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Search results

1000 results found for “Encephalitis”

Name

Description

Product #

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  • View Data Sheet

    Name :

    BHMT2 Human

    Description:

    Betaine-Homocysteine Methyltransferase 2 Human Recombinant

    BHMT2, Betaine--Homocysteine S-Methyltransferase 2, SMM-Hcy Methyltransferase, Betaine-Homocysteine Methyltransferase 2, S-Methylmethionine--Homocysteine S-Methyltransferase BHMT2, EC 2.1.1.10, EC 2.1.1.5.

    Product # :

    ENZ-798

    Price :

    Quantity :

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    Description

    BHMT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 386 amino acids (1-363 a.a.) and having a molecular mass of 42.7kDa. BHMT2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    BHMT2 protein 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

      Betaine-Homocysteine Methyltransferase 2 (BHMT2) is involved in the regulation of homocysteine metabolism. Homocysteine is a sulfur-containing amino acid which has a key role in methylation reactions. Transfer of the methyl group from betaine to homocysteine generates methionine, which donates the methyl group to methylate DNA, proteins, lipids, and other intracellular metabolites. BHMT2 is one of two methyl transferases which can catalyze the transfer of the methyl group from betaine to homocysteine. BHMT2 converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. Homocysteine metabolism anomalies are implicated in disorders varying from vascular disease to neural tube birth defects such as spina bifida.

    • Synonyms

      BHMT2, Betaine--Homocysteine S-Methyltransferase 2, SMM-Hcy Methyltransferase, Betaine-Homocysteine Methyltransferase 2, S-Methylmethionine--Homocysteine S-Methyltransferase BHMT2, EC 2.1.1.10, EC 2.1.1.5.

    • 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 MGSMAPAGRP GAKKGILERL ESGEVVIGDG SFLITLEKRG YVKAGLWTPE AVIEHPDAVR QLHMEFLRAG SNVMQTFTFS ASEDNMESKW EDVNAAACDL AREVAGKGDA LVAGGICQTS IYKYQKDEAR IKKLFRQQLE VFAWKNVDFL IAEYFEHVEE AVWAVEVLKE SDRPVAVTMC IGPEGDMHDI TPGECAVRLV KAGASIVGVN CRFGPDTSLK TMELMKEGLE WAGLKAHLMV QPLGFHAPDC GKEGFVDLPE YPFGLESRVA TRWDIQKYAR EAYNLGVRYI GGCCGFEPYH IRAIAEELAP ERGFLPPASE KHGSWGSGLD MHTKPWIRAR ARREYWENLL PASGRPFCPS LSKPDF.

    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.

    Bhmt2 Human
  • View Data Sheet

    Name :

    GADD45GIP1 Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant

    Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

    Product # :

    PRO-972

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    Description

    GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.

    • Synonyms

      Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

    • 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 MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS

    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.

    Gadd45Gip1 Human
  • View Data Sheet

    Name :

    GBA Human

    Description:

    Beta-Glucocerebrosidase Human Recombinant

    Glucosidase, Beta, Acid, D-Glucosyl-N-Acylsphingosine Glucohydrolase, Beta-Glucocerebrosidase, Acid Beta-Glucosidase, Glucosylceramidase, Alglucerase, EC 3.2.1.45, Beta-GC, GLUC, Glucosidase, Beta; Acid (Includes Glucosylceramidase), Glucosylceramidase-Like Protein, Lysosomal Glucocerebrosidase, GBA1, GCB, GC, Glucosylceramidase.

    Product # :

    ENZ-908

    Price :

    Quantity :

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    • description
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    • Citations

    Description

    GBA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 503 amino acids (40-536a.a.) and having a molecular mass of 56.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). GBA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GBA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Beta-Glucocerebrosidase, also known as GBA is amember of the glycosyl hydrolase 30 family. GBA is a lysosomal enzyme which requires a signal peptide for transport across the membrane of the rough endoplasmic reticulum as well as glycosylation for transport into lysosomes. Furthermore, Gaucher disease is caused by a deficiency in the activity of the enzyme glucocerebrosidase.

    • Synonyms

      Glucosidase, Beta, Acid, D-Glucosyl-N-Acylsphingosine Glucohydrolase, Beta-Glucocerebrosidase, Acid Beta-Glucosidase, Glucosylceramidase, Alglucerase, EC 3.2.1.45, Beta-GC, GLUC, Glucosidase, Beta; Acid (Includes Glucosylceramidase), Glucosylceramidase-Like Protein, Lysosomal Glucocerebrosidase, GBA1, GCB, GC, Glucosylceramidase.

    • 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

      ARPCIPKSFG YSSVVCVCNA TYCDSFDPPT FPALGTFSRY ESTRSGRRME LSMGPIQANH TGTGLLLTLQ PEQKFQKVKG FGGAMTDAAA LNILALSPPA QNLLLKSYFS EEGIGYNIIR VPMASCDFSI RTYTYADTPD DFQLHNFSLP EEDTKLKIPL IHRALQLAQR PVSLLASPWT SPTWLKTNGA VNGKGSLKGQ PGDIYHQTWA RYFVKFLDAY AEHKLQFWAV TAENEPSAGL LSGYPFQCLG FTPEHQRDFI ARDLGPTLAN STHHNVRLLM LDDQRLLLPH WAKVVLTDPE AAKYVHGIAV HWYLDFLAPA KATLGETHRL FPNTMLFASE ACVGSKFWEQ SVRLGSWDRG MQYSHSIITN LLYHVVGWTD WNLALNPEGG PNWVRNFVDS PIIVDITKDT FYKQPMFYHL GHFSKFIPEG SQRVGLVASQ KNDLDAVALM HPDGSAVVVV LNRSSKDVPL TIKDPAVGFL ETISPGYSIH TYLWRRQHHH HHH.

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

    Gba Human
  • View Data Sheet

    Name :

    CD5L Mouse

    Description:

    CD5 Molecule-Like Mouse Recombinant

    CD5 antigen-like, Apoptosis inhibitor expressed by macrophages, Apoptosis inhibitory 6 CT-2, SP-alpha, Cd5l' Aim, Api6.

    Product # :

    PRO-2243

    Price :

    Quantity :

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    • description
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    • More Info
    • Citations

    Description

    CD5L produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 339 amino acids (22-352a.a.) and having a molecular mass of 37.6 kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CD5L is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CD5L protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CD5 antigen-like (CD5L) participates in the regulation of the immune system. CD5L functions as an inhibitor of apoptosis. CD5L is expressed in the spleen, lymph node, thymus and bone marrow.

    • Synonyms

      CD5 antigen-like, Apoptosis inhibitor expressed by macrophages, Apoptosis inhibitory 6 CT-2, SP-alpha, Cd5l' Aim, Api6.

    • 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

      ESPTKVQLVG GAHRCEGRVE VEHNGQWGTV CDDGWDRRDV AVVCRELNCG AVIQTPRGAS YQPPASEQRV LIQGVDCNGT EDTLAQCELN YDVFDCSHEE DAGAQCENPD SDLLFIPEDV RLVDGPGHCQ GRVEVLHQSQ WSTVCKAGWN LQVSKVVCRQ LGCGRALLTY GSCNKSTQGK GPIWMGKMSC SGQEANLRSC LLSRLENNCT HGEDTWMECE DPFELKLVGG DTPCSGRLEV LHKGSWGSVC DDNWGEKEDQ VVCKQLGCGK SLHPSPKTRK IYGPGAGRIW LDDVNCSGKE QSLEFCRHRL WGYHDCTHKE DVEVICTDFD VLEHHHHHH.

    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.

    Cd5L Mouse
  • View Data Sheet

    Name :

    HAVCR1 Human, HEK

    Description:

    Hepatitis A Virus Cellular Receptor 1 Human Recombinant, HEK

    Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.

    Product # :

    HAV-223

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    Description

    HAVCR1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser21-Thr288) containing a total of 283 amino acids, having a calculated molecular mass of 30.5kDa. HAVCR1 is fused to a 2 aa N-terminal linker, a 2 aa C-terminal linker and a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    HAVCR1 was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% (w/v) Trehalose.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.

    • Synonyms

      Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. HAVCR1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      ASSVKVGGEA GPSVTLPCHY SGAVTSMCWN RGSCSLFTCQ NGIVWTNGTH VTYRKDTRYK LLGDLSRRDV SLTIENTAVS DSGVYCCRVE HRGWFNDMKI TVSLEIVPPK VTTTPIVTTV PTVTTVRTST TVPTTTTVPM TTVPTTTVPT TMSIPTTTTV LTTMTVSTTT SVPTTTSIPT TTSVPVTTTV STFVPPMPLP RQNHEPVATS PSSPQPAETH PTTLQGAIRR EPTSSPLYSY TTDGNDTVTE SSDGLWNNNQ TQLFLEHSLL TANTTKLHHH HHH.

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

    Havcr1 Human Hek
  • View Data Sheet

    Name :

    TNF alpha human

    Description:

    Tumor Necrosis Factor-Alpha Human Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-223

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    Description

    Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

    Purity

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

    Biological Activity

    The Specific Activity is >5.0×107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

    Citations

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, INS resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.

    • Background

      TNF Alpha Human: An Overview of Its Role and Importance in Immunology

      TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.

      This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.

      Production and Properties

      Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.

      Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.

      Solubility and Usage

      The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.

      This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.

      Storage and Stability

      For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.

      Biological Role and Implications

      TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.

      Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.

      Mechanism of Action

      TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.

      Research and Clinical Importance

      Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.

      Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.

      In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.



    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.

    Tnf Alpha Human
  • View Data Sheet

    Name :

    CCL14 Human (66 a.a.)

    Description:

    HCC-1 Human Recombinant (CCL14) (66 a.a.)

    Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    Product # :

    CHM-006

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    Description

    HCC-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 66 amino acids and having a molecular mass of 7.8kDa. The HCC-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL14 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

    Purity

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

    Biological Activity

    The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.

    Citations

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

    • Synonyms

      Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized HCC1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL14 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 HCC-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.

    • Background

      What is the molecular weight/Mw of CCL14 HUMAN (66 A.A.) Protein?
      CCL14 HUMAN (66 A.A.) Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CCL14 HUMAN (66 A.A.) Protein?
      Escherichia Coli.

      What is the Purity of CCL14 HUMAN (66 A.A.) Protein?
      CCL14 HUMAN (66 A.A.) Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL14 HUMAN (66 A.A.) Protein?
      The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.

      What is the amino acid sequence of CCL14 HUMAN (66 A.A.) Protein?
      GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.

      What applications can CCL14 HUMAN (66 A.A.) Protein be used in?
      CCL14 HUMAN (66 A.A.) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL14 HUMAN (66 A.A.) Protein?
      The endotoxin level is minimal, CCL14 HUMAN (66 A.A.) Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL14 HUMAN (66 A.A.) 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 CCL14 HUMAN (66 A.A.)?
      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.

    Hcc 1 Human 66 Aa
  • View Data Sheet

    Name :

    HCV Core 1-120

    Description:

    Hepatitis C Virus Nucleocapsid (core) 1-120 a.a. Recombinant

    Product # :

    HCV-006

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    Description

    Recombinant HCV Core 1-120 produced in E. coli is a single polypeptide chain containing 140 amino acids (aa 1-120) and having a molecular mass of 15.7kDa.Recombinant HCV Core 1-120 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNA virus in the family Flaviviridae.
      HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes (1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • 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 MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG RRQPIPKARR PEGRTWAQPG YPWPLYGNEG CGWAGWLLSP RGSRPSWGPT DPRRRSRNLG.

    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.

    Hcv Core 1 120
  • View Data Sheet

    Name :

    CCL23 Human

    Description:

    Macrophage Inflammatory Protein-3 Human Recombinant (CCL23)

    C-C motif chemokine 23, Small-inducible cytokine A23, Macrophage inflammatory protein 3, Myeloid progenitor inhibitory factor 1, CK-beta-8, MIP-3, MPIF-1, CKB-8, CCL23, MIP3, MPIF1, SCYA23, CKb8, Ckb-8-1.

    Product # :

    CHM-358

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    Description

    MIP-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 99 amino acids and having a molecular mass of 11.3kDa. The MIP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 150mM 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 cell population using a concentration range of 10-50ng/ml corresponding to a Specific Activity of 20,000-100,000IU/mg.

    Citations

    More Info

    • Introduction

      CCL23 (MIP-3) is a ligand for the CCR1chemokine receptor. CCL23 is one of several cytokine genes clustered on the q-arm of chromosome 17, in a locus containing several other CC chemokines. MIP-3 chemoattracts monocytes, resting T-lymphocytes and neutrophils, but not activated lymphocytes. Furthermore, it was shown that MIP-3 inhibits colony formation of bone marrow myeloid immature progenitors. MIP-3 is mainly expressed in lung and liver tissue, but can be also found in bone marrow and placenta, as well as in some cell lines of myeloid origin.
      Alternative splicing of the CCL23 gene produces 2 mRNAs which encode a short (CK?8) and a long (CK?81) isoform of the MIP-3. CK?8 cDNA encodes a 120 amino acid residue precursor protein with a putative 21 a.a. residue signal peptide which is cleaved to generate a 99 a.a. residue mature CK?8 (a.a. 22-120). Further N-terminal processing of the 99 a.a. residue variant can produce a 75 a.a. residue CK?8 (a.a. 46-120) which is considerably more active than the 99 a.a. residue variant.
      MIP-3 may be involved in the malignant progression of certain human cancer cells which overexpress ErbB2 through the transactivation of ErbB2 tyrosine kinase. MIP-3 may also be involved in angiogenesis via upregulation of matrix metalloproteinase MMP-2 expression.

    • Synonyms

      C-C motif chemokine 23, Small-inducible cytokine A23, Macrophage inflammatory protein 3, Myeloid progenitor inhibitory factor 1, CK-beta-8, MIP-3, MPIF-1, CKB-8, CCL23, MIP3, MPIF1, SCYA23, CKb8, Ckb-8-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL23 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 MIP-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RVTKDAETEF MMSKLPLENP VLLDRFHATS ADCCISYTPR SIPCSLLESYFETNSECSKP GVIFLTKKGR RFCANPSDKQ VQVCMRMLKL DTRIKTRKN.

    • Background

      What is the molecular weight/Mw of CCL23 HUMAN Protein?

      CCL23 HUMAN Protein has a total Mw of 11.3kDa.

       

      What is the source or expression system of CCL23 HUMAN
      Protein?

      Escherichia Coli.

       

      What is the Purity of CCL23 HUMAN Protein?

      CCL23 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

       

      What is the Biological Activity of CCL23 HUMAN Protein?

      Determined by its ability to chemoattract human T cell
      population using a concentration range of 10-50ng/ml corresponding to a
      Specific Activity of 20,000-100,000IU/mg.

       

      What is the amino acid sequence of CCL23 HUMAN Protein?

      RVTKDAETEF MMSKLPLENP VLLDRFHATS ADCCISYTPR
      SIPCSLLESYFETNSECSKP GVIFLTKKGR RFCANPSDKQ VQVCMRMLKL DTRIKTRKN.

       

      What applications can CCL23 HUMAN Protein be used in?

      CCL23 HUMAN Protein can probably be used in western blot,
      ELISA and Lateral Flow.

       

      What is the endotoxin level for CCL23 HUMAN Protein?

      The endotoxin level is minimal, CCL23 HUMAN Protein was
      purified using conventional chromatography techniques.

       

      Who supplies recombinant CCL23 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 CCL23 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.

    Mip 3 Human
  • View Data Sheet

    Name :

    CCL20 Human

    Description:

    Macrophage Inflammatory Protein-3 alpha Human Recombinant (CCL20)

    S Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20.

    Product # :

    CHM-351

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    Description

    MIP-3 Alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 8 kDa. The MIP-3a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4, 150mM 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 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

    Citations

    More Info

    • Introduction

      CCL-20 is a chemotactic factor that draws lymphocytes & neutrophils, rathar than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL-20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL-20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL-20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria.
      MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission.

    • Synonyms

      S Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL20 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 MIP-3 Alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ASNFDCCLGY TDRILHPKFI VGFTRQLANE GCDINAIIFH TKKKLSVCAN PKQTWVKYIV RLLSKKVKNM.

    • Background

      What is the molecular weight/Mw of CCL20 HUMAN Protein?
      CCL20 HUMAN Protein has a total Mw of 8kDa.

      What is the source or expression system of CCL20 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL20 HUMAN Protein?
      CCL20 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL20 HUMAN Protein?
      Determined by its ability to chemoattract human T lymphocytes using a concentration range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

      What is the amino acid sequence of CCL20 HUMAN Protein?
      ASNFDCCLGY TDRILHPKFI VGFTRQLANE GCDINAIIFH TKKKLSVCAN PKQTWVKYIV RLLSKKVKNM.

      What applications can CCL20 HUMAN Protein be used in?
      CCL20 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL20 HUMAN Protein?
      The endotoxin level is minimal, CCL20 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 3A Human
  • View Data Sheet

    Name :

    CCL15 68 a.a Human

    Description:

    Macrophage Inflammatory Protein-5 (68 a.a) 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-011

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    Description

    Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7.4kDa. The MIP5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIP5 was lyophilized from a 0.2µm filtered concentrated solution containing PBS, pH-7.4.

    Purity

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

    Biological Activity

    Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED50 for this effect is typically 2-4ng/ml.

    Citations

    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

      SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM KKLKPYSI.

    • Background

      What is the molecular weight/Mw of CCL15 68 A.A HUMAN Protein?
      CCL15 68 A.A HUMAN Protein has a total Mw of 7.4kDa.

      What is the source or expression system of CCL15 68 A.A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL15 68 A.A HUMAN Protein?
      CCL15 68 A.A HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL15 68 A.A HUMAN Protein?
      Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED50 for this effect is typically 2-4ng/ml.

      What is the amino acid sequence of CCL15 68 A.A HUMAN Protein?
      SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM KKLKPYSI.

      What applications can CCL15 68 A.A HUMAN Protein be used in?
      CCL15 68 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL15 68 A.A HUMAN Protein?
      The endotoxin level is minimal, CCL15 68 A.A 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 68 Aa Human
  • View Data Sheet

    Name :

    CCL15 Human

    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.

    Citations

    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

    Name :

    SELE Human, HEK

    Description:

    E-Selectin Human Recombinant, HEK

    E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    Product # :

    PRO-1645

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    Description

    SELE Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 543 amino acids (22-556). SELE is fused to an 8 amino acid His-tag at C-terminus is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    SELE was lyophilized from a 0.2 µM filtered solution of PBS and 4% Mannitol, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.

    • Synonyms

      E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SELE although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELE 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 SELE in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVW
      VWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTA
      ACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSY
      NSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPW
      NTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFT
      FKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFR
      YGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTY
      KSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKF
      ACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPVDHHHHHH.

    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.

    Sele Human Hek
  • View Data Sheet

    Name :

    CXCL7 Human

    Description:

    Neutrophil Activating Protein-2 Human Recombinant (CXCL7)

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-274

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    Description

    Neutrophil Activating Protein-2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The NAP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL7 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

    Greater than 97% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    sds-page

    CXCL7 Human SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7should 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 Neutrophil Activating Protein-2in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.

    • Background

      What is the molecular weight/Mw of CXCL7 HUMAN Protein?
      CXCL7 HUMAN Protein has a total Mw of 7.6kDa.

      What is the source or expression system of CXCL7 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 HUMAN Protein?
      CXCL7 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 HUMAN Protein?
      The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CXCL7 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.

      What applications can CXCL7 HUMAN Protein be used in?
      CXCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 HUMAN Protein?
      The endotoxin level is minimal, CXCL7 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.

    Nap2 Human
  • View Data Sheet

    Name :

    ASMT Human

    Description:

    Acetylserotonin O-Methyltransferase Human Recombinant

    HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    Product # :

    ENZ-664

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    Description

    ASMT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a) and having a molecular mass of 35.3kDa.ASMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.

    • Synonyms

      HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    • 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 MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK

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    Asmt Human
  • View Data Sheet

    Name :

    SNCA 1-60 Human

    Description:

    Alpha Synuclein 1-60 Human Recombinant

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

    Product # :

    PRO-165

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    Description

    A-Synuclein 1-60 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 1-60 and contains the N-terminal amphipathic domain, produced in E.Coli is a single, non-glycosylated polypeptide chain of 60 amino acids having a molecular mass of 6.1kDa. The Recombinant Human a-Synuclein 1-60 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA 1-60 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK.

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

    Snca 1 60 Human
  • View Data Sheet

    Name :

    SODA E.Coli

    Description:

    Superoxide Dismutase E.Coli Recombinant

    Superoxide dismutase [Mn], MnSOD, soda, b3908, JW3879.

    Product # :

    PRO-208

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    Description

    SODA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-206 a.a.) and having a molecular mass of 25.2kDa.SODA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SODA E.coli solution (1mg/ml) containining 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 350 units/mg, in which one unit will inhibit the rate of reduction of cytochrome c by 50% in a coupled system, using xanthine and xanthine oxidase at pH 7.8 at 25C in a 1.5 ml reaction volume.

    Citations

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    • Introduction

      Superoxide dismutase Mn (soda) belongs to the iron/manganese superoxide dismutase family. SodA destroys radicals that are typically produced within the cells and which are toxic to biological systems. SodA works by catalyzing the dismutation of the superoxide radical O2- to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase.

    • Synonyms

      Superoxide dismutase [Mn], MnSOD, soda, b3908, JW3879.

    • 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 MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA NLPVEELITK LDQLPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK AAIERDFGSV DNFKAEFEKA AASRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS
      GFPIMGLDVW EHAYYLKFQN RRPDYIKEFW NVVNWDEAAA RFAAKK.

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    Soda Ecoli
  • View Data Sheet

    Name :

    EIF4EBP2 Human

    Description:

    Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 Human Recombinant

    Eukaryotic Translation Initiation Factor 4E Binding Protein 2, 4E-BP2, eIF4E-binding protein 2, 4EBP2, PHASII, phosphorylated.

    Product # :

    PRO-176

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    Description

    EIF4EBP2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140amino acids (1-120a.a.) and having a molecular mass of 15.1 kDa. EIF4EBP2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF4EBP2 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EIF4EBP2 belongs to the eukaryotic translation initiation factor 4E binding protein family. Even though EIF4EBP2 protein binds eIF4E and inhibits translation initiation, growth factors can release this inhibition by a phosphorylation-dependent disruption. EIF4EBP2 mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. Regulation of this protein is associated to cell proliferation, cell differentiation and viral infection.

    • Synonyms

      Eukaryotic Translation Initiation Factor 4E Binding Protein 2, 4E-BP2, eIF4E-binding protein 2, 4EBP2, PHASII, phosphorylated.

    • 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 MSSSAGSGHQ PSQSRAIPTR TVAISDAAQL PHDYCTTPGG TLFSTTPGGT RIIYDRKFLL DRRNSPMAQT PPCHLPNIPG VTSPGTLIED SKVEVNNLNN LNNHDRKHAV GDDAQFEMDI.

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    Eif4Ebp2 Human
  • View Data Sheet

    Name :

    CXCL5 Human (8-78 a.a)

    Description:

    Epithelial Neutrophil-Activating Protein 78, 8-78 a.a. Human Recombinant (CXCL5)

    Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    Product # :

    CHM-265

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    Description

    Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids (8-78 a.a.) and having a molecular mass of 7.8kDa. The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, 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 was determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

    Citations

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II interferon IFN-?. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

    • Synonyms

      Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      LRELRCVCLQ TTQGVHPKMI SNLQVFAIGP QCSKVEVVAS LKNGKEICLD PEAPFLKKVI QKILDGGNKE N.

    • Background

      What is the molecular weight/Mw of CXCL5 HUMAN (8-78 A.A) Protein?
      CXCL5 HUMAN (8-78 A.A) Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CXCL5 HUMAN (8-78 A.A) Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 HUMAN (8-78 A.A) Protein?
      CXCL5 HUMAN (8-78 A.A) Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 HUMAN (8-78 A.A) Protein?
      The biological activity was determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CXCL5 HUMAN (8-78 A.A) Protein?
      LRELRCVCLQ TTQGVHPKMI SNLQVFAIGP QCSKVEVVAS LKNGKEICLD PEAPFLKKVI QKILDGGNKE N.

      What applications can CXCL5 HUMAN (8-78 A.A) Protein be used in?
      CXCL5 HUMAN (8-78 A.A) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 HUMAN (8-78 A.A) Protein?
      The endotoxin level is minimal, CXCL5 HUMAN (8-78 A.A) Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL5 HUMAN (8-78 A.A) 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 CXCL5 HUMAN (8-78 A.A)?
      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.

    Ena 78 Human 8 78 Aa
  • View Data Sheet

    Name :

    CCL26 Human

    Description:

    Eotaxin-3 Human Recombinant (CCL26)

    C-C motif chemokine 26, Small-inducible cytokine A26, Eotaxin-3, Macrophage inflammatory protein 4-alpha, MIP-4-alpha, Thymic stroma chemokine-1, TSC-1, CC chemokine IMAC, CCL26, SCYA26, IMAC, MIP-4a, MGC126714, MIP-4alpha.

    Product # :

    CHM-362

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • SDS-PAGE
    • Citations

    Description

    Eotaxin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 8.4kDa. The Eotaxin-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    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 BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect is typically 0.1-1.0 μg/ml.

    SDS-PAGE

    CCL26 Human-SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Eotaxin-3 (CCL26) is a small cytokine that belongs to the CC chemokine family also known as TARC (thymus and activation regulated chemokine). CCL26 is major eotaxin produced and released by alveolar epithelial cells which is involved in autoregulation of CCR3 receptors and other eotaxins. Eotaxin-3 is involved in immunoregulatory and inflammatory processes. Eotaxin-3 specifically binds and stimulates chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. CCL26 exhibits chemotactic activity for normal peripheral blood eosinophils and basophils. Eotaxin-3 may play a part in the eosinophil accumulation in atopic diseases. Eotaxin-3 is overexpressed in eosinophilic esophagitis, and the expression level correlates with disease severity. Eotaxin-3 is expressed constitutively in thymus, but only briefly in phytohemagglutinin-stimulated peripheral blood mononuclear cells. CCL26 is one of two Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 7.

    • Synonyms

      C-C motif chemokine 26, Small-inducible cytokine A26, Eotaxin-3, Macrophage inflammatory protein 4-alpha, MIP-4-alpha, Thymic stroma chemokine-1, TSC-1, CC chemokine IMAC, CCL26, SCYA26, IMAC, MIP-4a, MGC126714, MIP-4alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL26 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 Eotaxin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L.

    • Background

      What is the molecular weight/Mw of CCL26 HUMAN Protein?
      CCL26 HUMAN Protein has a total Mw of 8.4kDa.

      What is the source or expression system of CCL26 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL26 HUMAN Protein?
      CCL26 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL26 HUMAN Protein?
      Determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect is typically 0.1-1.0 μg/ml.

      What is the amino acid sequence of CCL26 HUMAN Protein?
      TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L.

      What applications can CCL26 HUMAN Protein be used in?
      CCL26 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL26 HUMAN Protein?
      The endotoxin level is minimal, CCL26 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL26 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 CCL26 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.

    Eotaxin 3 Human
  • View Data Sheet

    Name :

    CXCL8 Macaque

    Description:

    Interleukin-8 Rhesus Macaque Recombinant

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP

    Product # :

    CHM-004

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    IL 8 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa.The IL 8 Rhesus Macaque is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.

    Citations

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-8 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 IL-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP

    • Background

      What is the molecular weight/Mw of CXCL8 MACAQUE Protein?
      CXCL8 MACAQUE Protein has a total Mw of 9.1kDa.

      What is the source or expression system of CXCL8 MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 MACAQUE Protein?
      CXCL8 MACAQUE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 MACAQUE Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.

      What is the amino acid sequence of CXCL8 MACAQUE Protein?
      AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP

      What applications can CXCL8 MACAQUE Protein be used in?
      CXCL8 MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 MACAQUE Protein?
      The endotoxin level is minimal, CXCL8 MACAQUE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL8 MACAQUE 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 CXCL8 MACAQUE?
      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.

    Il 8 Rhesus Macaque
  • View Data Sheet

    Name :

    CX3CL1 Mouse

    Description:

    Fractalkine Mouse Recombinant (CX3CL1)

    Fractalkine, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1, Cx3cl1, Cx3c, Fkn, Scyd1, CX3C, ABCD-3, AB030188, AI848747, D8Bwg0439e.

    Product # :

    CHM-017

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    • description
    • source
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    • purity
    • biological activity
    • More Info
    • Citations

    Description

    Fractalkine Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa. The CX3CL1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 µg/ml, corresponding to a specific activity of > 2000IU/mg.

    Citations

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1, Cx3cl1, Cx3c, Fkn, Scyd1, CX3C, ABCD-3, AB030188, AI848747, D8Bwg0439e.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CX3CL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CX3CL1 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 CX3CL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG.

    • Background

      What is the molecular weight/Mw of CX3CL1 MOUSE Protein?
      CX3CL1 MOUSE Protein has a total Mw of 8.7kDa.

      What is the source or expression system of CX3CL1 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CX3CL1 MOUSE Protein?
      CX3CL1 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 MOUSE Protein?
      The ED50as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 µg/ml, corresponding to a specific activity of > 2000IU/mg.

      What is the amino acid sequence of CX3CL1 MOUSE Protein?
      QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG.

      What applications can CX3CL1 MOUSE Protein be used in?
      CX3CL1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 MOUSE Protein?
      The endotoxin level is minimal, CX3CL1 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CX3CL1 MOUSE 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 CX3CL1 MOUSE?
      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.

    Fractalkine Mouse
  • View Data Sheet

    Name :

    LACTB E.coli, His

    Description:

    Beta Lactamase E.coli Recombinant, His Tag

    Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.

    Product # :

    ENZ-088

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    Description

    Beta Lactamase is an E.coli Recombinant protein produced in E.Coli containing 379 amino acids (20-377) and having a molecular mass of 41.8kDa. Beta Lactamase is expressed with a 21 N-terminal His tag.The LACTB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LACTB enzyme (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.

    • Synonyms

      Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.

    • 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 MAPQQINDIV HRTITPLIEQ QKIPGMAVAV IYQGKPYYFT WGYADIAKKQ PVTQQTLFEL GSVSKTFTGV LGGDAIARGE IKLSDPTTKY WPELTAKQWN GITLLHLATY TAGGLPLQVP DEVKSSSDLL RFYQNWQPAW APGTQRLYAN SSIGLFGALA VKPSGLSFEQ AMQTRVFQPL KLNHTWINVP PAEEKNYAWG YREGKAVHVS PGALDAEAYG VKSTIEDMAR WVQSNLKPLD INEKTLQQGI QLAQSRYWQT GDMYQGLGWE MLDWPVNPDS IINGSDNKIA LAARPVKAIT PPTPAVRASW VHKTGATGGF GSYVAFIPEK ELGIVMLANK NYPNPARVDA AWQILNALQ.

    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.

    Lactb Ecoli His
  • View Data Sheet

    Name :

    CIAPIN1 Human

    Description:

    Cytokine Induced Apoptosis Inhibitor 1 Human Recombinant

    DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

    Product # :

    PRO-024

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    • description
    • source
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    Description

    CIAPIN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312 a.a.) and having a molecular mass of 36kDa.CIAPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CIAPIN1 protein solution (1mg/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

      Anamorsin, ( CIAPIN) is a member of anamorsin family. CIAPIN mainly expressed in the cytoplasm of liver, pancreas and heart tissue cells and does not show any homology to known apoptosis regulatory molecules of the Bcl-2 or CASP families, or to signal transduction molecules. CIAPIN1 Expression is reliant on growth factor stimulation. It is a ubiquitously expressed protein, and when it is overexpressed, it grants apoptotic resistance.

    • Synonyms

      DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

    • 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 MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA.

    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.

    Ciapin1 Human
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