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Search results

1000 results found for “Resistin”

Name

Description

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  • View Data Sheet

    Name :

    CST1 Human

    Description:

    Cystatin SN Human Recombinant

    Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.

    Product # :

    PRO-1006

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    Description

    CST1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (21-141 a.a.) and having a molecular mass of 16.9kDa. CST1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CST1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cystatin-SN (CST1) belongs to the type 2 salivary cystatin family found in a variety of fluids and secretions, including plasma, tears, and saliva. The cystatin superfamily includes proteins which contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, whereas others have lost or possibly never developed this inhibitory activity. CST1 is up-regulated in cancerous lesions of gastric cancer tissues compared to noncancerous regions, in addition clinicopathological analysis revealed a significant correlation between high expression of CST1.

    • Synonyms

      Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.

    • 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 MGSMWSPKEE DRIIPGGIYN ADLNDEWVQR ALHFAISEYN KATKDDYYRR PLRVLRARQQ TVGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WENRRSLVKS RCQES.

    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.

    Cst1 Human
  • View Data Sheet

    Name :

    CST4 Human

    Description:

    Cystatin 4 Human Recombinant

    Cystatin-SA-III, Cystatin-4, cystatin S, Salivary acidic protein 1.

    Product # :

    PRO-1097

    Price :

    Quantity :

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    Description

    CST4 Human Recombinant produced in E. coli is a single polypeptide chain containing 145 amino acids (21-141) and having a molecular mass of 16.8kDa.CST4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CST4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CST4 is a member of the cystatin superfamily which contains proteins that hold multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, whereas others have lost or possibly never attained this inhibitory activity. CST4 strongly inhibits papain (non-competitively) and ficin, partially inhibits stem bromelain and bovine cathepsin C, however does not inhibit porcine cathepsin B or clostripain.

    • Synonyms

      Cystatin-SA-III, Cystatin-4, cystatin S, Salivary acidic protein 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSSSKEE NRIIPGGIYD ADLNDEWVQR ALHFAISEYN KATEDEYYRR PLQVLRAREQ TFGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WEDRMSLVNS RCQEA

    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.

    Cst4 Human
  • View Data Sheet

    Name :

    ACTN1 Human

    Description:

    Actinin Alpha 1 Human Recombinant

    ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.

    Product # :

    PRO-2227

    Price :

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    Description

    ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

    • Synonyms

      ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.

    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.

    Actn1 Human
  • View Data Sheet

    Name :

    DEFB118 Human

    Description:

    Beta Defensin 118 Human Recombinant

    Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    Product # :

    CYT-714

    Price :

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    • sds-page
    • Citations

    Description

    DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    DEFB118-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.

    • Synonyms

      Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    • 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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

    • Background

      Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications

      Abstract:


      Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.

      Production and Characterization:


      Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. 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 BD118.

      Role in Innate Immunity:


      BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.

      Therapeutic Implications:


      Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.

      Conclusion:


      Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.

      What is the molecular weight/Mw of DEFB118 Protein?
      DEFB118 Protein has a total Mw of 13.8kDa.

      What is the source or expression system of DEFB118 Protein?
      Escherichia Coli.

      What is the Purity of DEFB118 Protein?
      DEFB118 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of DEFB118 Protein?
      The biological functionality of DEFB118 Protein will be determined in the future.

      What is the amino acid sequence of DEFB118 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

      What applications can DEFB118 Protein be used in?
      DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DEFB118 Protein?
      The endotoxin level is minimal, DEFB118 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.

    Defb118 Human
  • View Data Sheet

    Name :

    ANXA5 Human

    Description:

    Annexin A5 Human Recombinant

    PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.

    Product # :

    PRO-732

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    Description

    ANXA5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-320 a.a.) and having a molecular mass of 35.9 kDa.ANXA5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA5 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.

    • Synonyms

      PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.

    • 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

      MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI KGDTSGDYKK ALLLLCGEDD.

    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.

    Anxa5 Human
  • View Data Sheet

    Name :

    NRTN Human

    Description:

    Neurturin Human Recombinant

    Neurturin.

    Product # :

    CYT-818

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    Description

    NRTN Human Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains consisting of two 102 amino acids and having a molecular mass of 23.4kDa.

    Source

    Escherichia Coli.

    Formulation

    NRTN protein was lyophilized from a 0.2 µm filtered concentrated solution in 30 mM Citrate Sodium, pH 4.2, 400 mM NaCl, with 0.02 % Tween-20.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The biologically active as determined by its binding ability in a functional ELISA.

    Citations

    More Info

    • Introduction

      NRTN belongs to the GDNF family of ligands, a distant member of the TGF-beta superfamily. NRTN, a ligand used to bind to GFRA2 receptors, signals through RET and a GPI-linked coreceptor, and promotes endurance of neuronal populations, controls the size of non-neuronal cell population such as haemopoietic cells and regulate the development and maintenance of the CNS. Mutation in NRTN results in Hirschsprung Disease.

    • Synonyms

      Neurturin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NRTN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRTN 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 NRTN in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ARLGARPCGL RELEVRVSEL GLGYASDETV LFRYCAGACE AAARVYDLGL RRLRQRRRLR RERVRAQPCC RPTAYEDEVS FLDAHSRYHT VHELSARECA CV

    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.

    Nrtn Human
  • View Data Sheet

    Name :

    Elcatonin

    Description:

    Elcatonin

    Product # :

    HOR-302

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    Description

    Elcatonin Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3363.2 Dalton and a Molecular formula of C148H244N42O47.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 93.3% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.

    Citations

    More Info

    • Introduction

      Elcatonin is a Calcitonin derivative which is transformed from eel´s calcitonin by changing the S-S bond into the stable C-N bond. It inhibits the absorption and autolysis of bones, thus leads to blood calcium descending. In addition, it inhibits the bone salts dissolving and transferring and promotes the excretion of calcium and phosphorus in urine. Meanwhile, it inhibits renal tubules reabsorbing calcium, phosphorus and sodium and keeps blood calcium at normal level. It is mainly used for remitting or eliminating the pain caused by Osteoporosis.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.

    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.

    Elcatonin
  • View Data Sheet

    Name :

    CCL24 Human

    Description:

    Eotaxin-2 Human Recombinant (CCL24)

    C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    Product # :

    CHM-238

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    Description

    CCL24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8.8 kDa. The CCL24 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

    Purity

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

    Biological Activity

    The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

    Citations

    More Info

    • Introduction

      Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
      CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

    • Synonyms

      C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Human Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
      DPKQEWV QRYMKNLDAKQKKASPRARAVA.

    • Background

      What is the molecular weight/Mw of CCL24 HUMAN Protein?
      CCL24 HUMAN Protein has a total Mw of 8.8kDa.

      What is the source or expression system of CCL24 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL24 HUMAN Protein?
      CCL24 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL24 HUMAN Protein?
      The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

      What is the amino acid sequence of CCL24 HUMAN Protein?
      VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
      DPKQEWV QRYMKNLDAKQKKASPRARAVA.

      What applications can CCL24 HUMAN Protein be used in?
      CCL24 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL24 HUMAN Protein?
      The endotoxin level is minimal, CCL24 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL24 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL24 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Ccl24 Human
  • View Data Sheet

    Name :

    KRT19 Human, His

    Description:

    Cytokeratin 19 Human Recombinant , His Tag

    Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.

    Product # :

    PRO-1347

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    Description

    KRT19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 46.5kDa.KRT19 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KRT19 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CTK-19 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Unlike its related family members, this smallest known acidic cytokeratin is not paired with a basic cytokeratin in epithelial cells. It is specifically expressed in the periderm, the transiently superficial layer that envelopes the developing epidermis. The type I cytokeratins are clustered in a region of chromosome 17q12-q21.

    • Synonyms

      Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTSYSYR QSSATSSFGG LGGGSVRFGP GVAFRAPSIH GGSGGRGVSV SSARFVSSSS SGAYGGGYGG VLTASDGLLA GNEKLTMQNL NDRLASYLDK VRALEAANGE LEVKIRDWYQ KQGPGPSRDY SHYYTTIQDL RDKILGATIE NSRIVLQIDN ARLAADDFRT KFETEQALRM SVEADINGLR RVLDELTLAR TDLEMQIEGL KEELAYLKKN HEEEISTLRG QVGGQVSVEV DSAPGTDLAK ILSDMRSQYE VMAEQNRKDA EAWFTSRTEE LNREVAGHTE QLQMSRSEVT DLRRTLQGLE IELQSQLSMK AALEDTLAET EARFGAQLAH IQALISGIEA QLGDVRADSE RQNQEYQRLM DIKSRLEQEI ATYRSLLEGQ EDHYNNLSAS KVL.

    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.

    Krt19 Human His
  • View Data Sheet

    Name :

    CPLX1 Human

    Description:

    Complexin-1 Human Recombinant

    CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

    Product # :

    PRO-645

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    Description

    CPLX1 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 17.1kDa (molecular weight on SDS-PAGE will appear higher).The CPLX1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CPLX1protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 90% by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CPLX1 is part of the SNARE family complex binding proteins that are catalysts or inhibitors of vesicle exocytosis. CPLX1 shows reduced Ca2+-triggered fast neurotransmitter release at hippocampal glutamatergic synapses, indicating that CPLX1 is a positive regulator of transmitter release. In contrast, CPLX1 inhibits SNARE-mediated liposome and cell fusions in vitro, that result in hypothesis thus acts as a fusion clamp of synaptic exocytosis. CPLX1 regulates a late step in synaptic vesicle exocytosis.

    • Synonyms

      CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

    • 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 MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE AVRQGIRDKYGIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV IKYLPGPLQD MLKK.

    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.

    Cplx1 Human
  • View Data Sheet

    Name :

    Adiponectin Rat

    Description:

    Adiponectin Rat Recombinant

    Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-831

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    Description

    ACRP30 Rat Recombinant produced in 293 cell line is a polypeptide chain containing 238 amino acids and having a total molecular mass of 25.7 kDa. ACRP30 contains a C-Terminal linker (3 AA residue) and a C-Terminal Flag- tag (8 AA residue).

    Source

    HEK293 cell line.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

      Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ACRP30 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ACRP30 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

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

    • Amino Acid Sequence

      GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 25.7kDa.

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

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >90% 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 is the amino acid sequence of ADIPONECTIN Protein?
      GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK.

      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.

    Acrp30 Rat
  • View Data Sheet

    Name :

    Cardiac Actin Bovine

    Description:

    Cardiac Actin Bovine

    Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.

    Product # :

    PRO-519

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    Description

    Ultra pure Cardiac Actin having a Molecular mass of 43,000 dalton.

    Source

    Bovine Heart.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM Tris-acetate buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% SDS.

    Purity

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

    Citations

    More Info

    • Introduction

      Alpha-cardiac actin belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in the cardiac actin have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).

    • Synonyms

      Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      Protein standard in 1D and 2D SDS gelelectrophoresis
      Immunoassays
      Immunization.

    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.

    Cardiac Actin
  • View Data Sheet

    Name :

    Adiponectin Human, HEK

    Description:

    Adiponectin Human Recombinant, HEK

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

    Product # :

    CYT-434

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    • sds-page
    • Citations

    Description

    Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.

    Purity

    Greater than 98% as determined by HPLC and SDS PAGE.

    Biological Activity

    In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

    sds-page

    adiponectin human HEK sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

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

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.

    • Solubility

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

    • Amino Acid Sequence

      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

    • Background

      What is the molecular weight/Mw of adiponectin Protein?
      Adiponectin Protein has a total Mw of 25.5kDa.

      What is the source or expression system of adiponectin Protein?
      HEK293.

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

      What is the Biological Activity of adiponectin Protein?
      In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

      What is the amino acid sequence of adiponectin Protein?
      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

      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 Human Hek
  • View Data Sheet

    Name :

    Conglutin

    Description:

    Allergen Ara h 6.0101 Recombinant

    Conglutin, Allergen Ara h 6.

    Product # :

    ALR-009

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    Description

    Recombinant Conglutin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 16,217 Dalton. Conglutin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Conglutin is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Conglutin, also known as Ara h 6.0101 is a part of the 2S albumin protein family. Conglutin along with Ara h 2.0201 are considered as some of the most potent elicitors of anaphylaxis. Both proteins hold multiple disulphide-bridged cysteine residues, resulting in a tightly coiled, heat-stable, protease resistant core structure. Conglutin causes an allergic reaction in human and binds to IgE.

    • Synonyms

      Conglutin, Allergen Ara h 6.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Conglutin
  • View Data Sheet

    Name :

    TIGIT Human

    Description:

    T-Cell Immunoreceptor With Ig And ITIM Domains Human Recombinant

    VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.

    Product # :

    PRO-2498

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    Description

    TIGIT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 359 amino acids (22-141a.a.) and having a molecular mass of 40.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TIGIT is expressed with a 239 amino acid hlgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TIGIT protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      T cell immunoreceptor with Ig and ITIM domains or TIGIT, is an immune receptor located on part of T cells and Natural Killer Cells(NK). TIGIT is also known as Vstm3 and WUCAM. The receptor can bind with high affinity to dendritic cells(DCs), CD155(PVR) on macrophages, etc., and it can bind with lower affinity to CD112(PVRL2). TIGIT can inhibit the cytotoxicity of Natural Killer Cells through its ITIM domain via antibodies against the interaction with PVR and the activity is directed. It has been show on research that TIGIT-Fc fusion molecule can have interaction with PVR on dendritic cells and elevate its IL-10 secretion level or lower the secretion on IL-12 under the stimulation of LPS, moreover, it can inhibit the activation of T cell in vivo.

    • Synonyms

      VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.

    • 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

      MMTGTIETTG NISAEKGGSI ILQCHLSSTT AQVTQVNWEQ QDQLLAICNA DLGWHISPSF KDRVAPGPGL GLTLQSLTVN DTGEYFCIYH TYPDGTYTGR IFLEVLESSV AEHGARFQIP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.

    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.

    Tigit Human
  • View Data Sheet

    Name :

    NECTIN3 Human

    Description:

    Nectin Cell Adhesion Molecule 3 Human Recombinant

    Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3. 

    Product # :

    PRO-2504

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    Description

    NECTIN3 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 355 amino acids (58-404 a.a.) and having a molecular mass of 39.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    NECTIN3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NECTIN3, also known as Nectin Cell Adhesion Molecule 3, is part of the nectin family. NECTIN3 is intended to initiate cell-cell adhesion to stimulate cell attachment and to allow subsequent formation of JAM-and cadherin-based intercellular junctions. NECTIN3 induces endocytosis-mediated down-regulation of PVR from the cell surface, which results in reduction of cell movement & proliferation. Following Nectin-3 activity adds strength to the junction through trans-interaction with various molecules.

    • Synonyms

      Nectin-3, CDw113, Nectin cell adhesion molecule 3, Poliovirus receptor-related protein 3, CD113, PVRL3, PRR3, NECTIN-3, PVRR3, PPR3.

    • 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

      GPIIVEPHVT AVWGKNVSLK CLIEVNETIT QISWEKIHGK SSQTVAVHHP QYGFSVQGEY QGRVLFKNYS LNDATITLHN IGFSDSGKYI CKAVTFPLGN AQSSTTVTVL VEPTVSLIKG PDSLIDGGNE TVAAICIAAT GKPVAHIDWE GDLGEMESTT TSFPNETATI ISQYKLFPTR FARGRRITCV VKHPALEKDI RYSFILDIQY APEVSVTGYD GNWFVGRKGV NLKCNADANP PPFKSVWSRL DGQWPDGLLA SDNTLHFVHP LTFNYSGVYI CKVTNSLGQR SDQKVIYISD PPTTTTLQPT IQWHPSTADI EDLATEPKKL PFPLSTLATI KDDTIATLEH HHHHH.

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

    Nectin3 Human
  • View Data Sheet

    Name :

    RSG1 Human

    Description:

    REM2 and RAB-Like Small GTPase 1 Human Recombinant

    REM2- and Rab-like small GTPase 1, RSG1, C1orf89, RP4-733M16.4.

    Product # :

    PRO-1334

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    Description

    RSG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-258 a.a) and having a molecular mass of 30.9kDa.RSG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RSG1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      REM2 and RAB-Like Small GTPase 1 (RSG1) plays a part in targeted membrane trafficking most likely at the level of vesicle fusion with membranes. The RSG1 protein is involved in cilium biogenesis by regulating the transportation of cargo proteins to the basal body and to the apical tips of cilia. RSG1 is a potential effector of the planar cell polarity signaling pathway. RSG1 is also involved in exocytosis in secretory cells.

    • Synonyms

      REM2- and Rab-like small GTPase 1, RSG1, C1orf89, RP4-733M16.4.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMARPPVP GSVVVPNWHE SAEGKEYLAC ILRKNRRRVF GLLERPVLLP PVSIDTASYK IFVSGKSGVG KTALVAKLAG LEVPVVHHET TGIQTTVVFW PAKLQASSRV VMFRFEFWDC GESALKKFDH MLLACMENTD AFLFLFSFTD RASFEDLPGQ LARIAGEAPG VVRMVIGSKF DQYMHTDVPE RDLTAFRQAW ELPLLRVKSV PGRRLADGRT LDGRAGLADV AHILNGLAEQ LWHQDQVAAG LLPNPPESAP E.

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    Rsg1 Human
  • View Data Sheet

    Name :

    SNX1 Human

    Description:

    Sorting Nexin 1 Human Recombinant

    HsT17379, SNX1A, Vps5.

    Product # :

    PRO-665

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    Description

    SNX1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids (146-522 a.a.) and having a molecular mass of 48 kDa. SNX1 is fused to 38 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNX1 0.25mg/ml solution contains 20mM Tris-HCl buffer pH-8, 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SNX1 belongs to the large family of hydrophilic proteins that interact with a range of receptor types that participate in intracellular trafficking. SNX1 and the associated splice variant, SNX1A, bind the EGFR, enable its transport to the lysosome, and thus contribute to the degradation of the receptor. SNX1 is related with cellular membranes, and they, also, associate with EGF, PDGF and the receptor tyrosine kinases.

    • Synonyms

      HsT17379, SNX1A, Vps5.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      SNX1 although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGGSMTV GITDPEKIGD GMNAYVAYKV TTQTSLPLFR SKQFAVKRRF SDFLGLYEKL
      SEKHSQNGFI VPPPPEKSLI GMTKVKVGKE DSSSAEFLEK RRAALERYLQ RIVNHPTMLQ DPDVREFLEK EELPRAVGTQ TLSGAGLLKM
      FNKATDAVSK MTIKMNESDI WFEEKLQEVE CEEQRLRKLH AVVETLVNHR KELALNTAQF AKSLAMLGSS EDNTALSRAL SQLAEVEEKI
      EQLHQEQANN DFFLLAELLS DYIRLLAIVR AAFDQRMKTW QRWQDAQATL QKKREAEARL LWANKPDKLQ QAKDEILEWE SRVTQYERDF
      ERISTVVRKE VIRFEKEKSK DFKNHVIKYL ETLLYSQQQL AKYWEAFLPE AKAIS.

    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.

    Snx1 Human
  • View Data Sheet

    Name :

    PODXL Human

    Description:

    Podocalyxin-Like Human Recombinant

    Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.

    Product # :

    PRO-2768

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    Description

    PODXL Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 416 amino acids (23-429 a.a.) and having a molecular mass of 43.1 kDa. PODXL is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.

    • Synonyms

      Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      DGS-SPSPSPS PSQNATQTTT DSSNKTAPTP ASSVTIMATD TAQQSTVPTS KANEILASVK ATTLGVSSDS PGTTTLAQQV SGPVNTTVAR GGGSGNPTTT IESPKSTKSA DTTTVATSTA TAKPNTTSSQ NGAEDTTNSG GKSSHSVTTD LTSTKAEHLT TPHPTSPLSP RQPTSTHPVA TPTSSGHDHL MKISSSSSTV AIPGYTFTSP GMTTTLPSSV ISQRTQQTSS QMPASSTAPS SQETVQPTSP ATALRTPTLP ETMSSSPTAA STTHRYPKTP SPTVAHESNW AKCEDLETQT QSEKQLVLNL TGNTLCAGGA SDEKLISLIC RAVKATFNPA QDKCGIRLAS VPGSQTVVVK EITIHTKLPA KDVYERLKDK WDELKEAGVS DMKLGDQGPP EEAEDRFSMP-HHHHHH.

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

    Podxl Human
  • View Data Sheet

    Name :

    SEPT6 Human

    Description:

    Septin-6 Human Recombinant

    Septin 6, Septin 2, SEP2, KIAA0128, SEPT2.

    Product # :

    PRO-949

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    Description

    SEPT6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 52.1 kDa.SEPT6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SEPT6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SEPT6 is a member of the septin family of GTPases and is functionally involved in cytokinesis and conservation of cellular morphology. SEPT6 interact with SEPT2. The genes encoding the mixed-lineage leukemia and SEPT2 breakpoint proteins are associated with one type of pediatric acute myeloid leukemia which is caused by reciprocal translocation between chromosomes 11 and X.

    • Synonyms

      Septin 6, Septin 2, SEP2, KIAA0128, SEPT2.

    • 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 MGSMAATDIA RQVGEGCRTV PLAGHVGFDS LPDQLVNKSV SQGFCFNILC VGETGLGKST LMDTLFNTKF EGEPATHTQP GVQLQSNTYD LQESNVRLKL TIVSTVGFGD QINKEDSYKP IVEFIDAQFE AYLQEELKIR RVLHTYHDSR IHVCLYFIAP TGHSLKSLDL VTMKKLDSKV NIIPIIAKAD AISKSELTKF KIKITSELVS NGVQIYQFPT DDESVAEING TMNAHLPFAV IGSTEELKIG NKMMRARQYP WGTVQVENEA HCDFVKLREM LIRVNMEDLR EQTHTRHYEL YRRCKLEEMG FKDTDPDSKP FSLQETYEAK RNEFLGELQK KEEEMRQMFV QRVKEKEAEL KEAEKELHEK FDRLKKLHQD EKKKLEDKKK SLDDEVNAFK QRKTAAELPQ SQGSQAGGSQ TLKRDKEKKN NPWLCTE

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    Sept6 Human
  • View Data Sheet

    Name :

    Noggin Human

    Description:

    Noggin Human Recombinant

    SYM1, SYNS1, NOG.

    Product # :

    CYT-475

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    Description

    Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect  is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.

    Citations

    More Info

    • Introduction

      The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
      EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
      RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
      TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC.

    • Background

      Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.

      Abstract:

      Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.

      Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.

      This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.

      Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      1. Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.

      Molecular Characteristics of Noggin :

      1. This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.

      Inhibition of BMP Signaling by Noggin:

      1. Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.

      Physiological Functions of Noggin:

      1. Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.

      Therapeutic Implications of Noggin:

      1. The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.

      Clinical Studies and Translational Research:

      1. This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.

    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.

    Noggin Human
  • View Data Sheet

    Name :

    STX1A Human

    Description:

    Syntaxin-1A Human Recombinant

    STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    Product # :

    PRO-574

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    Description

    Syntaxin-1A Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-226) and having a molecular mass of 26.1 kDa.Recombinant Human STX1A contains N-terminal domain (Habc) and t_SNARE domain (H3 domain).

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5, 10% glycerol, and 1mM DTT.

    Purity

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

    Citations

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    • Introduction

      Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain (Habc), a SNARE domain (known as H3), and a single C-terminal transmembrane domain. The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process. Syntaxins also serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces exocytosis.

    • Synonyms

      STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    • 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

      MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQ.

    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.

    Stx1A Human
  • View Data Sheet

    Name :

    KRT14 Human, His

    Description:

    Cytokeratin 14 Human Recombinant, His Tag

    Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

    Product # :

    PRO-941

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    Description

    KRT14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 492 amino acids (1-472 a.a.) and having a molecular mass of 53.8kDa.KRT14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT14 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.

    • Synonyms

      Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

    • 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 MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL SVSSSRFSSG GAYGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGTGLGGGF GGGFAGGDGL LVGSEKVTMQ NLNDRLASYL DKVRALEEAN ADLEVKIRDW YQRQRPAEIK
      DYSPYFKTIE DLRNKILTAT VDNANVLLQI DNARLAADDF RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE SLKEELAYLK KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN
      LEIELQSQLS MKASLENSLE ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI LLDVKTRLEQ EIATYRRLLE GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT KVMDVHDGKV VSTHEQVLRT KN.

    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.

    Krt14 Human His
  • View Data Sheet

    Name :

    Vaspin Human, His

    Description:

    Vaspin Human Recombinant, His Tag

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-459

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid Vaspin although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

    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.

    Vaspin Human
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