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Search results

1000 results found for “GRO (CXCL1,2,3)”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    Cys-Protein-L

    Description:

    Cys-Protein L Recombinant

    Product # :

    PRO-1933

    Price :

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    Description

    Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized without any additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.

    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.

    Cys Protein L
  • View Data Sheet

    Name :

    IGF1 E3R Human

    Description:

    Insulin Like Growth Factor-1, Mutant E3R Human Recombinant

    Insulin-Like Growth Factor-1.

    Product # :

    CYT-1217

    Price :

    Quantity :

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    Description

    IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa. IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The filtered (0.4µm) concentrated protein solution was lyophilized from 0.5mg/ml solution in 50 mM NaCl, 20 mM Tris and 5% (w/v) trehalose, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Insulin-Like Growth Factor-1.

    • Physical Appearance

      Sterile 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.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. IGF1 E3R is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.

    • Background

      Insulin-like Growth Factor 1 (IGF-1) is a critical peptide hormone that plays a central role in regulating growth and development. Genetic mutations in the IGF-1 gene can result in altered IGF-1 variants, leading to various physiological consequences. Understanding these IGF-1 mutants is of paramount importance as they offer insights into growth disorders, metabolic regulation, and potential therapeutic avenues. This research delves into the world of IGF-1 mutants, shedding light on their diverse functions and implications for human health.

      The primary objective of this research is to elucidate the impact of IGF-1 mutations on growth regulation. In vitro and in vivo experiments will be conducted to investigate how these mutants interact with IGF-1 receptors, influence downstream signaling pathways, and modulate growth plate dynamics. Understanding these mechanisms is crucial for unraveling the complexities of growth disorders associated with IGF-1 mutations.

      The second objective is to assess the clinical relevance of IGF-1 mutants in growth-related conditions. Clinical studies involving individuals with growth hormone deficiencies or growth disorders linked to IGF-1 mutations will be conducted to evaluate the effects of these mutants on stature and overall health. These investigations may provide valuable insights into potential therapeutic strategies for individuals affected by growth-related disorders.

      The third objective is to explore the broader implications of IGF-1 mutants in metabolic regulation and age-related conditions. Research will investigate their roles in metabolic homeostasis, longevity, and susceptibility to age-related diseases. Understanding the multifaceted properties of IGF-1 mutants may open new avenues for therapeutic interventions in various health and aging-related conditions.

      By delving into the diverse functions of IGF-1 mutants, this research aims to expand our understanding of their physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for growth disorders, metabolic conditions, and age-related diseases.

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

    Igf1 Mutant
  • View Data Sheet

    Name :

    vMIP-II

    Description:

    MIP-2 Viral Recombinant

    MIP-2 Viral, Viral MIP-2, MIP2 Viral, Viral MIP2, Viral Macrophage inflammatory Protein-2.

    Product # :

    CHM-376

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
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    • More Info

    Description

    MIP-2 Viral Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.9 kDa. The MIP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 1mg/ml solution containing 20mM Phospahte Buffer, pH 7.4 % 0.15M NaCl.

    Purity

    Greater than 97.0% as determined by RP-HPLC & SDS-PAGE.

    Biological Activity

    Determined by the inhibitory effect on monocyte migration response to human MIP1A using a concentration range of 1µg-10µg/ml of viral MIP2 which will inhibit 25ng/ml of human MIP1A.

    More Info

    • Introduction

      Viral MIP-2 is closely related to MIP-1α, show amino acid sequence similarity of about 41%. At the amino acid sequence level, Viral MIP-1 and Viral MIP-2 share 48% similarity. Viral MIP-1 and Viral MIP-2 are more closely linked to one another phylogenetically than to other human chemokines, signifying that they have gene duplication within the virus rather than by two independent gene aquisitions. Viral MIP-2 binds to the CCR3 chemokine receptor through which eotaxin and other β chemokines activate eosinophils. Viral MIP-2 activates and chemoattract human eosinphils.

    • Synonyms

      MIP-2 Viral, Viral MIP-2, MIP2 Viral, Viral MIP2, Viral Macrophage inflammatory Protein-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-2 Viral protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 CXCL2 Viral in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      LGASWHRPDK CCLGYQKRPL PQVLLSSWYP TSQLCSKPGV IFLTKRGRQV
      CADKSKDWVK KLMQQLPVTA.

    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.

    Cxcl2 Viral
  • View Data Sheet

    Name :

    LR3 IGF1 Human

    Description:

    LR3 Insulin Like Growth Factor-1 Human Recombinant

    R3 IGF1, R3 IGF-1, R3IGF1, R3IGF-1, LONG IGF1, LONG IGF-1, LONG R3 IGF1, LONG R3IGF1, LONG R3 IGF-1, LONG R3IGF-1.

    Product # :

    CYT-022

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • sds-page

    Description

    The LR3 is a long-term analog of human IGF-1, specifically designed and manufactured for mammalian cell culture to support large-scale manufacturing of recombinant biopharmaceuticals. Recombinant Human LR3 Insulin Like Growth Factor-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9.1kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.2.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the stimulation of protein synthesis in L6 myoblasts is less than 10ng/ml, corresponding to a specific activity of 100,000units/mg.

    sds-page

    LR3 IGF1 sds-page - Product image 1

    More Info

    • Introduction

      IGF-1 (Insulin-like growth factor-1) is a major hormonal mediator of statural growth. Under regular circumstances, GH (growth hormone) binds to its receptor in the liver, and other tissues, and stimulates the synthesis/secretion of IGF-1. In target tissues, the Type 1 IGF receptor, that is homologous to the insulin receptor, is activated by IGF-1, leading to intracellular signaling which stimulates multiple processes leading to statural growth. IGF-1 metabolic actions are partly directed at stimulating the uptake of glucose, fatty acids, and amino acids so that metabolism supports growing tissues.

    • Synonyms

      R3 IGF1, R3 IGF-1, R3IGF1, R3IGF-1, LONG IGF1, LONG IGF-1, LONG R3 IGF1, LONG R3IGF1, LONG R3 IGF-1, LONG R3IGF-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LR3 IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution the LR3 IGF1 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 LR3 IGF1 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIV DECCFRSCDLRRLEMYCAPLKPAKSA.

    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.

    Long R3 Igf1 Human
  • View Data Sheet

    Name :

    Exodus-2 Mouse, Sf9

    Description:

    Exodus-2 (CCL21) Mouse Recombinant, Sf9

    Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    Product # :

    CHM-043

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    Description

    Exodus-2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (24-133aa) and having a molecular mass of 13.1kDa.Exodus-2 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Exodus-2 solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Exodus-2 protein or CCL21 is a cytokine, part of the CC chemokines subgroup. Because of its 6 conserved residues of the cysteine amino acid (instead of the 4 residues we usually see in chemokines), the protein is also named 6Ckine and SLC (secondary lymphoid-tissue chemokine). The gene that codes for this protein is located on chromosome 9 in humans. The Exodus-2 is binding to the CCR7 receptor, which is a chemokine receptor located to the cell’s surface.

    • Synonyms

      Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    • 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

      ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH

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    Exodus 2 Mouse
  • View Data Sheet

    Name :

    IDO1 Human

    Description:

    Indoleamine 2,3-Dioxygenase 1 Human Recombinant

    IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.

    Product # :

    ENZ-807

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    Description

    IDO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403a.a) and having a molecular mass of 47.7kDa. IDO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IDO1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.

    • Synonyms

      IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.

    • 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 MGSMAHAMEN SWTISKEYHI DEEVGFALPN PQENLPDFYN DWMFIAKHLP DLIESGQLRE RVEKLNMLSI DHLTDHKSQR LARLVLGCIT MAYVWGKGHG DVRKVLPRNI AVPYCQLSKK LELPPILVYA DCVLANWKKK DPNKPLTYEN MDVLFSFRDG DCSKGFFLVS LLVEIAAASA IKVIPTVFKA MQMQERDTLL KALLEIASCL EKALQVFHQI HDHVNPKAFF SVLRIYLSGW KGNPQLSDGL VYEGFWEDPK EFAGGSAGQS SVFQCFDVLL GIQQTAGGGH AAQFLQDMRR YMPPAHRNFL CSLESNPSVR EFVLSKGDAG LREAYDACVK ALVSLRSYHL QIVTKYILIP ASQQPKENKT SEDPSKLEAK GTGGTDLMNF LKTVRSTTEK SLLKEG.

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    Ido1 Human
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    Name :

    OXSR1 Human

    Description:

    Oxidative Stress Responsive 1 Human Recombinant

    Serine/threonine-protein kinase OSR1, Oxidative stress-responsive 1 protein, KIAA1101, OSR1, OXSR1, Oxidative Stress Responsive 1.

    Product # :

    PRO-2104

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    Description

    OXSR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 550 amino acids (1-527) and having a molecular mass of 60.4kDa.OXSR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OXSR1 solution (0.5mg/1ml) contains Phosphate Buffered Saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Oxidative Stress Responsive 1, also known as OXSR1 belongs to the neuronal calcium sensor gene family. OXSR1 encodes calcium-binding proteins which expressed mainly in neurons and regulates G protein-coupled receptor phosphorylation in a calcium-dependent way. OXSR1 regulates downstream kinases in response to environmental stress and functions in regulating the actin cytoskeleton.

    • Synonyms

      Serine/threonine-protein kinase OSR1, Oxidative stress-responsive 1 protein, KIAA1101, OSR1, OXSR1, Oxidative Stress Responsive 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSEDSSA LPWSINRDDY ELQEVIGSGA TAVVQAAYCA PKKEKVAIKR INLEKCQTSM DELLKEIQAM SQCHHPNIVS YYTSFVVKDE LWLVMKLLSG GSVLDIIKHI VAKGEHKSGV LDESTIATIL REVLEGLEYL HKNGQIHRDV KAGNILLGED GSVQIADFGV SAFLATGGDI TRNKVRKTFV GTPCWMAPEV MEQVRGYDFK ADIWSFGITA IELATGAAPY HKYPPMKVLM LTLQNDPPSL ETGVQDKEML KKYGKSFRKM ISLCLQKDPE KRPTAAELLR HKFFQKAKNK EFLQEKTLQR APTISERAKK VRRVPGSSGR LHKTEDGGWE WSDDEFDEES EEGKAAISQL RSPRVKESIS NSELFPTTDP VGTLLQVPEQ ISAHLPQPAG QIATQPTQVS LPPTAEPAKT AQALSSGSGS QETKIPISLV LRLRNSKKEL NDIRFEFTPG RDTAEGVSQE LISAGLVDGR DLVIVAANLQ KIVEEPQSNR SVTFKLASGV EGSDIPDDGK LIGFAQLSIS.

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    Oxsr1 Human
  • View Data Sheet

    Name :

    CMC1 Human

    Description:

    COX Assembly Mitochondrial Protein 1 Human Recombinant

    C3orf68, Cmc1p, COX assembly mitochondrial protein homolog.

    Product # :

    PRO-1651

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    Description

    CMC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106 a.a.) and having a molecular mass of 14.9kDa.CMC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CMC1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      COX Assembly Mitochondrial Protein 1(CMC1) is a member of the CMC family. CMC1 is required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. CMC1 attaches copper and might be involved in copper trafficking and distribution to COX and SOD1.

    • Synonyms

      C3orf68, Cmc1p, COX assembly mitochondrial protein homolog.

    • 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 MGSMALDPAD QHLRHVEKDV LIPKIMREKA KERCSEQVQD FTKCCKNSGV LMVVKCRKEN SALKECLTAY YNDPAFYEEC KMEYLKEREE FRKTGIPTKK RLQKLPTSM.

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    Cmc1 Human
  • View Data Sheet

    Name :

    REG1A Human

    Description:

    Regenerating Islet-Derived 1 Alpha Human Recombinant

    Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.

    Product # :

    PRO-289

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    Description

    The Recombinant Human REG 1 alpha is produced with N-terminal fusion His Tag. The Recombinant Human REG 1 alpha His-Tagged Fusion Protein, has a molecular weight of 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 alpha and 12 additional amino acid residues – His Tag.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 5mM Tris, 25mM NaCl, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
      Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system.

    • Synonyms

      Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.

    • 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

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

    • Amino Acid Sequence

      MKHHHHHHAS HMQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN.

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    Reg1A Human
  • View Data Sheet

    Name :

    ORM1 Human, HEK

    Description:

    Orosomucoid 1 Human Recombinant, HEK

    Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 1.

    Product # :

    PRO-2764

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    Description

    ORM1 Human Recombinant produced in HEK is a polypeptide chain containing 189 amino acids (19-201) and having a molecular mass of 22.4 kDa. The ORM1 is fused to a 6 a.a. amino acid His tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293

    Formulation

    The ORM1 solution (1mg/ml) contains 1x PBS pH-7 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      The acute phase plasma protein ORM1 synthesized by the liver mediates the interaction between blood cells and endothelial cells. In addition, together with haptoglobin and C reactive protein, ORM1 regulates the extravasation of the cells through infection and inflammation. Expression of ORM1 is induced by acute-phase stimulatory mediators such as bacterial lipopolysaccharides.

    • Synonyms

      Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 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

      QIPLCANLVP VPITNATLDR ITGKWFYIAS AFRNEEYNKS VQEIQATFFY FTPNKTEDTI FLREYQTRQD QCIYNTTYLN VQRENGTISR YVGGQEHFAH LLILRDTKTY MLAFDVNDEK NWGLSVYADK PETTKEQLGE FYEALDCLRI PKSDVVYTDW KKDKCEPLEK QHEKERKQEE GES HHHHHH

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    Orm1 Protein
  • View Data Sheet

    Name :

    GLO1 Human, Active

    Description:

    Glyoxalase-I Human Recombinant, Active

    GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.

    Product # :

    ENZ-999

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    Description

    Glyoxalase-I Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 184 amino acids and having a molecular mass of 20.7 kDa. Glyoxalase-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Glyoxalase-1 solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 400 units/mg. One unit will form 1.0umol of S-lactoylgutathione from methylglyoxal and reduced glutathione per minute at pH6.5 at 25C

    More Info

    • Introduction

      GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

    • Synonyms

      GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.

    • 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

      MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIAWALSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM.

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    Glo1 Human Active
  • View Data Sheet

    Name :

    MIG Bovine

    Description:

    MIG (CXCL9) Bovine Recombinant

    Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.

    Product # :

    CHM-041

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    Description

    MIG (CXCL9) BovineRecombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 104 amino acids and having a molecular mass of approximately 18.0kDa.MIG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.

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    • Introduction

      Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belongs to the CXC chemokine family that is also known as Monokine induced by gamma INF (MIG). CXCL9 is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.

    • Synonyms

      Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIG (CXCL9) 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 MIG (CXCL9) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VPAIRNGRCS CINTSQGMIH PKSLKDLKQF APSPSCEKTE IIATMKNGNE ACLNPDLPEV KELIKEWEKQ VNQKKKQRKG KKYKKTKKVP KVKRSQRPSQ KKTT.

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    Cxcl9 Bovine
  • View Data Sheet

    Name :

    Flt3 Ligand Porcine

    Description:

    Flt3 Ligand Porcine Recombinant

    Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    Product # :

    CYT-1041

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    Description

    Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

    • Synonyms

      Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

    • Background

      What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
      FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.

      What is the source or expression system of FLT3 LIGAND PORCINE Protein?
      Escherichia Coli.

      What is the Purity of FLT3 LIGAND PORCINE Protein?
      FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
      The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.

      What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
      MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

      What applications can FLT3 LIGAND PORCINE Protein be used in?
      FLT3 LIGAND PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FLT3 LIGAND PORCINE Protein?
      The endotoxin level is minimal, FLT3 LIGAND PORCINE Protein was purified using conventional chromatography techniques.

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    Flt3 Ligand Porcine
  • View Data Sheet

    Name :

    LGALS3 Mouse, Active

    Description:

    Galectin-3 Mouse Recombinant, BioActive

    Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.

    Product # :

    CYT-1151

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    • sds-page

    Description

    LGALS3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids ( 1-264 a.a) and having a molecular mass of 29.8kDa.LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    LGALS3 protein (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol,1mM DTT and 2mM EDTA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml. 

    sds-page

    LGALS3-sds-page - Product image 1

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    • Introduction

      Galectin 3, or LGALS3, is a protein which belongs to the animal lectins family, that binds betagalactoside residues selectively. LGALS3 is originated and leaves cells through ectocytosis. The protein is capable of inhibition apoptosis and the development of cancer. Galectin 3 is found in epithelial tissues in organisms, it can be located in dendritic cells, Kupffer cells, macrophages etc. LGALS3 levels elevated when inflammation is generating, cell proliferation, trans-activation by viral proteins and cell differentiation.

    • Synonyms

      Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.

    • 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 MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.

    • Background

      What is the molecular weight/Mw of LGALS3 MOUSE Protein?
      LGALS3 MOUSE Protein has a total Mw of 29.8kDa.

      What is the source or expression system of LGALS3 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of LGALS3 MOUSE Protein?
      LGALS3 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS3 MOUSE Protein?
      Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

      What is the amino acid sequence of LGALS3 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.

      What applications can LGALS3 MOUSE Protein be used in?
      LGALS3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

    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.

    Galectin 3 Mouse
  • View Data Sheet

    Name :

    Bcl XL Mouse

    Description:

    B-Cell Leukemia/Lymphoma XL Mouse Recombinant

    BclXL, Bcl-X(L), Bcl-XL.

    Product # :

    PRO-1362

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    Description

    Bcl-XL Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids, having an MW of 23.7kDa.The Bcl-XL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bcl-XL Mouse was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.

    Purity

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

    More Info

    • Introduction

      Bcl-XL is a transmembrane protein located in the mitochondrial membranes of cells that are long-lived and postmitotic, such as adult brain cells. It plays arole in the signal transduction pathway of the FAS-Ligand. Bcl-XL is an anti-apoptotic protein which is a member of the Bcl-2 family which are able to form heterodimers, and this is an significant event in the regulation of apoptosis. BCL-XL is involved in the survival of cancer cells.
      Bcl-xL is the leading monitor of apoptosis/active cell suicide. Bcl-xL has cell death repressor activity and therefore acts as a survival protein.

    • Synonyms

      BclXL, Bcl-X(L), Bcl-XL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SQSNRELVVD FLSYKLSQKG YSWSQFSDVE ENRTEAPEET EAERETPSAI NGNPSWHLAD SPAVNGATGH SSSLDAREVI PMAAVKQALR EAGDEFELRY RRAFSDLTSQ LHITPGTAYQ SFEQVVNELF RDGVNWGRIV AFFSFGGALC VESVDKEMQV LVSRIASWMA TYLNDHLEPW IQENGGWDTF VDLYGNNAAA ESRKGQERFN R.

    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.

    Bcl Xl Mouse
  • View Data Sheet

    Name :

    CYTL1 Human

    Description:

    Cytokine-Like 1 Human Recombinant

    Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.

    Product # :

    CYT-775

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    Description

    CYTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 23-136) containing 124 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 14.6kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    CYTL1 was filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokine-like protein 1 (CYTL1) is a secreted protein. CYTL1 is expressed in CD34+ cell populations of bone marrow and cord blood which function as hematopoietic stem/progenitor cells. However, CYTL1 is not expressed in CD34- cells. Experiments with knock-out mice (Cytl1-/-) propose that CYTL1 is essential for the maintenance of cartilage homeostasis rather than cartilage and bone development, and loss of CYTL1 function is linked with experimental osteoarthritic cartilage destruction in mice.

    • Synonyms

      Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.

    • 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. CYTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.

    • Background

      Title: Cytokine-Like 1 Human Recombinant: Exploring its Role in Immune Regulation and Therapeutic Potential

      Abstract:


      Cytokine-like 1 (CYTL1) is an emerging cytokine that exhibits pleiotropic effects on immune regulation and tissue homeostasis. This research paper provides a comprehensive analysis of human recombinant CYTL1, focusing on its production, characterization, and potential applications in immune modulation. The paper highlights the significance of CYTL1 in immune cell function, inflammation, and tissue repair. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYTL1 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYTL1 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Cytokine-like 1 (CYTL1) is a recently discovered cytokine with diverse biological functions, including immune regulation and tissue repair. Human recombinant CYTL1, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological activities and explore its therapeutic potential.

      Production and Characterization:


      Recombinant CYTL1 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYTL1.

      Role in Immune Regulation:


      CYTL1 has been shown to modulate immune cell function and inflammation. It can influence the differentiation and activation of various immune cell subsets, including T cells and macrophages. Recombinant CYTL1 serves as a valuable tool for investigating the mechanisms underlying immune regulation and exploring its potential as an immunomodulatory agent.

      Therapeutic Implications:


      The dysregulation of immune responses is associated with numerous pathological conditions, including autoimmune diseases and chronic inflammation. Recombinant CYTL1 holds promise as a potential immunotherapeutic agent due to its ability to modulate immune cell function and regulate inflammatory processes. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYTL1 in various diseases, including autoimmune disorders and tissue regeneration.

      Conclusion:


      Human recombinant CYTL1 is a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune regulation contribute to our understanding of immune responses and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYTL1 offer promising avenues for improving outcomes in autoimmune diseases, chronic inflammation, and tissue repair.

      What is the molecular weight/Mw of CYTL1 Protein?
      CYTL1 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of CYTL1 Protein?
      Escherichia Coli.

      What is the Purity of CYTL1 Protein?
      CYTL1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CYTL1 Protein?
      The biological functionality of CYTL1 Protein will be determined in the future.

      What is the amino acid sequence of CYTL1 Protein?
      MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.

      What applications can CYTL1 Protein be used in?
      CYTL1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CYTL1 Protein?
      The endotoxin level is minimal, CYTL1 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.

    Cytl1 Human
  • View Data Sheet

    Name :

    IL1RL1 Human, Sf9 Active

    Description:

    Interleukin-1 Receptor Like-1 Human Recombinant, Sf9 Active

    Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 1.

    Product # :

    CYT-1052

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    Description

    IL1RL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 318 amino acids (19-328a.a.) and having a molecular mass of 36.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL1RL1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL1RL1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is less or equal to 10ng/ml with IL-33.

    More Info

    • Introduction

      The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.

    • Synonyms

      Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 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

      KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.

    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.

    Il1Rl1
  • View Data Sheet

    Name :

    FASLG Human, HEK

    Description:

    FAS Ligand Human Recombinant, HEK

    Fas ligand (TNF superfamily, member 6), APT1LG1, FASL, TNFSF6, CD178, tumor necrosis factor (ligand) superfamily member 6, Apoptosis antigen ligand, Fas antigen ligand, APTL, CD95-L.

    Product # :

    CYT-051

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    Description

    Recombinant Human FAS Ligand produced in HEK293 cells is a polypeptide chain containing 147 amino acids (134-281a.a).FASLG is fused to a 6 amino acid His-tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The FASLG solution (0.6mg/ml) contains 1xPBS.

    Purity

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

    Biological Activity

    Fas ligand is biologically active as determined by its ability to induce cytotoxicity in Jurkat cells in the absence of any cross-linking. The expected ED50< 10 ng/ml, corresponding to a specific activity of 1x105 units/mg.

    More Info

    • Introduction

      The type II transmembrane protein FASLG is a member of the tumor necrosis factor (TNF) superfamily. A fas ligand/receptor interaction has a significant part in the regulation of the immune system and the advancement of cancer. FASLG is expressed on the activated T cell surface as a nondisulfidelinked homotrimer. FASLG binding to Fas/CD95/TNFRSF6 on a nearby cell prompts apoptosis in the Fas expressing cell. FASLG is released from the cell surface by metalloproteinases as a soluble molecule that stays trimeric and is able to bind with Fas, but its capability to activate apoptosis is radically reduced. In addition, FASLG binds to DcR3 - a soluble trap receptor with no signal transduction capabilities. Flawed Fas-mediated apoptosis causes oncogenesis in addition to drug resistance in existing tumors. Constitutive expression of FASLG in a variety of tumors enables their immune evasion. Both mouse and human FASLG are active on mouse and human cells.

    • Synonyms

      Fas ligand (TNF superfamily, member 6), APT1LG1, FASL, TNFSF6, CD178, tumor necrosis factor (ligand) superfamily member 6, Apoptosis antigen ligand, Fas antigen ligand, APTL, CD95-L.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      FASLG Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Background

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

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

      What is the Biological Activity of FASL Protein?
      Fas ligand is biologically active as determined by its ability to induce cytotoxicity in Jurkat cells in the absence of any cross-linking. The expected ED50< 10 ng/ml, corresponding to a specific activity of 1x105 units/mg.

      What is the amino acid sequence of FASL Protein?
      FASL Protein is composed from 147 amino acids.

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

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

    Faslg Human Hek
  • View Data Sheet

    Name :

    NCR3 antibody

    Description:

    Mouse Anti Human Natural Cytotoxicity Triggering Receptor 3

    Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    Product # :

    ANT-740

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    Formulation

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

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    • Introduction

      Cytotoxicity Triggering Receptor 3 also known as NCR3 is a natural cytotoxicity receptor (NCR) which assists NK cells in the lysis of tumor cells. Moreover, NCR3 interacts with CD3-zeta (CD247), a T-cell receptor. A single nucleotide polymorphism in the 5' untranslated region of NCR3 has been related with mild malaria suceptibility. Three transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human NCR3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human NCR3 protein 19-138 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT38D9AT.

    • Applications

      NCR3 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.

    • 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

      NCR3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Ncr3 Antibody
  • View Data Sheet

    Name :

    CCN1 (275-381)

    Description:

    Cysteine-Rich Angiogenic Inducer 61 (275-381 a.a.) Human Recombinant

    CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.

    Product # :

    CYT-1235

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    Description

    The CYR61Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CYR61His-Tagged Fusion Protein, produced in E. coli, is a 17kDa protein containing 107 amino acid residues of the CYR61Human, 275-381 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Synonyms

      CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized CYR61at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      Cysteine-Rich Angiogenic Inducer 61 also known as CYR61 is a growth factor-inducible, immediate-early gene which has many activities in various cancers. CYR61 is a part of to the CCN family a group of secreted extracellular matrix-associated proteins which regulate diverse biological processes including cell adhesion, proliferation, migration, survival and angiogenesis. CYR61 plays a significant role in development, tissue repair, wound healing, and various pathological conditions such as cancer and fibrosis. CYR61 is encoded by a growth factor-inducible immediate-early gene. CYR61 promotes the adhesion of endothelial cells by interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.

      What is the molecular weight/Mw of CCN1 Protein?
      CCN1 Protein has a total Mw of 17kDa.

      What is the source or expression system of CCN1 Protein?
      Escherichia Coli.

      What is the Purity of CCN1 Protein?
      CCN1 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCN1 Protein?
      The biological functionality of CCN1 Protein will be determined in the future.

      What is the amino acid sequence of CCN1 Protein?
      CCN1 Protein is composed from 107 amino acids.

      What applications can CCN1 Protein be used in?
      CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCN1 Protein?
      The endotoxin level is minimal, CCN1 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.

    Cyr61 Protein
  • View Data Sheet

    Name :

    UCHL1 (1-126) Human

    Description:

    Ubiquitin Carboxyl-Terminal Hydrolase L1 (1-126) Human Recombinant

    PGP 9.5, UCHL1, PGP9.5, PARK5.

    Product # :

    PRO-2823

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    Description

    The UCHL1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCHL1 His-Tagged Fusion Protein, produced in E. coli, is a 19kDa protein containing 126 amino acid residues of the UCHL1 Human, 1-126 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      PGP 9.5, UCHL1, PGP9.5, PARK5.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized UCHL1 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      Human Ubiquitin Carboxyl-Terminal Hydrolase L1 (UCH-L1) is an important enzyme involved in the ubiquitin-proteasome system, which regulates protein degradation and turnover in cells.

      UCHL1 Function:

      UCHL1 mainly removes ubiquitin molecules from proteins, thereby recycling ubiquitin and regulating protein stability. This action is important for controlling various cellular processes and maintaining cellular homeostasis and.

      UCHL1 Structure

      UCHL1 is characterized by a catalytic domain which facilitates its hydrolase activity, allowing it to cleave ubiquitin from substrates.

      UCHL1 Role in Neurodegeneration

      UCHL1 has been implicated in neurodegenerative diseases, such as Parkinson’s and Alzheimer's disease. Its expression levels and activity can affect neuronal survival and function.

      UCH-L1 is also studied in the context of cancer. Altered levels of UCHL1 may affect on tumour progression and response to therapy.

      UCHL1 Biomarker Potential

      UCHL1 is being investigated as a potential biomarker for diseases, especially neurodegenerative disorders due to its involvement in various pathologies.

      UCHL1 Research

      Ongoing studies focus on understanding its role in various cellular contexts, its regulation, and its potential as a therapeutic target.

      In conclusion, UCHL1 is a very important component of cellular regulation, with implications in health and disease.

    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.

    Uchl1 Protein
  • View Data Sheet

    Name :

    GHRP6

    Description:

    Growth Hormone Releasing Peptide-6

    GHRP-6, GHRP6

    Product # :

    HOR-298

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    • description
    • formulation
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    Description

    Growth Hormone Releasing Peptide-6 Synthetic is a single, non-glycosylated polypeptide chain containing 6 amino acids, having a molecular mass of 873 Dalton and a Molecular formula of C46H56N12O6.

    Formulation

    The GHRP-6 peptide was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by analysis by RP-HPLC.

    More Info

    • Introduction

      GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH act directly on pituitary somatotrophs to stimulate GH release. Growth hormone (GH) release is stimulated by a variety of synthetic secretagogues, of which growth hormone-releasing hexapeptide (GHRP-6) has been most thoroughly studied; it is thought to have actions at both pituitary and hypothalamic site.

    • Synonyms

      GHRP-6, GHRP6

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Hormone Releasing Peptide-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP-6 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 GHRP-6 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      His-D-Trp-Ala-Trp-D-Phe-Lys-NH2.

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

    Ghrp 6
  • View Data Sheet

    Name :

    MIP 3b Human

    Description:

    Macrophage Inflammatory Protein-3 Beta Human Recombinant (CCL19)

    Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433.

    Product # :

    CHM-287

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    • source
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    Description

    Macrophage Inflammatory Protein-3 beta Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8.8kDa. The MIP-3b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized without any additives.

    Purity

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

    Biological Activity

    The Activity of CCL19 is calculated by the ability to chemoattract Human T cells using a concentration of 7-40ng/ml corresponding to a Specific Activity of 25,000-143,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colon and low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cells and antigen-engaged B cells.

    • Synonyms

      Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL19 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 Macrophage Inflammatory Protein-3b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GTNDAEDCCL SVTQKPIPGY IVRNFHYLLI KDGCRVPAVV FTTLRGRQLC APPDQPWVER IIQRLQRTSA KMKRRSS.

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

    Mip 3B Human
  • View Data Sheet

    Name :

    SCGB1A1 Human

    Description:

    Uteroglobin Human Recombinant

    Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

    Product # :

    CYT-743

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    Description

    Uteroglobin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 15.8kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.

    More Info

    • Introduction

      Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.

    • Synonyms

      Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.

    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.

    Scgb1A1 Human
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