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Search results

1000 results found for “CDNF”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CUEDC2 Human

    Description:

    CUE Domain Containing 2 Human Recombinant

    CUE domain-containing protein 2, CUEDC2, C10orf66, HOYS6, bA18I14.5.

    Product # :

    PRO-1680

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    Description

    CUEDC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-287) and having a molecular mass of 34 kDa.CUEDC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CUEDC2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUE Domain Containing 2 also known as CUEDC2 is a part of the CUEDC2 family and contains 1 CUE domain. CUEDC2 down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway and controls PGR protein levels through a parallel mechanism.

    • Synonyms

      CUE domain-containing protein 2, CUEDC2, C10orf66, HOYS6, bA18I14.5.

    • 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 MGSMELERIV SAALLAFVQT HLPEADLSGL DEVIFSYVLG VLEDLGPSGP SEENFDMEAF TEMMEAYVPG FAHIPRGTIG DMMQKLSGQL SDARNKENLQ PQSSGVQGQV PISPEPLQRP EMLKEETRSS AAAAADTQDE ATGAEEELLP GVDVLLEVFP TCSVEQAQWV LAKARGDLEE AVQMLVEGKE EGPAAWEGPN QDLPRRLRGP QKDELKSFIL QKYMMVDSAE DQKIHRPMAP KEAPKKLIRY IDNQVVSTKG ERFKDVRNPE AEEMKATYIN LKPARKYRFH.

    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.

    Cuedc2 Human
  • View Data Sheet

    Name :

    SHFM1 Human

    Description:

    Split Hand/Foot Malformation Type 1 Human Recombinant

    SHFM1, Split Hand/Foot Malformation (Ectrodactyly) Type 1, DSS1, SHFD1, Deleted In Split Hand/Split Foot Protein 1, Split Hand/Foot Deleted Protein 1, Split Hand/Foot Malformation Type 1 Protein, Deleted In Split-Hand/Foot 1, 26S Proteasome Complex Subunit DSS1, ECD, SEM1, SHSF1, Shfdg1, Deleted In Split-Hand/Split-Foot 1, SHFDG1.

    Product # :

    PRO-1777

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    Description

    SHFM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-70 a.a) and having a molecular mass of 10.7kDa (Molecular size on SDS-PAGE will appear higher).SHFM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SHFM1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      26S proteasome complex subunit DSS1 (SHFM1) has been suggested as a candidate gene for the autosomal dominant form of the heterogeneous limb developmental disorder split hand/split foot malformation type 1. SHFM1 is a subunit of the 26S proteasome which plays a part in ubiquitin-dependent proteolysis. SHFM1 binds and stabilizes BRCA2 and is therefore involved in the control of R-loop-associated DNA damage and thus transcription-associated genomic instability. Furthermore, SHFM1 may have a role in the completion of the cell cycle. SHFM1 is a component of the TREX-2 complex (transcription and export complex 2), comprised of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3.

    • Synonyms

      SHFM1, Split Hand/Foot Malformation (Ectrodactyly) Type 1, DSS1, SHFD1, Deleted In Split Hand/Split Foot Protein 1, Split Hand/Foot Deleted Protein 1, Split Hand/Foot Malformation Type 1 Protein, Deleted In Split-Hand/Foot 1, 26S Proteasome Complex Subunit DSS1, ECD, SEM1, SHSF1, Shfdg1, Deleted In Split-Hand/Split-Foot 1, SHFDG1.

    • 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 MGSMSEKKQP VDLGLLEEDD EFEEFPAEDW AGLDEDEDAH VWEDNWDDDN VEDDFSNQLR AELEKHGYKM ETS.

    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.

    Shfm1 Human
  • View Data Sheet

    Name :

    EIF3J Human

    Description:

    Eukaryotic Translation Initiation Factor 3J Human Recombinant

    Eukaryotic translation initiation factor 3 subunit J, Eukaryotic translation initiation factor 3 subunit 1, eIF-3-alpha, eIF3 p35, EIF3J, EIF3S1, eIF3-alpha.

    Product # :

    PRO-970

    Price :

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    Description

    EIF3J Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (70-258) and having a molecular mass of 24kDa (Molecular weight on SDS-PAGE will appear higher).EIF3J is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF3J solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic translation initiation factor 3 subunit J (EIF3J) is a member of the EIF-3 subunit J family. EIF3 has a crucial role in binding of initiator methionyl-tRNA and mRNA to the 40S ribosomal subunit to produce the 40S initiation complex. EIF3J binds to the aminoacyl (A) site and mRNA access channel of the 40S subunit, setting EIF3J directly in the ribosomal decoding center. In addition, EIF3J interacts with eIF1A and reduces 40S subunit affinity for mRNA. An elevated affinity for mRNA is restored upon enlistment of initiator tRNA, despite the fact EIF3J remains in the mRNA-binding cleft in the presence of tRNA.

    • Synonyms

      Eukaryotic translation initiation factor 3 subunit J, Eukaryotic translation initiation factor 3 subunit 1, eIF-3-alpha, eIF3 p35, EIF3J, EIF3S1, eIF3-alpha.

    • 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 MKISEKKKIA EKIKEKERQQ KKRQEEIKKR LEEPEEPKVL TPEEQLADKL RLKKLQEESD LELAKETFGV NNAVYGIDAM NPSSRDDFTE FGKLLKDKIT QYEKSLYYAS FLEVLVRDVC ISLEIDDLKK ITNSLTVLCS EKQKQEKQSK AKKKKKGVVP GGGLKATMKD DLADYGGYDG GYVQDYEDFM.

    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.

    Eif3J Human
  • View Data Sheet

    Name :

    NUDCD2 Human

    Description:

    NudC Domain Containing 2 Human Recombinant

    NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 2.

    Product # :

    PRO-1881

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    Description

    NUDCD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-157 a.a) and having a molecular mass of 20kDa.NUDCD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUDCD2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NudC Domain Containing 2 also known as NUDCD2 contains 1 CS domain and interacts with LIS1. NUDCD2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone.

    • Synonyms

      NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAPFEE RSGVVPCGTP WGQWYQTLEE VFIEVQVPPG TRAQDIQCGL QSRHVALSVG GREILKGKLF DSTIADEGTW TLEDRKMVRI VLTKTKRDAA NCWTSLLESE YAADPWVQDQ MQRKLTLERF QKENPGFDFS GAEISGNYTK GGPDFSNLEK

    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.

    Nudcd2 Human
  • View Data Sheet

    Name :

    LZTFL1 Human

    Description:

    Leucine Zipper Transcription Factor-Like 1 Human Recombinant

    Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.

    Product # :

    PRO-2157

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    Description

    LZTFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 37.0kDa. LZTFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LZTFL1 protein solution (1mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine Zipper Transcription Factor-Like 1, also known as LZTFL1 is a ubiquitously expressed protein which localizes to the cytoplasm. LZTFL1 interacts with Bardet-Biedl Syndrome proteins (BBS) and during its interaction with BBS protein complexes, regulates protein trafficking to the ciliary membrane. Nonsense mutations in LZTFL1 cause a form of Bardet-Biedl Syndrome; a ciliopathy characterized partly by polydactyly, obesity, cognitive impairment, hypogonadism, and kidney failure. LZTFL1 also acts as a tumor suppressor; possibly by interacting with E-cadherin as well as the actin cytoskeleton and in this manner regulating the transition of epithelial cells to mesenchymal cells.

    • Synonyms

      Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAELGLN EHHQNEVINY MRFARSKRGL RLKTVDSCFQ DLKESRLVED TFTIDEVSEV LNGLQAVVHS EVESELINTA YTNVLLLRQL FAQAEKWYLK LQTDISELEN RELLEQVAEF EKAEITSSNK KPILDVTKPK LAPLNEGGTA ELLNKEILRL QEENEKLKSR LKTIEIQATN ALDEKSKLEK ALQDLQLDQG NQKDFIKAQD LSNLENTVAA LKSEFQKTLN DKTENQKSLE ENLATAKHDL LRVQEQLHMA EKELEKKFQQ TAAYRNMKEI LTKKNDQIKD LRKRLAQYEP ED.

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    Lztfl1 Human
  • View Data Sheet

    Name :

    VEGF Rat, Yeast

    Description:

    Vascular Endothelial Growth Factor Rat Recombinant, Yeast

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-1126

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    Description

    Vascular Endothelial Growth Factor Rat Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x165 amino acid polypeptide chains, having a molecular mass of approximately 25.7kDa each.VEGF is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50  was measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells and was found to be 0.75‑3.75 ng/ml.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both angiogenesis and vasculogenesis.VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of VEGF is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in VEGF have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

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    Rat Vegf Protein
  • View Data Sheet

    Name :

    CD99L2 Mouse

    Description:

    CD99 Molecule Like 2 Mouse Recombinant

    CD99 antigen-like protein 2, MIC2-like protein 1, Cd99l2, Mic2l1, CD99 antigen-like protein 2 isoform 1, Xap89, Mic2l1.

    Product # :

    PRO-2780

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    Description

    CD99L2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 378 amino acids (26-161a.a) and having a molecular mass of 41.8kDa. CD99L2 is fused to a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The CD99L2 solution (1mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CD99 antigen-like protein 2, MIC2-like protein 1, Cd99l2, Mic2l1, CD99 antigen-like protein 2 isoform 1, Xap89, Mic2l1.

    • 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

      DGSDTDGFNL EDALKETSSV KQRWDHFSTT TRRPVTTRAP ANPAERWDHV ATTTTRRPGT TRAPSNPMEL DGFDLEDALD DRNDLDGPKK PSAGEAGGWS DKDLEDIVEG GGYKPDKNKG GGGYGSNDDP GSGISTETGLEPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

    • Background

      The CD99L2 human recombinant, a variant of the CD99L2 protein, has gained substantial attention in biomedical research due to its intriguing molecular characteristics and potential implications in various biological processes. CD99L2, a member of the CD99 family of proteins, plays diverse roles in cellular adhesion, migration, and signal transduction. The CD99L2 human recombinant, generated through recombinant DNA technology, offers a valuable tool for investigating the intricate functions and therapeutic potential of this protein.

      Understanding the molecular characteristics of CD99L2 is pivotal in unraveling its functional significance. CD99L2 belongs to the immunoglobulin superfamily and is primarily expressed on the cell surface. It exhibits unique structural features, including extracellular immunoglobulin-like domains and intracellular signaling motifs. These characteristics contribute to the complexity of CD99L2 and its ability to interact with various cellular components and modulate signaling pathways.

      CD99L2 plays diverse roles in different physiological contexts. It is involved in cellular adhesion processes, regulating cell-cell interactions and migration in various tissues. Additionally, CD99L2 has been implicated in immune responses, particularly in the modulation of T-cell activation and leukocyte migration. The precise mechanisms underlying these functions are still being elucidated, highlighting the need for further investigation.

      The CD99L2 human recombinant offers exciting prospects for research and therapeutic applications. By utilizing this recombinant protein, scientists can investigate the role of CD99L2 in disease pathogenesis, explore its interactions with other molecules, and potentially develop targeted therapies. CD99L2 has been implicated in cancer progression, immune disorders, and neurodevelopmental conditions, making it a promising candidate for novel therapeutic interventions.

      This research aims to provide a comprehensive analysis of the CD99L2 human recombinant, focusing on its molecular characteristics, biological roles, and potential therapeutic implications. By shedding light on the intricate nature of CD99L2, we aim to contribute to a deeper understanding of its functional significance and pave the way for future research and therapeutic advancements.

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    Cd99L2 Mouse
  • View Data Sheet

    Name :

    GADD45G Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Gamma Human Recombinant

    DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.

    Product # :

    PRO-570

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    Description

    GADD45G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids and having a molecular mass of 17.1 kDa.

    Source

    Escherichia Coli.

    Formulation

    The GADD45G protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GADD45G is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45G reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45G acts as a new-age tumor suppressor however is being frequently inactivated epigenetically in multiple tumors. GADD45G mRNA expression is down-regulated in hepatocellular carcinoma. GADD45G causes cell cycle arrest at G2/M transition when transfected into Hep-G2 cells. GADD45 Gamma induction by androgens involves new protein synthesis. Overexpression of GADD45 Gamma inhibits cell growth and causes morphological modifications in prostate cell lines thus GADD45 gamma takes part in differentiation induction by androgens.

    • Synonyms

      DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.

    • 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

      MTLEEVRGQD TVPESTARMQ GAGKALHELL LSAQRQGCLT AGVYESAKVL NVDPDNVTFC VLAAGEEDEG DIALQIHFTL IQAFCCENDIDIVRVGDVQR LAAIVGAGEE AGAPGDLHCI LISNPNEDAW KDPALEKLSL FCEESRSVND WVPSITLPE.

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    Gadd45G Human
  • View Data Sheet

    Name :

    CHRAC1 Human

    Description:

    Chromatin Accessibility Complex 1 Human Recombinant

    CHARC1, CHARC15, CHRAC-1, CHRAC-15, CHRAC15, YCL1, Chromatin accessibility complex protein 1, Chromatin accessibility complex 15 kDa protein, DNA polymerase epsilon subunit p15.

    Product # :

    PRO-1391

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    Description

    CHRAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-131 a.a.) and having a molecular mass of 17.1kDa. CHRAC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CHRAC1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chromatin Accessibility Complex 1 (CHRAC1) is a histone-fold protein which interacts with further histone-fold proteins to bind DNA in a sequence-independent mode. These histone-fold protein dimers combine within larger enzymatic complexes for DNA replication, transcription, and packaging.

    • Synonyms

      CHARC1, CHARC15, CHRAC-1, CHRAC-15, CHRAC15, YCL1, Chromatin accessibility complex protein 1, Chromatin accessibility complex 15 kDa protein, DNA polymerase epsilon subunit p15.

    • 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 MGSMADVVVG KDKGGEQRLI SLPLSRIRVI MKSSPEVSSI NQEALVLTAK ATELFVQCLA TYSYRHGSGK EKKVLTYSDL ANTAQQSETF QFLADILPKK ILASKYLKML KEEKREEDEE NDNDNESDHD EADS.

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    Chrac1 Human
  • View Data Sheet

    Name :

    TXNDC12 Human

    Description:

    Thioredoxin Domain Containing 12 Human Recombinant

    Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.

    Product # :

    PRO-1133

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    Description

    TXNDC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (27-172) and having a molecular mass of 20.8 kDa.TXNDC12 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TXNDC12 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TXNDC12 is a member of the thioredoxin super family. This Family members have a thioredoxin fold with a consensus active-site sequence (CxxC) and take part in redox regulation, protection against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.

    • Synonyms

      Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMHN GLGKGFGDHI HWRTLEDGKK EAAASGLPLM VIIHKSWCGA CKALKPKFAE STEISELSHN FVMVNLEDEE EPKDEDFSPD GGYIPRILFL DPSGKVHPEI INENGNPSYK YFYVSAEQVV QGMKEAQERL TGDAFRKKHL EDEL

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    Txndc12 Human
  • View Data Sheet

    Name :

    CXCL5 Human

    Description:

    Epithelial Neutrophil-Activating Protein 78 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-331

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    Description

    Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8020 Dalton. The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL5 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg)  of recombinant human ENA-78.

    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 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

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

    • Background

      What is the molecular weight/Mw of CXCL5 HUMAN Protein?
      CXCL5 HUMAN Protein has a total Mw of 8.02kDa.

      What is the source or expression system of CXCL5 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 HUMAN Protein?
      CXCL5 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 HUMAN Protein?
      The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.

      What is the amino acid sequence of CXCL5 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.

      What applications can CXCL5 HUMAN Protein be used in?
      CXCL5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 HUMAN Protein?
      The endotoxin level is minimal, CXCL5 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.

    Ena 78 Human
  • View Data Sheet

    Name :

    CXCL14 Human

    Description:

    BRAK (CXCL14) Human Recombinant

    C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687. 

    Product # :

    CHM-001

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    Description

    CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL14 was lyophilized after extensive dialysis against 20mM Tris-HCl, pH 8.5 and 1M NaCl.

    Purity

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

    Biological Activity

    The ED50 of CXCL14 as determined by its ability to induce calcium flux of prostaglandin E2 treated THP1 human acute monocytic leukemia cells was 1.0-10.0 ng/ml.

    More Info

    • Introduction

      CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.

    • Synonyms

      C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 in sterile 18M-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 Ser-Lys-Cys-Lys-Cys.

    • Background

      What is the molecular weight/Mw of CXCL14 HUMAN Protein?
      CXCL14 HUMAN Protein has a total Mw of 9.4kDa.

      What is the source or expression system of CXCL14 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL14 HUMAN Protein?
      CXCL14 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL14 HUMAN Protein?
      The ED50 of CXCL14 as determined by its ability to induce calcium flux of prostaglandin E2 treated THP1 human acute monocytic leukemia cells was 1.0-10.0 ng/ml.
      What is the amino acid sequence of CXCL14 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Cys-Lys-Cys.

      What applications can CXCL14 HUMAN Protein be used in?
      CXCL14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL14 HUMAN Protein?
      The endotoxin level is minimal, CXCL14 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.

    Cxcl14 Human
  • View Data Sheet

    Name :

    FGF14 Human

    Description:

    Fibroblast Growth Factor 14 Human Recombinant

    Fibroblast growth factor 14, FGF-14, Fibroblast growth factor homologous factor 4, FHF-4, FGF14, FHF4, SCA27, bA397O8.2.

    Product # :

    CYT-756

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    • sds-page

    Description

    FGF14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-247 a.a) and having a molecular mass of 30kDa.FGF14 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    FGF14 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    FGF14-sds-page - Product image 1

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    • Introduction

      Fibroblast Growth Factor 14 (FGF14) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in a various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF14 gene mutation is linked with autosomal dominant cerebral ataxia.

    • Synonyms

      Fibroblast growth factor 14, FGF-14, Fibroblast growth factor homologous factor 4, FHF-4, FGF14, FHF4, SCA27, bA397O8.2.

    • 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 MGSHMAAAIA SGLIRQKRQA REQHWDRPSA SRRRSSPSKN RGLCNGNLVD IFSKVRIFGL KKRRLRRQDP QLKGIVTRLY CRQGYYLQMH PDGALDGTKD DSTNSTLFNL IPVGLRVVAI QGVKTGLYIA MNGEGYLYPS ELFTPECKFK ESVFENYYVI YSSMLYRQQE SGRAWFLGLN KEGQAMKGNR VKKTKPAAHF LPKPLEVAMY REPSLHDVGE TVPKPGVTPS KSTSASAIMN GGKPVNKSKT T.

    • Background

      What is the molecular weight/Mw of FGF14 Protein?
      FGF14 Protein has a total Mw of 30kDa.

      What is the source or expression system of FGF14 Protein?
      Escherichia Coli.

      What is the Purity of FGF14 Protein?
      FGF14 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF14 Protein?
      The biological functionality of FGF14 Protein will be determined in the future.

      What is the amino acid sequence of FGF14 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMAAAIA SGLIRQKRQA REQHWDRPSA SRRRSSPSKN RGLCNGNLVD IFSKVRIFGL KKRRLRRQDP QLKGIVTRLY CRQGYYLQMH PDGALDGTKD DSTNSTLFNL IPVGLRVVAI QGVKTGLYIA MNGEGYLYPS ELFTPECKFK ESVFENYYVI YSSMLYRQQE SGRAWFLGLN KEGQAMKGNR VKKTKPAAHF LPKPLEVAMY REPSLHDVGE TVPKPGVTPS KSTSASAIMN GGKPVNKSKT T.

      What applications can FGF14 Protein be used in?
      FGF14 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF14 Protein?
      The endotoxin level is minimal, FGF14 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.

    Fgf14 Human
  • View Data Sheet

    Name :

    FGF17 Human

    Description:

    Fibroblast Growth Factor 17 Human Recombinant

    Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    Product # :

    CYT-817

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    Description

    FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa.

    Source

    Escherichia Coli.

    Formulation

    FGF17 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

    More Info

    • Introduction

      Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.

    • Synonyms

      Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF17 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 FGF17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

    • Background

      What is the molecular weight/Mw of FGF17 Protein?
      FGF17 Protein has a total Mw of 22.6kDa.

      What is the source or expression system of FGF17 Protein?
      Escherichia Coli.

      What is the Purity of FGF17 Protein?
      FGF17 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF17 Protein?
      Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

      What is the amino acid sequence of FGF17 Protein?
      MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

      What applications can FGF17 Protein be used in?
      FGF17 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF17 Protein?
      The endotoxin level is minimal, FGF17 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.

    Fgf 17 Human
  • View Data Sheet

    Name :

    CXCL1 Mouse

    Description:

    GRO1/KC Mouse Recombinant (CXCL1)

    Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    Product # :

    CHM-335

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    Description

    KC Mouse Recombinant also known as N51 and GRO-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of approximately 7.8 kDa. The GRO-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer pH-7.4 and 0.1M NaCl.

    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 measuring the ability to chemoattrat human neutrophilsat a concentration of 10ng/ml-100ng/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, neutrophils and 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 alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KC Mouse 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 GRO1 Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APIANELRCQ CLQTMAGIHL KNIQSLKVLP SGPHCTQTEV IATLKNGREA CLDPEAPLVQ KIVQKMLKGV PK.

    • Background

      What is the molecular weight/Mw of CXCL1 MOUSE Protein?
      CXCL1 MOUSE Protein has a total Mw of 7.8kDa.

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

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

      What is the Biological Activity of CXCL1 MOUSE Protein?
      The biological activity was determined by measuring the ability to chemoattrat human neutrophilsat a concentration of 10ng/ml-100ng/ml.

      What is the amino acid sequence of CXCL1 MOUSE Protein?
      APIANELRCQ CLQTMAGIHL KNIQSLKVLP SGPHCTQTEV IATLKNGREA CLDPEAPLVQ KIVQKMLKGV PK.

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

      What is the endotoxin level for CXCL1 MOUSE Protein?
      The endotoxin level is minimal, CXCL1 MOUSE 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 0.03 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 KC 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.

    Gro A Mouse
  • View Data Sheet

    Name :

    NDRG3 Human

    Description:

    N-Myc Downstream Regulated 3 Human Recombinant

    Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.

    Product # :

    PRO-2100

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    Description

    NDRG3 Human Recombinant produced in E. coli is a single polypeptide chain containing 386 amino acids (1-363) and having a molecular mass of 42.4 kDa.NDRG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NDRG3 solution (0.25mg/1ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-Myc Downstream Regulated 3, also known as NDRG3, is a protein coding gene which is a part of the NDRG family and is expressed greatly in brain. NDRG2 is an important paralog of NDRG3.

    • Synonyms

      Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDELQDV QLTEIKPLLN DKEHDIETTH GVVHVTIRGL PKGNRPVILT YHDIGLNHKS CFNAFFNFED MQEITQHFAV CHVDAPGQQE GAPSFPTGYQ YPTMDELAEM LPPVLTHLSL KSIIGIGVGA GAYILSRFAL NHPELVEGLV LINVDPCAKG WIDWAASKLS GLTTNVVDII LAHHFGQEEL QANLDLIQTY RMHIAQDINQ DNLQLFLNSY NGRRDLEIER PILGQNDNKS KTLKCSTLLV VGDNSPAVEA VVECNSRLNP INTTLLKMAD CGGLPQVVQP GKLTEAFKYF LQGMGYIPSA SMTRLARSRT HSTSSSLGSG ESPFSRSVTS NQSDGTQESC ESPDVLDRHQ TMEVSC.

    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.

    Ndrg3 Human
  • View Data Sheet

    Name :

    ARL15 Human

    Description:

    ADP-Ribosylation Factor-Like 15 Human Recombinant

    ADP-ribosylation factor-like 15, ADP-ribosylation factor related protein 2, ARFRP2, ARF-related protein 2, FLJ20051.

    Product # :

    PRO-956

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    Description

    ARL15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (1-204) and having a molecular mass of 25.0 kDa.ARL15 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ARL15 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARL15 is a member of the ARF family which are essential in eukaryotic vesicular trafficking pathways and have a vital part in the activation of phospholipase D. ARL15 variants influence levels of Acrp30, an adipocyte-derived protein that is extremely genetic and inversely related to the prospect of type 2 diabetes mellitus and coronary heart disease.

    • Synonyms

      ADP-ribosylation factor-like 15, ADP-ribosylation factor related protein 2, ARFRP2, ARF-related protein 2, FLJ20051.

    • 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 MSDLRITEAF LYMDYLCFRA LCCKGPPPAR PEYDLVCIGL TGSGKTSLLS KLCSESPDNV VSTTGFSIKA VPFQNAILNV KELGGADNIR KYWSRYYQGS QGVIFVLDSA SSEDDLEAAR NELHSALQHP QLCTLPFLIL ANHQDKPAAR SVQEIKKYFE LEPLARGKRW ILQPCSLDDM DALKDSFSQL INLLEEKDHE AVRM

    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.

    Arl15 Human
  • View Data Sheet

    Name :

    CAMK2N1 Human

    Description:

    Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 Human Recombinant

    PRO1489; RP11-401M16.1, Calcium/calmodulin-dependent protein kinase II inhibitor 1, CaMKII inhibitory protein alpha, CaMKIIN-alpha, CAMK2N1.

    Product # :

    PRO-1873

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    Description

    CAMK2N1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 10.9kDa. CAMK2N1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CAMK2N1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).

    • Synonyms

      PRO1489; RP11-401M16.1, Calcium/calmodulin-dependent protein kinase II inhibitor 1, CaMKII inhibitory protein alpha, CaMKIIN-alpha, CAMK2N1.

    • 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 MGSMSEVLPY GDEKLSPYGD GGDVGQIFSC RLQDTNNFFG AGQNKRPPKL GQIGRSKRVV IEDDRIDDVL KNMTDKAPPG V.

    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.

    Camk2N1 Human
  • View Data Sheet

    Name :

    SNRPF Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide F Human Recombinant

    Sm-F, Sm protein F, snRNP-F, SMF, PBSCF, Small Nuclear Ribonucleoprotein Polypeptide F.

    Product # :

    PRO-041

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    Description

    SNRPF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (1-86a.a.) and having a molecular mass of 11.8kDa.SNRPF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNRPF protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 1mM EDTA , and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNRPF is a member of the snRNP Sm proteins family. There are at least seven isoforms, E, F, G, D1, D2, D3 and B/B. This type of common proteins have a crucial part in the biogenesis of the snRNPs. Moreover, they represent the major targets for the so-called anti-Sm auto-antibodies that are diagnostic for systemic lupus erythematosus (SLE). SNRPF assist in the cytoplasmic construction of the UsnRNPs by binding to aconserved Sm site on UsnRNA and forming a stable snRNP core complex.

    • Synonyms

      Sm-F, Sm protein F, snRNP-F, SMF, PBSCF, Small Nuclear Ribonucleoprotein Polypeptide F.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSLPLNPKPF LNGLTGKPVM VKLKWGMEYK GYLVSVDGYM NMQLANTEEY IDGALSGHLG EVLIRCNNVL YIRGVEEEEE DGEMRE

    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.

    Snrpf Human
  • View Data Sheet

    Name :

    LTF Human S.Plasma

    Description:

    Lactoferrin Human (Seminal Plasma)

    Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    Product # :

    PRO-1591

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    Description

    The Human Lactoferrin produced from pooled Human seminal plasma has a molecular mass of 76.165kDa (calculated without glycosylation) containing 691 amino acid residues.

    Source

    Human seminal plasma.

    Formulation

    LTF protein filtered (0.4µm) and lyophilized in 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Purity greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

    • Synonyms

      Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    • 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      GRRRSVQWCA VSQPEATKCF QWQRNMRKVR GPPVSCIKRD SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPRT HYYAVAVVKK GGSFQLNELQ GLKSCHTGLR RTAGWNVPIG TLRPFLNWTG PPEPIEAAVA RFFSASCVPG ADKGQFPNLC RLCAGTGENK CAFSSQEPYF SYSGAFKCLR DGAGDVAFIR ESTVFEDLSD EAERDEYELL CPDNTRKPVD KFKDCHLARV PSHAVVARSV NGKEDAIWNL LRQAQEKFGK DKSPKFQLFG SPSGQKDLLF KDSAIGFSRV PPRIDSGLYL GSGYFTAIQN LRKSEEEVAA RRARVVWCAV GEQELRKCNQ WSGLSEGSVT CSSASTTEDC IALVLKGEAD AMSLDGGYVY TAGKCGLVPV LAENYKSQQS SDPDPNCVDR PVEGYLAVAV VRRSDTSLTW NSVKGKKSCH TAVDRTAGWN IPMGLLFNQT GSCKFDEYFS QSCAPGSDPR SNLCALCIGD EQGENKCVPN SNERYYGYTG AFRCLAENAG DVAFVKDVTV LQNTDGNNNE AWAKDLKLAD FALLCLDGKR KPVTEARSCH LAMAPNHAVV SRMDKVERLK QVLLHQQAKF GRNGSDCPDK FCLFQSETKN LLFNDNTECL ARLHGKTTYE KYLGPQYVAG ITNLKKCSTS PLLEACEFLR K.

    • Human Virus Test

      Samples from each donor have been tested and found negative for HBsAg, HIV-1+2, HCV, syphilis, aHBc, RRR.

    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.

    Ltf Human Seminal Plasma
  • View Data Sheet

    Name :

    CLEC1B Human

    Description:

    C-type Lectin Domain Family 1, Member B Human Recombinant

    C-Type Lectin Domain Family 1, Member B, CLEC2, C-Type Lectin-Like Receptor 2, CLEC2B, CLEC-2, C-Type Lectin Domain Family 1 Member B, C-Type Lectin-Like Receptor-2, 1810061I13Rik, PRO1384, QDED721, C-type lectin domain family 1 member B, C-type lectin-like receptor 2.

    Product # :

    PRO-2185

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    Description

    CLEC1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (55-229 a.a) and having a molecular mass of 23.1kDa. CLEC1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLEC1B protein solution (1mg/ml) containing 20mM Tris, PH 8.0 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C-type Lectin Domain Family 1 Member B, also known as CLEC1B. NK-Natural killer cells express multiple calcium-dependent (C-type) lectin-like receptors, for instance CD94 (KLRD1; MIM 602894) and NKG2D (KLRC4; MIM 602893), which interact with major histocompatibility complex class I molecules and either inhibit or else activate cytotoxicity and cytokine secretion. CLEC1B is a C-type lectin-like receptor which is expressed in myeloid cells as well as in NK cells.

    • Synonyms

      C-Type Lectin Domain Family 1, Member B, CLEC2, C-Type Lectin-Like Receptor 2, CLEC2B, CLEC-2, C-Type Lectin Domain Family 1 Member B, C-Type Lectin-Like Receptor-2, 1810061I13Rik, PRO1384, QDED721, C-type lectin domain family 1 member B, C-type lectin-like receptor 2.

    • 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 MGSSVMQRNY LQGENENRTG TLQQLAKRFC QYVVKQSELK GTFKGHKCSP CDTNWRYYGD SCYGFFRHNL TWEESKQYCT DMNATLLKID NRNIVEYIKA RTHLIRWVGL SRQKSNEVWK WEDGSVISEN MFEFLEDGKG NMNCAYFHNG KMHPTFCENK HYLMCERKAG MTKVDQLP.

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    Clec1B Human
  • View Data Sheet

    Name :

    CD1D Human

    Description:

    CD1D Human Recombinant

    Antigen-presenting glycoprotein CD1d, R3G1, CD antigen: CD1d, Differentiation Antigen CD1-Alpha-3, T-Cell Surface Glycoprotein CD1d, Thymocyte Antigen CD1D, CD1A, R3, CD1d Molecule, CD1D Antigen, D Polypeptide, CD1d Antigen, R3G1, HMC Class I, Antigen-Like Glycoprotein CD1D, Antigen-Presenting Glycoprotein CD1d.

    Product # :

    PRO-2491

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    Description

    CD1D produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 290 amino acids (20-301 a.a.) and having a molecular mass of 32.9kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CD1Dis expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CD1D protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD1D, also known as antigen-presenting glycoprotein CD1d, is a transmembrane glycoprotein which belongs to the CD1 family of glycolipid antigen-presenting MHC-like molecules. CD1d-presented lipid antigens activate a special class of T cells, familiar as natural killer T (NKT) cells, during the interaction with the T-cell receptor present on NKT membranes. Once activated, NKT cells rapidly produce Th1 &Th2 cytokines, usually represented by interleukin 4 production.

    • Synonyms

      Antigen-presenting glycoprotein CD1d, R3G1, CD antigen: CD1d, Differentiation Antigen CD1-Alpha-3, T-Cell Surface Glycoprotein CD1d, Thymocyte Antigen CD1D, CD1A, R3, CD1d Molecule, CD1D Antigen, D Polypeptide, CD1d Antigen, R3G1, HMC Class I, Antigen-Like Glycoprotein CD1D, Antigen-Presenting Glycoprotein CD1d.

    • 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

      EVPQRLFPLR CLQISSFANS SWTRTDGLAW LGELQTHSWS NDSDTVRSLK PWSQGTFSDQ QWETLQHIFR VYRSSFTRDV KEFAKMLRLS YPLELQVSAG CEVHPGNASN NFFHVAFQGK DILSFQGTSW EPTQEAPLWV NLAIQVLNQD KWTRETVQWL LNGTCPQFVS GLLESGKSEL
      KKQVKPKAWL SRGPSPGPGR LLLVCHVSGF YPKPVWVKWM RGEQEQQGTQ PGDILPNADE TWYLRATLDV VAGEAAGLSC RVKHSSLEGQ DIVLYWGGSY TSLEHHHHHH.

    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.

    Cd1D Human
  • View Data Sheet

    Name :

    CRP Human

    Description:

    C-Reactive Protein Human

    C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

    Product # :

    PRO-557

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    Shipped with Ice Packs

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    • description
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    Description

    Human CRP produced in Human plasma having a molecular mass of 114 kDa. It can be used as a marker for inflammation and also used for monitoring and prediction of future events in coronary artery disease.

    Source

    Human Plasma.

    Formulation

    The protein solution is in 20mM TRIS buffer pH 8.0 containing 0.28M NaCl, 0.09% NaN3 and 5mM CaCl2.

    Purity

    Greater than 96.0%.

    More Info

    • Introduction

      CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically ( up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.

    • Synonyms

      C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Human CRP should be stored at 2-8°C. Do not freeze!

    • Human Virus Test

      Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG and HIV/HBV/HCV (PCR).

    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.

    CRP Human
  • View Data Sheet

    Name :

    FGF 2 Human

    Description:

    Fibroblast Growth Factor-Basic Human Recombinant

    Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.

    Product # :

    CYT-218

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    Shipped at Room temp

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    Description

    Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.2kDa.The FGF-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris-HCl, pH7.4 and 1M NaCl.

    Purity

    Greater than 98.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.

    More Info

    • Introduction

      Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The HPR -binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.

    • Background

      FGF 2 HUMAN: Insights into Fibroblast Growth Factor-2

      Basic Fibroblast Growth Factor or FGF 2 HUMAN is a protein with crucial roles in cell growth, tissue repair, and embryonic development. This is part of the larger fibroblast growth factor family and is vital for various biological processes, including the modulation of cell survival activities.

      Production and Properties

      Produced in E. coli, FGF 2 is a non-glycosylated polypeptide chain possessing 154 amino acids with a molecular weight of about 17.2 kDa. It is purified through advanced chromatographic techniques, ensuring high purity and activity for laboratory use.

      Physical Characteristics and Preparation

      The physical form of FGF 2 HUMAN is a sterile, white lyophilized powder. For experimental use, it is reconstituted with sterile water to at least 100µg/ml. This reconstitution is crucial for maintaining the integrity and effectiveness of the protein in various research applications.

      Storage and Handling

      To maintain stability, lyophilized FGF 2 should be stored at -18°C and used within three weeks if kept at room temperature. Once reconstituted, it should be kept at 4°C and used within 2-7 days or stored at -18°C for longer-term storage.

      Proper handling and avoiding repeated freeze-thaw cycles are essential to preserve the protein's functionality.

      Purity and Biological Activity

      FGF 2 is characterized by a purity greater than 98%, verified by SDS-PAGE analysis. Its biological activity is primarily defined by its efficacy in promoting the proliferation of specific cell lines, with an effective dose (ED50) typically below 0.1 ng/ml.

      Research Applications and Impact

      In the research context, FGF 2 is used extensively to study its effects on cell migration, proliferation, and angiogenesis. Moreover, its role in disease models, particularly in cancer and tissue repair studies, makes it a valuable resource for developing new therapeutic approaches.

      Usage Guidelines

      FGF 2 HUMAN is strictly for laboratory research use and is not suitable for drug development, food production, or cosmetic applications. Researchers are advised to comply with safety and handling guidelines to ensure that experiments are conducted under optimal conditions.

      The Broad Impact on Development and Disease

      FGF-2 is known for its multifunctional role across numerous biological processes such as tissue repair, embryonic development, angiogenesis, and even tumorigenesis.

      This growth factor, existing in various synonymous forms such as Basic FGF, FGF-b, and HBGF-2, is essential in cellular processes that underpin both health and disease.

      Furthermore, FGF-2's ability to bind to cellular receptors triggers a cascade of signaling pathways, including PI3K/Akt, MAPK/ERK, and PLCγ, which in turn influence cell growth, migration, and survival.

      These pathways are pivotal in mediating the factor's diverse effects on cell behavior, contributing to its critical roles in wound healing, angiogenesis, and tissue remodeling.

      What is the molecular weight/Mw of FGF 2 Protein?
      FGF 2 Protein has a total Mw of 17.2kDa.

      What is the source or expression system of FGF 2 Protein?
      Escherichia Coli.

      What is the Purity of FGF 2 Protein?
      FGF 2 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 2 Protein?
      The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.

      What is the amino acid sequence of FGF 2 Protein?
      AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.

      What applications can FGF 2 Protein be used in?
      FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF 2 Protein?
      The endotoxin level is minimal, FGF 2 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.

    Fgf 2 Human
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