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Search results

1000 results found for “killer cell”

Name

Description

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  • View Data Sheet

    Name :

    IL1A Human

    Description:

    Interleukin-1 alpha Human Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    Product # :

    CYT-253

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    Description

    Interleukin-1 alpha Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids and having a molecular mass of 18022 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 25mM Tris-HCl, pH 8.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.

    More Info

    • Introduction

      IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.

    • Synonyms

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.

    • Background

      What is the molecular weight/Mw of IL1A HUMAN Protein?
      IL1A HUMAN Protein has a total Mw of 18kDa.

      What is the source or expression system of IL1A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL1A HUMAN Protein?
      IL1A HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A HUMAN Protein?
      The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.

      What is the amino acid sequence of IL1A HUMAN Protein?
      SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.

      What applications can IL1A HUMAN Protein be used in?
      IL1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1A HUMAN Protein?
      The endotoxin level is minimal, IL1A HUMAN Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.13 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 as a Reference Standard.

    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 1 Alpha Human
  • View Data Sheet

    Name :

    ATP5F1 Human

    Description:

    Synthase Transporting Mitochondrial Fo Complex B1 Human Recombinant

    ATP Synthase Proton-Transporting Mitochondrial F(0) Complex Subunit B1, ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit B Isoform 1, ATPase Subunit B, ATP Synthase B Chain Mitochondrial, Cell Proliferation-Inducing Protein 47, PIG47.

    Product # :

    PRO-1839

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    Description

    ATP5F1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (83-256) and having a molecular mass of 22.6 kDa. ATP5F1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ATP5F1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      ATP5F1 is a mitochondrial ATP synthase subunit catalyzes ATP synthesis, using an electrochemical gradient of protons all through the inner membrane for the duration of the oxidative phosphorylation. ATP synthase is comprised of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, including the proton channel. The catalytic segment of mitochondrial ATP synthase contains 9 subunits: 3 alpha, 3 beta, and one unit of gamma, delta, and epsilon. The proton route is known to have 9 subunits (a, b, c, d, e, f, g, F6 and 8).

    • Synonyms

      ATP Synthase Proton-Transporting Mitochondrial F(0) Complex Subunit B1, ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit B Isoform 1, ATPase Subunit B, ATP Synthase B Chain Mitochondrial, Cell Proliferation-Inducing Protein 47, PIG47.

    • 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 MGSLILYALS KEIYVISAET FTALSVLGVM VYGIKKYGPF VADFADKLNE QKLAQLEEAK QASIQHIQNA IDTEKSQQAL VQKRHYLFDV QRNNIAMALE VTYRERLYRV YKEVKNRLDY HISVQNMMRR KEQEHMINWV EKHVVQSIST QQEKETIAKC IADLKLLAKK AQAQPVM

    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.

    Atp5F1 Human
  • View Data Sheet

    Name :

    CCL14 Human, His

    Description:

    HCC-1 (CCL14) Human Recombinant, His Tag

    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-253

    Price :

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    • description
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    Description

    HCC-1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids (20-93 a.a.) and having a molecular mass of 10.9kDa. The HCC-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HCC-1 solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 containing 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    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 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 MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.

    • Background

      What is the molecular weight/Mw of CCL14 HUMAN, HIS Protein?
      CCL14 HUMAN, HIS Protein has a total Mw of 10.9kDa.

      What is the source or expression system of CCL14 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL14 HUMAN, HIS Protein?
      CCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL14 HUMAN, HIS Protein?
      The biological functionality of CCL14 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL14 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.

      What applications can CCL14 HUMAN, HIS Protein be used in?
      CCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

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


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

    Hcc 1 Human His
  • View Data Sheet

    Name :

    S100A8 Human, His-Myc

    Description:

    S100 Calcium Binding Protein A8, His-Myc Tag Human Recombinant

    S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.

    Product # :

    PRO-2329

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    Description

    S100A8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids (1-93) and having a molecular mass of 14.5kDa. S100A8 is fused to a 24 aa His-tag at N-terminus and to a 10 aa Myc-tag at C-terminus.

    Source

    Escherichia Coli.

    Formulation

    The S100A8 solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.

    • 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 MGSHMLTELE KALNSIIDVY HKYSLIKGNF HAVYRDDLKK LLETECPQYI RKKGADVWFK ELDINTDGAV NFQEFLILVI KMGVAAHKKS HEESHKEEQK LISEEDL.

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    S100A8 His Myc Human
  • View Data Sheet

    Name :

    AKR1C3 Human, His

    Description:

    Aldo-Keto Reductase Family 1 Member C3 Human Recombinant, His Tag

    DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.

    Product # :

    ENZ-406

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    Description

    AKR1C3 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39 kDa. The AKR1C3 is fused to a 20 amino acid His tag purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR1C3 solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately < 0.1 units/mg.
    Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.

    More Info

    • Introduction

      AKR1C3 is part of the aldo/keto reductase superfamily, which has at least 40 identified proteins. AKR1C3 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. AKR1C3 displays overlapping but distinct substrate specificity. AKR1C3 catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. AKR1C3 is involved in the pathogenesis of allergic diseases such as asthma. AKR1C3 controls cell growth and/or differentiation. AKR1C3 takes part in adrenal testosterone production. AKR1C3 expression is affected by metabolic disease, and its levels are considerably reduced in response to diet-induced weight loss and correlate with leptin levels.

    • Synonyms

      DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.

    • Physical Appearance

      Sterile Filtered clear 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 MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKPGLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY.

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    Akr1C3 Human
  • View Data Sheet

    Name :

    NKX3-1 Human

    Description:

    NK3 Homeobox 1 Human Recombinant

    Homeobox protein Nkx-3.1, Homeobox protein NK-3 homolog A, NKX3-1, NKX3.1, NKX3A, NKX3, BAPX2.

    Product # :

    PRO-1341

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    Description

    NKX3-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 257 amino acids (1-234 a.a) and having a molecular mass of 28.7kDa.NKX3-1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NKX3-1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NK3 Homeobox1 (NKX3-1) is a homeobox-containing transcription factor, which binds preferentially the consensus sequence 5'-TAAGT[AG]-3' and may act as a transcriptional repressor. The NKX3-1 transcription factor functions as a negative regulator of epithelial cell growth in prostate tissue. NKX3-1 has an imperative role in normal prostate development, regulating proliferation of glandular epithelium and in the formation of ducts in prostate. In addition, NKX3-1 functions as a tumor suppressor controlling prostate carcinogenesis, as shown by its ability to inhibit proliferation and invasion activities of PC-3 prostate cancer cells. Abnormal expression of NKX3-1 is linked with prostate tumor progression.

    • Synonyms

      Homeobox protein Nkx-3.1, Homeobox protein NK-3 homolog A, NKX3-1, NKX3.1, NKX3A, NKX3, BAPX2.

    • 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 MGSMLRVPEP RPGEAKAEGA APPTPSKPLT SFLIQDILRD GAQRQGGRTS SQRQRDPEPE PEPEPEGGRS RAGAQNDQLS TGPRAAPEEA ETLAETEPER HLGSYLLDSE NTSGALPRLP QTPKQPQKRS RAAFSHTQVI ELERKFSHQK YLSAPERAHL AKNLKLTETQ VKIWFQNRRY KTKRKQLSSE LGDLEKHSSL PALKEEAFSR ASLVSVYNSY PYYPYLYCVG SWSPAFW.

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    Nkx3 1 Human
  • View Data Sheet

    Name :

    SOD2 Mouse

    Description:

    Superoxide Dismutase-2 Mouse Recombinant

    Superoxide dismutase [Mn], Superoxide Dismutase-2, mitochondrial, Sod-2.

    Product # :

    PRO-2192

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    Description

    SOD2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (25-222 a.a) and having a molecular mass of 24.6kDa.SOD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOD2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems.

    • Synonyms

      Superoxide dismutase [Mn], Superoxide Dismutase-2, mitochondrial, Sod-2.

    • 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 MGSKHSLPDL PYDYGALEPH INAQIMQLHH SKHHAAYVNN LNATEEKYHE ALAKGDVTTQ VALQPALKFN GGGHINHTIF WTNLSPKGGG EPKGELLEAI KRDFGSFEKF KEKLTAVSVG VQGSGWGWLG FNKEQGRLQI AACSNQDPLQ GTTGLIPLLG IDVWEHAYYL QYKNVRPDYL KAIWNVINWE NVTERYTACK K.

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    Sod2 Mouse
  • View Data Sheet

    Name :

    NSL1 Human

    Description:

    NSL1 Human Recombinant

    NSL1 MIS12 Kinetochore Complex Component, NSL1 MIND Kinetochore Complex Component Homolog (S. Cerevisiae), Kinetochore-Associated ProteinNSL1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14.

    Product # :

    PRO-1557

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    Description

    NSL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-281) and having a molecular mass of 34.6kDa.NSL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NSL1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      NSL1 holds two coiled-coil domains.NSL1 proteins, localized to kinetochores - chromosome associated structures which attach to microtubules and mediate chromosome movements throughout cell division. NSL1 is a fragment of a conserved protein complex that hold two chromodomain-containing proteins and a component of the outer plate of the kinetochore. NSL1 connect centromeric heterochromatin with the outer kinetochore structure. Several transcript variants are known to encod different isoforms for this gene.

    • Synonyms

      NSL1 MIS12 Kinetochore Complex Component, NSL1 MIND Kinetochore Complex Component Homolog (S. Cerevisiae), Kinetochore-Associated ProteinNSL1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14.

    • 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 MGSMAGSPEL VVLDPPWDKE LAAGTESQAL VSATPREDFR VRCTSKRAVT EMLQLCGRFV QKLGDALPEE IREPALRDAQ WTFESAVQEN ISINGQAWQE ASDNCFMDSD IKVLEDQFDE IIVDIATKRK QYPRKILECV IKTIKAKQEI LKQYHPVVHP LDLKYDPDPA PHMENLKCRG ETVAKEISEA MKSLPALIEQ GEGFSQVLRM QPVIHLQRIH QEVFSSCHRK PDAKPENFIT QIETTPTETA SRKTSDMVLK RKQTKDCPQR KWYPLRPKKI NLDT

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    Nsl1 Human
  • View Data Sheet

    Name :

    BD 3 Mouse

    Description:

    Beta Defensin-3 Mouse Recombinant

    Beta-defensin 3, BD-3, mBD-3, Defensin beta 3, Defb3, Bd3, MGC129397.

    Product # :

    CYT-036

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    Description

    Beta Defensin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.6kDa. The BD-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse BD-3 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

    Purity

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

    Biological Activity

    Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

    More Info

    • Introduction

      Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.

    • Synonyms

      Beta-defensin 3, BD-3, mBD-3, Defensin beta 3, Defb3, Bd3, MGC129397.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K.

    • Background

      What is the molecular weight/Mw of BD3 Protein?
      BD3 Protein has a total Mw of 4.6kDa.

      What is the source or expression system of BD3 Protein?
      Escherichia Coli.

      What is the Purity of BD3 Protein?
      BD3 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD3 Protein?
      Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

      What is the amino acid sequence of BD3 Protein?
      KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K.

      What applications can BD3 Protein be used in?
      BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD3 Protein?
      The endotoxin level is minimal, BD3 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.

    Bd 3 Mouse
  • View Data Sheet

    Name :

    C12ORF5 Human

    Description:

    Chromosome 12 Open Reading Frame 5 Human

    Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    Product # :

    PRO-1791

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    Description

    TIGAR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids and having a molecular mass of 30.1kDa. The TIGAR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TIGAR was Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH8.5, 150mM NaCl.

    Purity

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

    More Info

    • Introduction

      TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.

    • Synonyms

      Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TIGAR stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TIGAR should be stored at 4C between 2-7 days and for future use below -18C. 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 TIGAR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MARFALTVVR HGETRFNKEK IIQGQGVDEP LSETGFKQAA AAGIFLNNVK FTHAFSSDLM RTKQTMHGIL ERSKFCKDMT VKYDSRLRER KYGVVEGKAL SELRAMAKAA REECPVFTPP GGETLDQVKM RGIDFFEFLC QLILKEADQK EQFSQGSPSN CLETSLAEIF PLGKNHSSKV NSDSGIPGLA ASVLVVSHGA YMRSLFDYFL TDLKCSLPAT LSRSELMSVT PNTGMSLFII NFEEGREVKP TVQCICMNLQ DHLNGLTETR

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    Tigar Human
  • View Data Sheet

    Name :

    CARD17 Human

    Description:

    Caspase Recruitment Domain Family, Member 17 Human Recombinant

    CARD17, Caspase Recruitment Domain Family, Member 17, Caspase recruitment domain-containing protein 17, INCA, Caspase-1 inhibitor INCA, Inhibitory caspase recruitment domain protein.

    Product # :

    PRO-1688

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    Description

    CARD17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.3 kDa.CARD17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CARD17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Caspase Recruitment Domain Family, Member 17 (CARD17) is a regulator of procaspase-1/CASP1 activation involved in the regulation of the proteolytic maturation of pro-IL-1beta/IL1B and its release throughout inflammation. CARD17 inhibits the release of IL1B in reaction to LPS in monocytes. Though, unlike CASP1, CARD17 do not induce NF-kappa-B activation.

    • Synonyms

      CARD17, Caspase Recruitment Domain Family, Member 17, Caspase recruitment domain-containing protein 17, INCA, Caspase-1 inhibitor INCA, Inhibitory caspase recruitment domain protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADKVLK EKRKQFIRSV GEGTINGLLG ELLETRVLSQ EEIEIVKCEN ATVMDKARAL LDSVIRKGAP ACQICITYIC EEDSHLAGTL GLSAGPTSGN HLTTQDSQIV LPS.

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    Card17 Human
  • View Data Sheet

    Name :

    PIN1 Human

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, EC 5.2.1.8, Rotamase Pin1, PPIase Pin1, DOD, UBL5, PIN1, PPIase.

    Product # :

    ENZ-331

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    Description

    PPIase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids & having a molecular mass of 18.2 kDa. The PIN1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PIN1 protein solution (1 mg/ml) containing 20mM Tris-HCl buffer (pH7.5) 0.1M NaCl, 5mM DTT & 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 330 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-HCl pH8.0 using chymotrypsin.

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    • Introduction

      Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, EC 5.2.1.8, Rotamase Pin1, PPIase Pin1, DOD, UBL5, PIN1, PPIase.

    • 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

      MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE.

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    Pin1 Human
  • View Data Sheet

    Name :

    KRT16 Human

    Description:

    Cytokeratin 16 Human Recombinant

    Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.

    Product # :

    PRO-1899

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    Description

    KRT16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-473) and having a molecular mass of 53.7 kDa.KRT16 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KRT16 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.

    More Info

    • Introduction

      Cytokeratin 16, also known as KRT16, is a member of the keratin gene family. KRT16 which acts as a regulator of innate immunity in response to skin barrier breach is required for some inflammatory checkpoint for the skin barrier maintenance. KRT16 is coexpressed with keratin 14 in a few epithelial tissues as esophagus, tongue, and hair follicles.

    • Synonyms

      Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.

    • 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 MGSMTTCSRQ FTSSSSMKGS CGIGGGIGGG SSRISSVLAG GSCRAPSTYG GGLSVSSRFS SGGACGLGGG YGGGFSSSSS FGSGFGGGYG GGLGAGFGGG LGAGFGGGFA GGDGLLVGSE KVTMQNLNDR LASYLDKVRA LEEANADLEV KIRDWYQRQR PSEIKDYSPY FKTIEDLRNK IIAATIENAQ PILQIDNARL AADDFRTKYE HELALRQTVE ADVNGLRRVL DELTLARTDL EMQIEGLKEE LAYLRKNHEE EMLALRGQTG GDVNVEMDAA PGVDLSRILN EMRDQYEQMA EKNRRDAETW FLSKTEELNK EVASNSELVQ SSRSEVTELR RVLQGLEIEL QSQLSMKASL ENSLEETKGR YCMQLSQIQG LIGSVEEQLA QLRCEMEQQS QEYQILLDVK TRLEQEIATY RRLLEGEDAH LSSQQASGQS YSSREVFTSS SSSSSRQTRP ILKEQSSSSF SQGQSS.

    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.

    Krt16 Human
  • View Data Sheet

    Name :

    TPT1 Mouse

    Description:

    Tumor Protein Translationally-Controlled 1 Mouse Recombinant

    Translationally-controlled tumor protein, TCTP, 21 kDa polypeptide, p21, p23.

    Product # :

    PRO-2196

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    Description

    TPT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-172 a.a) and having a molecular mass of 22.1kDa.TPT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPT1 protein solution (1mg/ml) containing Phosphate Buffered Saline, 10% glycerol And 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TPT1 takes part in calcium binding and microtubule stabilization. TPT1 is an immunoglobulin E dependent histamine-releasing factor produced by lymphocytes of atopic children and present in biologic fluids of allergic patients. TPT1 protein is similar to p23, a protein of Ehrlich ascites tumor cells, synthesized in the exponentially growing tumor. TPT1 is similar with IgE-dependent histamine releasing factor. TPT1 has a cell housekeeping function. TPT1 is involved in spermatogenesis and acts as a calcium binding protein of the human placenta that regulates calcium handling in trophoblast cells.

    • Synonyms

      Translationally-controlled tumor protein, TCTP, 21 kDa polypeptide, p21, p23.

    • 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 MGSHMMIIYR DLISHDELFS DIYKIREIAD GLCLEVEGKM VSRTEGAIDD SLIGGNASAE GPEGEGTEST VVTGVDIVMN HHLQETSFTK EAYKKYIKDY MKSLKGKLEE QKPERVKPFM TGAAEQIKHI LANFNNYQFF IGENMNPDGM VALLDYREDG VTPFMIFFKD GLEMEKC.

    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.

    Tpt1 Mouse
  • View Data Sheet

    Name :

    GlpK E. coli

    Description:

    Glycerol kinase E. Coli Recombinant

    Glycerol kinase, glycerol 3-phosphotransferase, Glycerokinase, GK.

    Product # :

    PKA-038

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    Description

    GlpK E. Coli Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 525 amino acids (1-502 a.a) and having a molecular mass of 58.6 kDa.GlpK is fused to a 23 amino acid His-tag at N-terminus& purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GlpK protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GlpK also known as glycerol kinase, is a member of the FGGY kinase family. GlpK catalyzes the transfer of a phosphate group from ATP to glycerol, thereby forming glycerol phosphate. Furthermore, this intermediate can then be converted to dihydroxyacetone phosphate (DHAP), which is utilized in either glycolysis or gluconeogenesis. The activity of GlpK is affected by numerous metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) triggers modifications in the quaternary structure of Glpk.

    • Synonyms

      Glycerol kinase, glycerol 3-phosphotransferase, Glycerokinase, GK.

    • 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 MGSMTEKKYI VALDQGTTSS RAVVMDHDAN IISVSQREFE QIYPKPGWVE HDPMEIWATQ SSTLVEVLAK ADISSDQIAA IGITNQRETT IVWEKETGKP IYNAIVWQCR RTAEICEHLK RDGLEDYIRS NTGLVIDPYF SGTKVKWILD HVEGSRERAR RGELLFGTVD TWLIWKMTQG RVHVTDYTNA SRTMLFNIHT LDWDDKMLEV LDIPREMLPE VRRSSEVYGQ TNIGGKGGTR IPISGIAGDQ QAALFGQLCV KEGMAKNTYG TGCFMLMNTG EKAVKSENGL LTTIACGPTG EVNYALEGAV FMAGASIQWL RDEMKLINDA YDSEYFATKV QNTNGVYVVP AFTGLGAPYW DPYARGAIFG LTRGVNANHI IRATLESIAY QTRDVLEAMQ ADSGIRLHAL RVDGGAVANN FLMQFQSDIL GTRVERPEVR EVTALGAAYL AGLAVGFWQN LDELQEKAVI EREFRPGIET TERNYRYAGW KKAVKRAMAW EEHDE.

    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.

    Glpk E Coli
  • View Data Sheet

    Name :

    CXCL1 Human

    Description:

    GRO-Alpha Human Recombinant (CXCL1)

    Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    Product # :

    CHM-329

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    Description

    GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM 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 peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.

    • Synonyms

      Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 CXCL1 in 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-Ser-Val-Ala-Thr.

    • Background

      What is the molecular weight/Mw of CXCL1 HUMAN Protein?
      CXCL1 HUMAN Protein has a total Mw of 7.81kDa.

      What is the source or expression system of CXCL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL1 HUMAN Protein?
      CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL1 HUMAN Protein?
      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 CXCL1 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.

      What applications can CXCL1 HUMAN Protein be used in?
      CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL1 HUMAN Protein?
      The endotoxin level is minimal, CXCL1 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.

    Gro A Human
  • View Data Sheet

    Name :

    CCL12 Mouse

    Description:

    Monocyte Chemotactic Protein-5 Mouse Recombinant (CCL12)

    C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.

    Product # :

    CHM-266

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    Description

    MCP-5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 82 amino acids and having a molecular mass of 9.3kDa. The MCP5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×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 human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.

    More Info

    • Introduction

      MCP-5 (CCL12) is a cloned mouse CC chemokine most closely related to human MCP1 (66% amino acid sequence identity in the mature protein). MCP5 is expressed constitutively in the thymus and the lymph nodes. Under inflammatory conditions, moreover CCL12 expression is induced in activated macrophages and mast cells. The mouse MCP1 gene is mapped to the CC chemokine cluster on chromosome 11. Recombinant CCL12 is a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also chemoattracts eosinophils. CCL12 is a functional ligand for CCR2.

    • Synonyms

      C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP5 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 MCP5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.

    • Background

      What is the molecular weight/Mw of CCL12 MOUSE Protein?
      CCL12 MOUSE Protein has a total Mw of 9.3kDa.

      What is the source or expression system of CCL12 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL12 MOUSE Protein?
      CCL12 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL12 MOUSE Protein?
      Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.

      What is the amino acid sequence of CCL12 MOUSE Protein?
      GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.

      What applications can CCL12 MOUSE Protein be used in?
      CCL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL12 MOUSE Protein?
      The endotoxin level is minimal, CCL12 MOUSE 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.

    Mcp 5 Mouse
  • View Data Sheet

    Name :

    RELM g Mouse, His

    Description:

    RELM-Gamma Mouse Recombinant, His Tag

    Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    Product # :

    CYT-455

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    Description

    RELM-gamma Mouse Recombinant is a His -Tagged Fusion Protein having a molecular weight of 11 kDa containing 86 amino acid residues of the RELM-gamma Mouse and 16 additional amino acid residues – HisTag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.

    • Synonyms

      Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    • 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.The lyophilized protein remains stable until the expiry date when stored at -20°C.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMTLES IVEKKVKELL ANRDDCPSTV TKTFSCTSIT ASGRLASCPS GMTVTGCACG YGCGSWDIRD GNTCHCQCST MDWATARCCQ LA.

    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.

    Relm Gamma Mouse
  • View Data Sheet

    Name :

    IL12B Antibody

    Description:

    Interleukin-12 subunit beta, Mouse Anti Human

    Interleukin-12 subunit beta, IL-12 subunit p40, Cytotoxic lymphocyte maturation factor 40 kDa subunit, NK cell stimulatory factor chain 2, IL-12B, CLMF p40, NKSF2, IL12B, CLMF, CLMF2, IL-12B.

    Product # :

    ANT-435

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      IL12B is a subunit of interleukin 12 which is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. Interleukin 12 is a disulfide-linked heterodimer composed of the 40kDa cytokine receptor like subunit encoded by the IL12B gene, and a 35kDa subunit encoded by IL12A. The IL12B cytokine is expressed by activated macrophages which serve as an important inducer of Th1 cells development. The IL12B cytokine has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Overexpression of the IL12B gene was observed in the central nervous system of patients with multiple sclerosis (MS), suggesting a role of the IL12B cytokine in the pathogenesis of the disease. The promoter polymorphism of the IL12B gene has been reported to be linked to the severity of atopic and non-atopic asthma in children.

    • Synonyms

      Interleukin-12 subunit beta, IL-12 subunit p40, Cytotoxic lymphocyte maturation factor 40 kDa subunit, NK cell stimulatory factor chain 2, IL-12B, CLMF p40, NKSF2, IL12B, CLMF, CLMF2, IL-12B.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human IL12B mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human IL12B amino acids 23-328 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT1D6AT.

    • Applications

      IL12B antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1000 ~ 2000. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      IL12B antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Il12B Antibody
  • View Data Sheet

    Name :

    BATF3 Human

    Description:

    Basic Leucine Zipper Transcription Factor ATF-Like 3 Human Recombinant

    JDP1, JUNDM1, SNFT, Basic leucine zipper transcriptional factor ATF-like 3, B-ATF-3, 21 kDa small nuclear factor isolated from T-cells, Jun dimerization protein p21SNFT, BATF3.

    Product # :

    PRO-1871

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    Description

    BATF3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-127 a.a) and having a molecular mass of 16.9kDa. BATF3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BATF3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Basic Leucine Zipper Transcription Factor ATF-Like 3 (BATF3) which is localizes to the nucleus, contains 1 bZIP domain. BATF3 functions as a negative regulator of AP-1-mediated transcription when interacting with c-Jun, particularly by heterodimerizing with c-Jun and binding to DNA response elements. BATF3 also takes part in repression of interleukin-2.

    • Synonyms

      JDP1, JUNDM1, SNFT, Basic leucine zipper transcriptional factor ATF-like 3, B-ATF-3, 21 kDa small nuclear factor isolated from T-cells, Jun dimerization protein p21SNFT, BATF3.

    • 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 MGSMSQGLPA AGSVLQRSVA APGNQPQPQP QQQSPEDDDR KVRRREKNRV AAQRSRKKQT QKADKLHEEY ESLEQENTML RREIGKLTEE LKHLTEALKE HEKMCPLLLC PMNFVPVPPR PDPVAGCLPR.

    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.

    Batf3 Human
  • View Data Sheet

    Name :

    EBI3 Mouse

    Description:

    Epstein Barr Virus Induced 3 Mouse Recombinant

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

    Product # :

    CYT-621

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    Description

    EBI3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 22.9kDa. The Murine EBI3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EBI3 was lyophilized from 10mM Sodium Citrate pH-3.

    Purity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized EBI3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

    • Background

      What is the molecular weight/Mw of EBI3 Protein?
      EBI3 Protein has a total Mw of 22.9kDa.

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

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

      What is the Biological Activity of EBI3 Protein?
      The biological functionality of EBI3 Protein will be determined in the future.

      What is the amino acid sequence of EBI3 Protein?
      MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

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

      What is the endotoxin level for EBI3 Protein?
      The endotoxin level is minimal, EBI3 Protein was purified using conventional chromatography techniques.

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

    Ebi3 Mouse
  • View Data Sheet

    Name :

    IL 19 Mouse

    Description:

    Interleukin-19 Mouse Recombinant

    Interleukin-19, IL-19, Il19.

    Product # :

    CYT-855

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Interleukin-19 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17.7kDa. The IL-19 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile filtered aqueous solution containing 5mM Na3PO4 and 150mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. It can bind the IL20 receptor complex and lead to the activation of the signal transducer and activator of transcription 3 (STAT3). A similar cytokine in mouse is reported to up-regulate the expression of IL6 and TNF-alpha and induce apoptosis, which suggests a role of this cytokine in inflammatory responses. Alternatively spliced transcript variants encoding the distinct isoforms have been described.

    • Synonyms

      Interleukin-19, IL-19, Il19.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-19 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL19 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 IL-19 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLRRCLISVDMRLIEKSFHEIKRAMQTKDTFKNVTILSLENLRSIKPGDVCCMTNNLL
      TFYRDRVFQDHQERSLEVLRRISSIANSFLCVQKSLERCQVHRQCNCSQEATNATRII
      HDNYNQLEVSSAALKSLGELNILLAWIDRNHLETPAA.

    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 19 Mouse
  • View Data Sheet

    Name :

    CRYAA Antibody

    Description:

    Crystallin Alpha A , Mouse Anti Human

    CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-4.

    Product # :

    ANT-305

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • formulation
    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of -crystallins are an autokinase activity and participation in the intracellular architecture. The expression of alpha-A is preferentially restricted to the lens cell.

    • Synonyms

      CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-4.

    • Immunogen

      Anti-human CRYAA mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CRYAA amino acids 1-173 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chains and κ light chain.

    • Clone

      Pc9F2AT.

    • Applications

      CRYAA antibody has been tested by ELISA and by Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should titrate the reagent to obtain optimal results. Recommended dilution range for Western blot analysis: 1:500 ~ 1:2000. Recommended starting dilution: 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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

    Cryaa Antibody
  • View Data Sheet

    Name :

    CSNK1A1 Antibody

    Description:

    Casein kinase I isoform alpha, Mouse Anti Human

    Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.

    Product # :

    ANT-442

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    More Info

    • formulation
    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    More Info

    • Introduction

      Caseine Kinase 1 alpha belongs is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily. The CK1 isoforms - alpha, beta, gamma, delta, epsilon and their splice variants are involved in diverse cellular processes including membrane trafficking, circadian rhythm, cell cycle progression, chromosome segregation, apoptosis and cellular differentiation. Possibly CSNK1A1 can phosphorylate a large number of proteins and is involved in Wnt signaling where it phosphorylates CTNNB1 on Ser45. CSNK1A1 also interacts with the Axin complex.

    • Synonyms

      Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.

    • Immunogen

      Anti-human CSNK1A1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CSNK1A1 amino acids 1-337 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT2E2AT.

    • Applications

      CSNK1A1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1000 ~ 2000. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      CSNK1A1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Csnk1A1 Antibody
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