLDPSKMT PLADLCYPFH GPAQMKVGCD NTVVRMVSSG KHVNRVTFEY RQLEPYELEN PNGNSIGEFC LSGL

    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.

    Crhbp Protein
  • View Data Sheet

    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.

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    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

    Description:

    IP-10 (CXCL10) Guinea Pig Recombinant

    CXCL10, CRG-2.

    Product # :

    CHM-046

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    Description

    IP10 Guinea Pig Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a total molecular mass of 8.7kDa.The IP10 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 10 mM Sodium Phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.

    • Synonyms

      CXCL10, CRG-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IP10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IP10 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 reconstitute the lyophilized IP10 in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPHSRTIRCT CIETSTQPVN PKSFKKLEII PASQSCPRVE IIATMKMNGE KRCLDPESKV IKNLLKAVRK ERSKRS

    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.

    Cxcl10 Guinea Pig
  • View Data Sheet

    Description:

    Fatty Acid Binding Protein-1, Mouse Anti Human

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

    Product # :

    ANT-346

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    Formulation

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

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    • Introduction

      FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel β strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acids. 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.

    • Immunogen

      Anti-human FABP1 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human FABP1 amino acids 1-127 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      P2G4AT.

    • Applications

      FABP1 antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:1,000 ~ 1:2,000 and immunohistochemistry analysis is 1:100~300. Recommended starting dilution for Western blot is 1:1,000 and Immunohistochemistry is 1:100.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      FABP1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Fabp1 Antibody
  • View Data Sheet

    Description:

    NT-Pro-B-type Natriuretic Protein Canine Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-1223

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    Description

    NT-proBNP Canine produced in E.coli is a single, non-glycosylated polypeptide chain (1-85 a.a) containing 101 a.a and having a molecular mass of 10,545 Dalton. NT-proBNP is fused with a 16 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT-proBNP was lyophilized from 10mM potassium phosphate, pH 7.4 and 150 mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      N-terminal pro-brain natriuretic peptide, or NT-proBNP, has emerged as a significant biomarker in cardiovascular medicine, providing crucial insights into heart function and aiding in the diagnosis and management of heart-related conditions. This peptide, released in response to cardiac stress, reflects the heart's intricate signaling mechanisms and physiological responses. The study of NT-proBNP, especially in its recombinant form, has not only deepened our understanding of heart diseases but has also led to the development of advanced diagnostic tools and potential therapeutic interventions. This research delves into the world of NT-proBNP Recombinant Protein, exploring its biochemical intricacies, physiological roles, and its profound impact on cardiovascular healthcare.

      Structural and Molecular Complexity of NT-proBNP:

      NT-proBNP, derived from proBNP through enzymatic cleavage, is a stable peptide fragment. It acts as a precursor to the biologically active B-type natriuretic peptide (BNP) hormone. Understanding the molecular structure and processing of NT-proBNP is essential for unraveling the regulatory mechanisms governing its release and its significance in cardiovascular physiology.

      Physiological Significance in Heart Function:

      BNP and its precursor, NT-proBNP, play pivotal roles in cardiac homeostasis. They are secreted by ventricular myocardial cells in response to increased wall stress, primarily due to volume and pressure overload. Elevated levels of NT-proBNP serve as a sensitive indicator of heart failure, reflecting the heart's struggle to maintain effective circulation. Monitoring NT-proBNP levels aids clinicians in diagnosing heart failure, assessing its severity, and guiding therapeutic strategies, ultimately improving patient outcomes.

      Diagnostic Applications and Clinical Relevance:

      NT-proBNP assays, often utilizing recombinant NT-proBNP proteins, have become cornerstones in cardiovascular diagnostics. Elevated levels of NT-proBNP are indicative of heart failure, providing vital information for early intervention and personalized treatment plans. Moreover, the peptide's utility extends to predicting cardiovascular events, aiding in risk stratification among individuals with or at risk of heart diseases. The incorporation of NT-proBNP testing into clinical practice has significantly enhanced the accuracy and timeliness of cardiovascular disease diagnosis.

      Potential Therapeutic Implications:

      Research into NT-proBNP’s regulatory pathways has opened avenues for therapeutic interventions. Targeted therapies aimed at modulating the BNP system are under investigation, offering potential strategies for managing heart failure and related conditions. By understanding the complex interplay between NT-proBNP, its receptor systems, and cardiac function, researchers are exploring novel therapies to optimize cardiovascular health.

      NT-proBNP Recombinant Protein, with its intricate involvement in cardiac physiology and its applications in diagnostics and potential therapeutics, stands as a beacon of hope in the realm of cardiovascular medicine. Its role as a diagnostic marker not only aids in early disease detection but also empowers clinicians to tailor treatments, improving patient outcomes and quality of life. As research continues to unravel the complexities of NT-proBNP, it holds the promise of not only enhancing our understanding of heart diseases but also shaping the future of cardiovascular healthcare. This research underscores the vital role of NT-proBNP in cardiovascular medicine, emphasizing its potential to transform the landscape of heart disease diagnosis and treatment.

      What is the molecular weight / Mw of NT-proBNP Canine?
      NT-proBNP Canine has a total Mw of 10,545 Da.

      What is the source or expression system of NT-proBNP Canine?
      Escherichia Coli.

      What is the Purity of NT-proBNP Canine?
      NT-proBNP Canine is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of NT-proBNP Canine?
      The biological functionality of NT-proBNP Canine will be determined in the future.

      What is the amino acid sequence of NT-proBNP Canine?
      NT-proBNP Canine Protein is composed from 16 amino acids.

      What applications can NT-proBNP Canine be used in?
      NT-proBNP Canine can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for NT-proBNP Canine?
      The endotoxin level is minimal, NT-proBNP Canine 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.

    Probnp Canine
  • View Data Sheet

    Description:

    Creatine Kinase MB Human Recombinant

    CKMB, CK-MB 

     

    Product # :

    CKI-286

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    Description

    Recombinant Human Creatine Kinase MB produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 50mM Tris-HCL, 5mM B-mercaptoethanol, 1mM EDTA, 5mM disodium Succinate, Ph 8.0 and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      CKMB although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.

    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.

    ckmb-protein
  • View Data Sheet

    Description:

    Epstein Barr Virus Induced 3 Human Recombinant

    Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.

    Product # :

    CYT-367

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    Description

    EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 23.3kDa. The EBI3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EBI3 Human Recombinant was lyophilized from a solution containing 10mM Acetic Acid and 0.5% Mannitol.

    Purity

    Greater than 90% as determined by
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.

    More Info

    • Introduction

      EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.

    • Synonyms

      Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 in sterile 10mM Acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
      IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
      NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
      VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
      ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK.

    • Background

      Title: Epstein-Barr Virus Induced 3 Human Recombinant: Unveiling its Role in Epstein-Barr Virus-Associated Diseases

      Abstract:


      Epstein-Barr Virus Induced 3 (EBI3) is a crucial cytokine involved in the immune response against Epstein-Barr virus (EBV) and various other pathogens. This research paper provides an extensive analysis of human recombinant EBI3, focusing on its production, characterization, and potential applications in understanding EBV-associated diseases. The paper highlights the significance of EBI3 in modulating immune responses and explores its role in the pathogenesis of EBV-related malignancies. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EBI3 in immune disorders and cancer. The information presented in this paper aims to enhance our understanding of human recombinant EBI3 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Epstein-Barr Virus Induced 3 (EBI3) is a cytokine that plays a critical role in the immune response against EBV. Human recombinant EBI3, produced through genetic engineering techniques, provides a valuable tool for studying its immunomodulatory properties and exploring its potential therapeutic applications.

      Production and Characterization:


      Recombinant EBI3 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EBI3.

      Role in EBV-Associated Diseases:


      EBI3 is involved in the regulation of immune responses during EBV infection. It acts as a subunit of the heterodimeric cytokine interleukin-27 (IL-27), which plays a crucial role in anti-viral immunity. Recombinant EBI3 serves as a valuable tool for investigating the mechanisms underlying EBI3-mediated immune regulation and its potential implications in EBV-associated diseases, including infectious mononucleosis, nasopharyngeal carcinoma, and EBV-related lymphomas.

      Therapeutic Implications:


      Dysregulation of the immune response is implicated in various immune disorders and cancers. Recombinant EBI3 holds promise as a potential immunotherapeutic agent due to its immunomodulatory properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant EBI3 in conditions such as autoimmune diseases, viral infections, and cancer.

      Conclusion:


      Human recombinant EBI3 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in understanding EBV-associated diseases contribute to our understanding of immune regulation and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EBI3 offer promising avenues for improving outcomes in immune disorders and EBV-related malignancies.

      What is the molecular weight/Mw of EBI3 Protein?
      EBI3 Protein has a total Mw of 23.3kDa.

      What is the source or expression system of EBI3 Protein?
      Escherichia Coli.

      What is the Purity of EBI3 Protein?
      EBI3 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of EBI3 Protein?
      Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.

      What is the amino acid sequence of EBI3 Protein?
      RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
      IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
      NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
      VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
      ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK.

      What applications can EBI3 Protein be used in?
      EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EBI3 Protein?
      The endotoxin level is minimal, EBI3 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.

    Ebi3 Human
  • View Data Sheet

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Rhesus Macaque Recombinant

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

    Product # :

    CYT-720

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Monkey Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.4 kDa.GM-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13. GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APARSPSPGT QPWEHVNAIQ EARRLLNLSR DTAAEMNKTV EVVSEMFDLQ EPSCLQTRLE LYKQGLQGSL TKLKGPLTMM ASHYKQHCPP TPETSCATQI ITFQSFKENL KDFLLVIPFD CWEPVQE.

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    Gm Csf Monkey
  • View Data Sheet

    Description:

    Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant

    ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.

    Product # :

    HSP-091

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    Description

    HSP90B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 819 amino acids (22-803 a.a.) and having a molecular mass of 94.4 kDa.HSP90B1 is expressed with a 36 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GRP94 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM EDTA, 0.1M NaCl, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.

    • Synonyms

      ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDDE VDVDGTVEED LGKSREGSRT DDEVVQREEE AIQLDGLNAS QIRELREKSE KFAFQAEVNR MMKLIINSLY KNKEIFLREL ISNASDALDK IRLISLTDEN ALSGNEELTV KIKCDKEKNL LHVTDTGVGM TREELVKNLG TIAKSGTSEF LNKMTEAQED GQSTSELIGQ FGVGFYSAFL VADKVIVTSK HNNDTQHIWE SDSNEFSVIA DPRGNTLGRG TTITLVLKEE ASDYLELDTI KNLVKKYSQF INFPIYVWSS KTETVEEPME EEEAAKEEKE ESDDEAAVEE EEEEKKPKTK KVEKTVWDWE LMNDIKPIWQ RPSKEVEEDE YKAFYKSFSK ESDDPMAYIH FTAEGEVTFK SILFVPTSAP RGLFDEYGSK KSDYIKLYVR RVFITDDFHD MMPKYLNFVK GVVDSDDLPL NVSRETLQQH KLLKVIRKKL VRKTLDMIKK IADDKYNDTF WKEFGTNIKL GVIEDHSNRT RLAKLLRFQS SHHPTDITSL DQYVERMKEK QDKIYFMAGS SRKEAESSPF VERLLKKGYE VIYLTEPVDE YCIQALPEFD GKRFQNVAKE GVKFDESEKT KESREAVEKE FEPLLNWMKD KALKDKIEKA VVSQRLTESP CALVASQYGW SGNMERIMKA QAYQTGKDIS TNYYASQKKT FEINPRHPLI RDMLRRIKED EDDKTVLDLA VVLFETATLR SGYLLPDTKA YGDRIERMLR LSLNIDPDAK VEEEPEEEPE ETAEDTTEDT EQDEDEEMDV GTDEEEETAK ESTAEKDEL.

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    Hsp90B1 Human
  • View Data Sheet

    Description:

    Candida Albicans Phospholipase B1 Recombinant

    Product # :

    PRO-2809

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    Description

    Recombinant Candida Albicans Phospholipase B1 (24-526 a.a) produced in E. coli having a Mw of 52kDa. C.Albicans PLB1 is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Phosphate buffer and 25mM K2CO3.

    Purity

    Protein is >90% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • 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.

    • Background

      Potential as a Therapeutic Target:

      Understanding the role of PLB1 in fungal pathogenesis opens avenues for developing novel antifungal strategies. Inhibiting PLB1 activity could potentially render C. albicans less virulent and susceptible to host immune defenses. Recombinant Candida Albicans Phospholipase B1 studies play a critical role in identifying and characterizing potential inhibitors that could form the basis for antifungal drug development.

      Challenges and Future Directions:

      While the potential of Recombinant Candida Albicans Phospholipase B1 in antifungal research is promising, challenges persist. Fine-tuning its applications, deciphering its role in different infection scenarios, and optimizing strategies for therapeutic use are critical considerations for translational success. Additionally, understanding the interplay between PLB1 and other virulence factors in C. albicans pathogenesis remains an active area of investigation.

      Recombinant Candida Albicans Phospholipase B1 emerges as a key player in the intricate dance between the fungus and its human host. Its structural insights, enzymatic activities, and implications in host-pathogen interactions position it as a central focus in the exploration of C. albicans virulence. As researchers continue to unravel the molecular intricacies of PLB1, they not only deepen our understanding of fungal pathogenesis but also pave the way for transformative advancements in antifungal drug development, shaping the future of precision medicine in the realm of fungal infections.

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    Candida Albicans Plb1
  • View Data Sheet

    Description:

    Cytohesin 3 Human Recombinant

    Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.

    Product # :

    PRO-1951

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    Description

    CYTH3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (1-399) and having a molecular mass of 48.7 kDa.CYTH3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CYTH3 solution (0.25mg/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.

    More Info

    • Introduction

      Cytohesin 3 (CYTH3) belongs to the PSCD family, whose members have identical structural organization which consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain, and seem to mediate the regulation of protein sorting and membrane trafficking. CYTH3 is involved in the regulation of Golgi structure and function, and it might have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.

    • Synonyms

      Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.

    • 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 MGSMDEDGGG EGGGVPEDLS LEEREELLDI RRRKKELIDD IERLKYEIAE VMTEIDNLTS VEESKTTQRN KQIAMGRKKF NMDPKKGIQF LIENDLLQSS PEDVAQFLYK GEGLNKTVIG DYLGERDEFN IKVLQAFVEL HEFADLNLVQ ALRQFLWSFR LPGEAQKIDR MMEAFASRYC LCNPGVFQST DTCYVLSFAI IMLNTSLHNH NVRDKPTAER FIAMNRGINE GGDLPEELLR NLYESIKNEP FKIPEDDGND LTHTFFNPDR EGWLLKLGGR VKTWKRRWFI LTDNCLYYFE YTTDKEPRGI IPLENLSIRE VEDPRKPNCF ELYNPSHKGQ VIKACKTEAD GRVVEGNHVV YRISAPSPEE KEEWMKSIKA SISRDPFYDM LATRKRRIAN KK.

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    Cyth3 Human
  • View Data Sheet

    Description:

    Collapsin Response Mediator Protein-1 Mouse Recombinant

    Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.

    Product # :

    PRO-2521

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    Description

    CRMP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (1-572 a.a) and having a molecular mass of 64.8kDa.CRMP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CRMP1 protein solution (0.25mg/ml) contains 40% glycerol, 20mM Tris-HCl (pH 8.5), 0.2M NaCl & 0.1mM PMSF.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation as well as axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.

    • Synonyms

      Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, Unc-33-like phosphoprotein 3, ULIP-3.

    • 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 MGSEFMSHQG KKSIPHITSD RLLIRGGRII NDDQSFYADV YLEDGLIKQI GENLIVPGGV KTIEANGRMV IPGGIDVNTY LQKPSQGMTS ADDFFQGTKA ALAGGTTMII DHVVPEPGSS LLTSFEKWHE AADTKSCCDY SLHVDITSWY DGVREELEVL VQDKGVNSFQ VYMAYKDLYQ MSDSQLYEAF TFLKGLGAVI LVHAENGDLI AQEQKRILEM GITGPEGHAL SRPEELEAEA VFRAIAIAGR INCPVYITKV MSKSAADIIA LARKKGPLVF GEPIAASLGT DGTHYWSKNW AKAAAFVTSP PLSPDPTTPD YLTSLLACGD LQVTGSGHCP YSTAQKAVGK DNFTLIPEGV NGIEERMTVV WDKAVATGKM DENQFVAVTS TNAAKIFNLY PRKGRIAVGS DADVVIWDPD KMKTITAKSH KSTVEYNIFE GMECHGSPLV VISQGKIVFE DGNISVSKGM GRFIPRKPFP EHLYQRVRIR SKVFGLHSVS RGMYDGPVYE VPATPKHAAP APSAKSSPSK HQPPPIRNLH QSNFSLSGAQ IDDNNPRRTG HRIVAPPGGR SNITSLG.

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    CRMP1 Mouse
  • View Data Sheet

    Description:

    C-type Lectin Domain Family 2, Member B Human Recombinant, Sf9

    C-Type Lectin Domain Family 2 Member B, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 2 (Activation-Induced), IFN-Alpha-2b-Inducing-Related Protein 1, C-Type Lectin Superfamily Member 2, Activation-Induced C-Type Lectin, CLECSF2, IFNRG1, AICL, C-Type Lectin Domain Family 2 Member B, IFN-Alpha2b-Inducing Related Protein 1, HP10085.

    Product # :

    PRO-2542

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    Description

    CLEC2B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 366 amino acids (26-149a.a.) and having a molecular mass of 41.7kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CLEC2B is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques

    Source

    Sf9, Baculovirus cells.

    Formulation

    CLEC2B 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

      C-type Lectin Domain Family 2, Member B (CLEC2B) belongs to the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of the CTL/CTLD family share a common protein fold and have various functions, such as cell adhesion, cell-cell signaling, glycoprotein turnover, and roles in inflammation and immune response. The CLEC2B gene is closely connected to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. CLEC2B is expressed preferentially in lymphoid tissues, and in most hematopoietic cell types.

    • Synonyms

      C-Type Lectin Domain Family 2 Member B, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 2 (Activation-Induced), IFN-Alpha-2b-Inducing-Related Protein 1, C-Type Lectin Superfamily Member 2, Activation-Induced C-Type Lectin, CLECSF2, IFNRG1, AICL, C-Type Lectin Domain Family 2 Member B, IFN-Alpha2b-Inducing Related Protein 1, HP10085.

    • 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

      ADPKLTRDSQ SLCPYDWIGF QNKCYYFSKE EGDWNSSKYN CSTQHADLTI IDNIEEMNFL RRYKCSSDHW IGLKMAKNRT GQWVDGATFT KSFGMRGSEG CAYLSDDGAA TARCYTERKW ICRKRIHLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

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    Clec2B Protein
  • View Data Sheet

    Description:

    Adiponectin Mouse Recombinant, Trimeric form

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-247

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    Description

    Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

    Purity

    Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
      In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      Filtered white lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse 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

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

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293

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

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

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

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

    Adiponectin Mouse Trimeric
  • View Data Sheet

    Description:

    Creatine Kinase MB Isoenzyme Type-1 Human Recombinant

    Creatine Kinase MB 1, CKMB1

    Product # :

    CKI-269

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    Description

    CKMB1 Human Recombinant produced in E.Coli is a non covalently linked heterodimer that consists of 381 a.a. and having a total Mw of ~85.6kDa. The CKMB1 is purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    CKMB1 was lyophilized a concentrated solution containing 20mM Tris, 150mM NaCl, pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    CKMB1 activity was measured kinetically by the CK-NAC assay at 37°C which was found to be between 500-600 units/mg. 1U converts 1µmole of creatine phosphate to creatine/min at 37˚C

    More Info

    • Introduction

      The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

    • Synonyms

      Creatine Kinase MB Isoenzyme Type-1, CK MB1

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized CKMB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 CKMB1 in sterile 18MΩ-cm H2O at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CKM1
      MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ

      CKB
      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K

    • Background

      What is the molecular weight / Mw of CKMB1 Protein?
      CKMB1 Protein is a non covalently heterodimer having a total Mw of 85.6

      What is the source or expression system of CKMB1 Protein?
      Escherichia Coli.

      What is the Purity of CKMB1 Protein?
      CKMB1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CKMB1 Protein?
      The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.

      What is the amino acid sequence of CKMB1 Protein?
      CKM1
      MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ
      CKB
      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K

      What applications can CKMB1 Protein be used in?
      CKMB1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CKMB1 Protein?
      The endotoxin level is minimal, CKMB1 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.

    Ckmbi Human
  • View Data Sheet

    Description:

    Complement Component 1, Mouse Anti Human

    p32, HABP1, gC1Qr, GC1QBP, SF2p32, gC1Q-R, Complement component 1 Q subcomponent-binding protein mitochondrial, Glycoprotein gC1qBP, C1qBP, GC1q-R protein, Hyaluronan-binding protein 1, Mitochondrial matrix protein p32, p33, C1QBP.

    Product # :

    ANT-556

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    Formulation

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

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    • Introduction

      C1QBP binds to the globular "heads" of c1q thus inhibiting c1 activation. C1QBP interacts with a wide range of ligands and is implicated in cell signaling. C1QBP associates with C1r and C1s in order to yield the first component of the serum complement system. C1QBP protein has been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein.
      C1QBP is a new marker of tumor cells and tumor-associated macrophages/myeloid cells in hypoxic/metabolically deprived areas of tumors.
      Mitochondrial C1QBP is a critical mediator of p14ARF-induced apoptosis.
      C1QBP functions as a chemotactic factor for immature dendritic cells, and migration is mediated through ligation of both C1QBP and cC1qR/CR.
      C1QBP overexpression successfully blocks mRNA accumulation from the adenovirus major late transcription unit (MLTU) and stimulates RNA polymerase II carboxy-terminal domain phosphorylation in virus-infected cells.
      C1QBP binds with Hepacivirus core protein on CD8+ and CD4+ positive t-cells and inactivates lck and akt.

    • Synonyms

      p32, HABP1, gC1Qr, GC1QBP, SF2p32, gC1Q-R, Complement component 1 Q subcomponent-binding protein mitochondrial, Glycoprotein gC1qBP, C1qBP, GC1q-R protein, Hyaluronan-binding protein 1, Mitochondrial matrix protein p32, p33, C1QBP.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human C1QBP mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human C1QBP protein 74-282 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT1G7AT.

    • Applications

      C1QBP antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      C1QBP antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    C1Qbp Antibody
  • View Data Sheet

    Description:

    Macrophage Inflammatory Protein-5 Human Recombinant (CCL15)

    Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.

    Product # :

    CHM-230

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    Description

    Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10.1 kDa. The MIP5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIP5 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 100mM NaCl.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.

    • Synonyms

      Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 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 MIP5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.

    • Background

      What is the molecular weight/Mw of CCL15 HUMAN Protein?
      CCL15 HUMAN Protein has a total Mw of 10.1kDa.

      What is the source or expression system of CCL15 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL15 HUMAN Protein?
      CCL15 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL15 HUMAN Protein?
      Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CCL15 HUMAN Protein?
      QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.

      What applications can CCL15 HUMAN Protein be used in?
      CCL15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL15 HUMAN Protein?
      The endotoxin level is minimal, CCL15 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.

    Mip 5 Human
  • View Data Sheet

    Description:

    Platelet Factor-4 Human Recombinant (CXCL4)

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-350

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    Description

    CXCL4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    The CXCL4 protein was filtered (0.2µm) and lyophilized from a concentrated solution containing 20mM PB and 1.5M NaCl, pH 7.4.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human fibroblasts is in a concentration of 1.0-10 ng/ml.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized CXCL4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL4 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 CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EAEEDGDLQC LCVKTTSQVR PRHITSLEVI KAGPHCPTAQ LIATLKNGRK ICLDLQAPLY KKIIKKLLES.

    • Background

      What is the molecular weight/Mw of PLATELET FACTOR 4 HUMAN Protein?
      PLATELET FACTOR 4 HUMAN Protein has a total Mw of 7.8kDa.

      What is the source or expression system of PLATELET FACTOR 4 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of PLATELET FACTOR 4 HUMAN Protein?
      PLATELET FACTOR 4 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of PLATELET FACTOR 4 HUMAN Protein?
      The biological activity determined by a chemotaxis bioassay using human fibroblasts is in a concentration of 1.0-10 ng/ml.

      What is the amino acid sequence of PLATELET FACTOR 4 HUMAN Protein?
      EAEEDGDLQC LCVKTTSQVR PRHITSLEVI KAGPHCPTAQ LIATLKNGRK ICLDLQAPLY KKIIKKLLES.

      What applications can PLATELET FACTOR 4 HUMAN Protein be used in?
      PLATELET FACTOR 4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for PLATELET FACTOR 4 HUMAN Protein?
      The endotoxin level is minimal, PLATELET FACTOR 4 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.

    Pf 4 Human Recombinant
  • View Data Sheet

    Description:

    Uncoupling protein 3 Human Recombinant

    Product # :

    PRO-2821

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    Description

    The UCP3 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCP3 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 34 amino acid residues of the Resistin Human, 181-214 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized UCP3 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      Uncoupling protein 3 (UCP3) is a mitochondrial protein which takes part in energy metabolism and thermoregulation.

      UCP3 Function

      Proton Uncoupling - UCP3 helps dissipate the proton gradient across the inner mitochondrial membrane. This uncoupling leads to the production of heat instead of ATP, a necessary process for thermogenesis.

      Energy Regulation - UCP3 takes part in the regulation of energy expenditure and can influence metabolic efficiency.

      UCP3 Location

      UCP3 is predominantly expressed in skeletal muscle and brown adipose tissue, where its activity is critical for energy metabolism.

      UCP3 Role in Metabolism

      according to some studies, UCP3 may improve insulin sensitivity and help manage body weight. In addition, UCP3 participates in the metabolism of fatty acids and may help reduce the accumulation of reactive oxygen species (ROS) by decreasing oxidative stress.

      UCP3 Regulation

      UCP3 expression can raise in response to physical activity, emphasising its role in adapting to varius energy demands during exercise.

      Changes in UCP3 levels have been associated with diabetes, obesity and other metabolic disorders.

      Clinical Relevance

      UCP3 is being investigated as a potential target for obesity and metabolic disease treatments because of its role in energy balance

      UCP3 is a central player in energy metabolism and thermogenesis, with implications for metabolic health and the body's response to exercise and diet.

    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.

    Ucp3 Human
  • View Data Sheet

    Description:

    Macrophage Inflammatory protein-4 (CCL18) Human Recombinant, His-Tag

    Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

    Product # :

    CHM-339

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    Description

    MIP-4 Human Recombinant fused with a 25 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (22-89 a.a.) and having a molecular mass of 10.4kDa. The MIP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MIP-4 solution (0.25 mg/ml) contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 18 (CCL18) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). CCL18 is approximately 60% identical in amino acid sequence to CCL3. It is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

    • 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 MGSHMQVGTN KELCCLVYTS WQIPQKFIVD YSETSPQCPK PGVILLTKRG RQICADPNKK WVQKYISDLK LNA.

    • Background

      What is the molecular weight/Mw of CCL18 HUMAN, HIS Protein?
      CCL18 HUMAN, HIS Protein has a total Mw of 10.4kDa.

      What is the source or expression system of CCL18 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL18 HUMAN, HIS Protein?
      CCL18 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL18 HUMAN, HIS Protein?
      The biological functionality of CCL18 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL18 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMQVGTN KELCCLVYTS WQIPQKFIVD YSETSPQCPK PGVILLTKRG RQICADPNKK WVQKYISDLK LNA.

      What applications can CCL18 HUMAN, HIS Protein be used in?
      CCL18 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL18 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL18 HUMAN, HIS 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.

    Mip 4 Human His
  • View Data Sheet

    Description:

    BCA-1/ BLC (CXCL13) Rhesus Macaque Recombinant

    C-X-C motif chemokine 13, Small-inducible cytokine B13, B lymphocyte chemoattractant, CXC chemokine BLC, CXCL13, BCA1, BCA-1, CXCL-13, B cell Attracting Chemokine-1, BLC, ANGIE, BLR1L, SCYB13, ANGIE2.

    Product # :

    CHM-035

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    Description

    BCA-1/ BLC (CXCL13) Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 87 amino acid and having a molecular mass of approximately 10.3kDa.BCA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0 and 300mM NaCl.

    Purity

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

    More Info

    • Introduction

      BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.

    • Synonyms

      C-X-C motif chemokine 13, Small-inducible cytokine B13, B lymphocyte chemoattractant, CXC chemokine BLC, CXCL13, BCA1, BCA-1, CXCL-13, B cell Attracting Chemokine-1, BLC, ANGIE, BLR1L, SCYB13, ANGIE2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA-1/ BLC (CXCL13) Rhesus Macaque 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 BCA-1/ BLC (CXCL13) Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VLEVYYTHLR CRCVQESSVF IPRRFIDRIQ ISPRGNGCPR KEIIVWKKNK SVVCVDPQAE WIQRIMEMLR KKSSSTPPVP VFKRKIP.

    • Background

      What is the molecular weight/Mw of CXCL13 MACAQUE Protein?
      CXCL13 MACAQUE Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CXCL13 MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of CXCL13 MACAQUE Protein?
      CXCL13 MACAQUE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL13 MACAQUE Protein?
      The biological functionality of CXCL13 MACAQUE Protein will be determined in the future.

      What is the amino acid sequence of CXCL13 MACAQUE Protein?
      VLEVYYTHLR CRCVQESSVF IPRRFIDRIQ ISPRGNGCPR KEIIVWKKNK SVVCVDPQAE WIQRIMEMLR KKSSSTPPVP VFKRKIP.

      What applications can CXCL13 MACAQUE Protein be used in?
      CXCL13 MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL13 MACAQUE Protein?
      The endotoxin level is minimal, CXCL13 MACAQUE 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.

    Bca1 Monkey
  • View Data Sheet

    Description:

    Complement C3b Rabbit

    Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

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    PRO-2814

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    Description

    Rabbit Complement C3b is composed of 2 disulfide-linked chains having a molecular weight of 176kDa.

    Source

    Rabbit serum.

    Formulation

    C3b Rabbit solution contains PBS, pH 7.2.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      C3b is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -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.

    • Background

      Rabbit C3b serves as a critical opsonin, enhancing the recognition and engulfment of pathogens and immune complexes by phagocytic cells. Through its covalent attachment to target surfaces, C3b facilitates the recognition of foreign antigens and promotes their clearance by the immune system. C3b contributes to the inflammatory response by generating C5 convertase complexes, leading to the cleavage of C5 into C5a and C5b. C5a is a potent chemoattractant and activator of immune cells, promoting the recruitment of neutrophils and macrophages to sites of infection or tissue damage.

    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.

    C3B Rabbit
  • View Data Sheet

    Description:

    Epstein - Barr virus (HHV-4) p18 Recombinant, GST Tag

    Product # :

    EBV-277

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    Description

    The E.Coli derived recombinant protein contains the HHV-4 p18 regions, having a molecular mass of 35.4kDa which includes GST tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    3.8mg/ml in 50mM Tris-HCl, pH 8.0.

    Purity

    Protein is >90% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virus of the herpes family (which includes Herpes simplex virus and Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expression which can be broadly categorized as being lytic cycle or latent cycle. The lytic cycle or productive infection results in staged expression of a host of viral proteins with the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cell as EBV virions are produced by budding from the infected cell. The latent cycle (lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen (EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins (LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs (EBERs).

    • Stability

      EBV p18, GST although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      ASAGTGALAS SAPSTAVAQS ATPSVSSSIS SLRAATSGAT AAASAAAAVD TGSGGGGQPH DTAPRGARKK Q.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Ebv P18 Gst
  • View Data Sheet

    Description:

    Ephrin-B1 Human Recombinant

    ephrin-B1, LERK2, EPLG2, Elk-L, EPH-related receptor tyrosine kinase ligand 2, EFL-3, ELK ligand, CFND, CFNS, Craniofrontonasal Syndrome (craniofrontonasal dysplasia), MGC8782.

    Product # :

    PRO-918

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    Description

    EFNB1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (28-237) and having a molecular mass of 25.3 kDa.The EFNB1 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EFNB1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.

    • Synonyms

      ephrin-B1, LERK2, EPLG2, Elk-L, EPH-related receptor tyrosine kinase ligand 2, EFL-3, ELK ligand, CFND, CFNS, Craniofrontonasal Syndrome (craniofrontonasal dysplasia), MGC8782.

    • 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 MLAKNLEPVS WSSLNPKFLS GKGLVIYPKI GDKLDIICPR AEAGRPYEYY KLYLVRPEQA AACSTVLDPN VLVTCNRPEQ EIRFTIKFQE FSPNYMGLEF KKHHDYYITS TSNGSLEGLE NREGGVCRTR TMKIIMKVGQ DPNAVTPEQL TTSRPSKEAD NTVKMATQAP GSRGSLGDSD GKHETVNQEE KSGPGASGGS SGDPDGFFNS K

    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.

    Efnb1 Human