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Search results

1000 results found for “Centromere Protein”

Name

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  • View Data Sheet

    Name :

    COMP Human

    Description:

    Cartilage Oligomeric Matrix Protein Human Recombinant

    Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5

    Product # :

    PRO-2727

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    Description

    COMP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 749 amino acids (21-757a.a) and having a molecular mass of 82.4kDa.COMP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The COMP solution (0. 5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COMP is a non-collagenous glycoprotein and is belongs to the thrombospondin family of extracellular proteins. COMP is a calcium-binding protein of high molecular weight (>500kDa) found in the extracellular matrix of articular, nasal and tracheal cartilage. COMP is not only cartilage-derived but is common in other tissues, such as synovium and tendon. Intact COMP is pentameric, with 5 equal subunits and the carboxy-terminal globular domain of native COMP binds to collagens I, II, and IX. COMP molecules are vital for conserving the properties and integrity of collagen network. Moreover, COMP has a storage and delivery function for hydrophobic cellsignaling molecules such as vitamin D. Mutations of the COMP gene cause Pseudoachondroplasia and some forms of multiple epiphyseal dysplasia which implicates that it is vital that COMP develops and functions normally.

    • Synonyms

      Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-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

      ADPDAHSLWY NFTIIHLPRH GQQWCEVQSQ VDQKNFLSYD CGSDKVLSMG HLEEQLYATD AWGKQLEMLR EVGQRLRLEL ADTELEDFTP SGPLTLQVRM SCECEADGYI RGSWQFSFDG RKFLLFDSNN RKWTVVHAGA RRMKEKWEKD SGLTTFFKMV SMRDCKSWLR DFLMHRKKRL EPTAPPTMAP GLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH

    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.

    Comp Protein
  • View Data Sheet

    Name :

    CCNH Antibody

    Description:

    Cyclin-H, Mouse Anti Human

    CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    Product # :

    ANT-583

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    Formulation

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

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    • Introduction

      CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

    • Synonyms

      CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CCNH mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CCNH amino acids 1-323 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT3G6AT.

    • Applications

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

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      CCNH 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.

    Ccnh Antibody
  • View Data Sheet

    Name :

    CXCL8 Human (1-72)

    Description:

    Interleukin-8 (1-72 a.a.) Human Recombinant (CXCL8)

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

    Product # :

    CHM-231

    Price :

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    • description
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    Description

    Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 72 amino acids and having a molecular mass of 8452 Dalton. The IL-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL-8 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 Interleukin-8 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 Ser-Ala-Lys-Glu-Leu.

    • Background

      What is the molecular weight/Mw of CXCL8 HUMAN (1-72) Protein?
      CXCL8 HUMAN (1-72) Protein has a total Mw of 8.45kDa.

      What is the source or expression system of CXCL8 HUMAN (1-72) Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN (1-72) Protein?
      CXCL8 HUMAN (1-72) Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN (1-72) Protein?
      Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CXCL8 HUMAN (1-72) Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.

      What applications can CXCL8 HUMAN (1-72) Protein be used in?
      CXCL8 HUMAN (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN (1-72) Protein?
      The endotoxin level is minimal, CXCL8 HUMAN (1-72) 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.

    Il 8 72 Human
  • View Data Sheet

    Name :

    MOG Human

    Description:

    Myelin Oligodendrocyte Glycoprotein Human Recombinant

    Myelin Oligodendrocyte Glycoprotein, MOG, MOGIG-2, MGC26137.

    Product # :

    PRO-466

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    Quantity :

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    • description
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    Description

    Myelin Oligodendrocyte Glycoprotein produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 132 amino acids (Met + 30-154 a.a. + 6x His tag at C-terminus) and having a total molecular mass of 15.2 kDa.

    Source

    Escherichia Coli.

    Formulation

    The Myelin Oligodendrocyte Glycoprotein was lyophilized from a 0.2µm filtered solution in 20mM HAc-NaAc and 150mM NaCl pH-4.5

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myelin Oligodendrocyte Glycoprotein is a membrane protein expressed on the oligodendrocyte cell surface and the outermost surface of myelin sheaths. Due to this localization, it is a prime target antigen that plays a role in immune-mediated demyelination. Myelin Oligodendrocyte Glycoprotein is involved in completion and maintenance of the myelin sheath and in cell-cell communication. MOG protein was found to differentially expressed in the dorsolateral prefrontal cortex and in the temporal lobe from patients with schizophrenia. MOG-specific antibody is crucial to the initiation of MOG-induced murine experimental autoimmune encephalomyelitis.

    • Synonyms

      Myelin Oligodendrocyte Glycoprotein, MOG, MOGIG-2, MGC26137.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MOG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MOG 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 MOG in sterile 50mM Acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGQFRVIGPRHPIRALVGDEVELPCRISPGKNATGMEVGWYRPPFSRVVHLYRN
      GKDQDGDQAPEYRGRTELLKDAIGEGKVTLRIRNVRFSDEGGFTCFFRDHSYQE
      EAAMELKVEDPFYWVSPGHHHHHH.

    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.

    Mog Human
  • View Data Sheet

    Name :

    SSSCA1 Human

    Description:

    Sjogren Syndrome/Scleroderma Autoantigen 1 Human Recombinant

    Sjogren Syndrome/Scleroderma Autoantigen 1, Sjogren'S Syndrome/Scleroderma Autoantigen 1, Autoantigen P27, Centromeric Autoantigen (27kD), p27, Sjoegren Syndrome/Scleroderma Autoantigen 1.

    Product # :

    PRO-1743

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    Description

    SSSCA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-199aa) and having a molecular mass of 23.9kDa. SSSCA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SSSCA1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sjogren syndrome/scleroderma autoantigen 1, SSSCA1 is involved in mitosis. SSSCA1 is a centromere-associated protein which can induce anti-centromere antibodies. In addition SSSCA1 is recognized by a subset of anti-centromere antibodies from patients with sclerodermaand Sjogren's syndrome.

    • Synonyms

      Sjogren Syndrome/Scleroderma Autoantigen 1, Sjogren'S Syndrome/Scleroderma Autoantigen 1, Autoantigen P27, Centromeric Autoantigen (27kD), p27, Sjoegren Syndrome/Scleroderma Autoantigen 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMALNGAE VDDFSWEPPT EAETKVLQAR RERQDRISRL MGDYLLRGYR MLGETCADCG TILLQDKQRK IYCVACQELD SDVDKDNPAL NAQAALSQAR EHQLASASEL PLGSRPAPQP PVPRPEHCEG AAAGLKAAQG PPAPAVPPNT DVMACTQTAL LQKLTWASAE LGSSTSLETS IQLCGLIRAC AEALRSLQQL QH

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    Sssca1 Human
  • View Data Sheet

    Name :

    BMF Human

    Description:

    Bcl2 Modifying Factor, Isoform 3 Human Recombinant

    Bcl-2-modifying factor, FLJ00065, BMF.

    Product # :

    PRO-700

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    Description

    Bcl2 modifying factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids (1-129 a.a.) and having a molecular mass of 15.6 kDa.The Bcl2 modifying factor is fused to 15 amino acid His Tag at Nterminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Bcl2 modifying factor solution contains 20mM Tris pH-7.5, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Bcl2 modifying factor, is a member of the Bcl2 protein family of apoptosis mediators. Bcl2 modifying factor is widely expressed in many tissues.
      Bcl2 modifying factor contains a single Bcl2 homology domain 3 (BH3), and binds Bcl2 proteins and functions as an apoptotic activator. Also, Bcl2 modifying factor is important for histone deacetylase (HDAC) inhibitors which alters the balance between acetylation and deacetylation, significantly increasing histone acetylation, while strongly inducing apoptosis in a variety of cancer cell types. Bcl2 modifying factor supports Bim in regulating cell death processes in response to many stimuli. A synergistic role for bim and Bcl2 modifying factor in an apoptotic pathway leading to the clearance of Neisseria gonorrhoeae -infected cells.

    • Synonyms

      Bcl-2-modifying factor, FLJ00065, BMF.

    • 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

      MASMTGGQQM GRGSHMEPSQ CVEELEDDVF QPEDGEPVTQ PGSLLSADLF AQSLLDCPLS RLQLFPLTHC CGPGLRPTSQ EDKATQTLSPASPSQGVMLP CGVTEEPQRL FYAPAEPKSC VVADPPLPAQ PCFEWRREQE RGRP.

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    Bcl2 Modifying Factor Human
  • View Data Sheet

    Name :

    MoeX

    Description:

    Mycobacterium Tuberculosis MoeX Recombinant

    Product # :

    PRO-1919

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    Description

    Recombinant Mycobacterium Tuberculosis MoeX produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 38 kDa. The MoeX is fused to a His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MoeX protein solution 0.75mg/ml contains 1xPBS, 25mM arginine and 0.02% NaN3.

    Purity

    Protein is >95% pure as determined by 12% PAGE (coomassie staining).

    More Info

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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    Moex
  • 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 :

    DPH3P1 Human

    Description:

    Diphthamide Biosynthesis 3 Pseudogene 1 Human Recombinant

    Diphthamide Biosynthesis 3 Pseudogene 1, C20orf143, DPH3B, ZCSL1, CSL-Type Zinc Finger-Containing Protein 1, Chromosome 20 Open Reading Frame 143, DPH3, KTI11 Homolog (S. Cerevisiae) Pseudogene, DPH3B, KTI11 Homolog B (S. Cerevisiae), Zinc Finger, CSL-Type Containing 1, DPH3 Homolog B (KTI11, S. Cerevisiae), Putative DPH3 Homolog B, Zinc Finger, CSL Domain Containing 1.

    Product # :

    PRO-1914

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    Description

    DPH3P1 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 11.1kDa.DPH3P1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DPH3P1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Diphthamide Biosynthesis 3 Pseudogene 1 also known as DPH3P1 may stand for a processed pseudogene of DPH3 since it lacks the exon/intron structurefound in the functional gene. Yet, DPH3P1 does contain an intact open reading frame, though its translation has not been established.

    • Synonyms

      Diphthamide Biosynthesis 3 Pseudogene 1, C20orf143, DPH3B, ZCSL1, CSL-Type Zinc Finger-Containing Protein 1, Chromosome 20 Open Reading Frame 143, DPH3, KTI11 Homolog (S. Cerevisiae) Pseudogene, DPH3B, KTI11 Homolog B (S. Cerevisiae), Zinc Finger, CSL-Type Containing 1, DPH3 Homolog B (KTI11, S. Cerevisiae), Putative DPH3 Homolog B, Zinc Finger, CSL Domain Containing 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAVFHDE VEIEDFQYDE DSETYFCPCP CGDNFSITKE ELENGEGVAM CPGCSLIIKV IYDKDQFACG ETVPVPSVNK E

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    Dph3P1 Human
  • View Data Sheet

    Name :

    CCL1 Human, His

    Description:

    I-309 (CCL1) Human Recombinant, His Tag

    Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

    Product # :

    CHM-254

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    • SDS-PAGE

    Description

    I-309 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 94 amino acids (24-96 a.a.) and having a molecular mass of 10.8kDa. The I-309 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The I-309 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    CCL1 Human, His-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.

    • Synonyms

      Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

    • 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 MKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK.

    • Background

      What is the molecular weight/Mw of CCL1 HUMAN, HIS Protein?
      CCL1 HUMAN, HIS Protein has a total Mw of 10.8kDa.

      What is the source or expression system of CCL1 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL1 HUMAN, HIS Protein?
      CCL1 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL1 HUMAN, HIS Protein?
      The biological functionality of CCL1 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL1 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK.

      What applications can CCL1 HUMAN, HIS Protein be used in?
      CCL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL1 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.


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

    I 309 Human His
  • View Data Sheet

    Name :

    A2LD1 Human

    Description:

    AIG2-Like Domain 1 Human Recombinant

    Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.

    Product # :

    PRO-172

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    Description

    A2LD1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 173 amino acids (1-153 a.a.) and having a molecular mass of 19.4kDa. The A2LD1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The A2LD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gamma-glutamylaminecyclotransferase (A2LD1) is an enzyme which converts gamma-glutamylamines to free amines and 5-oxoproline. A2LD1 demonstrates high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. A2LD1 assists in the proteolytic degradation of crosslinked fibrin by breaking down isodipeptide L-gamma-glutamyl-L-epsilon-lysine, which is a byproduct of fibrin degradation. The reaction catalyzed by the A2LD1 produces 5-oxo-L-proline and a free alkylamine.

    • Synonyms

      Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.

    • 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 MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI PWLLHLPGSG RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED RAPGAEEPPA PTAVQCFVYS RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR ENR.

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    A2LD1 Human
  • View Data Sheet

    Name :

    FKBP4 Human

    Description:

    FK506 Binding Protein 4 Human Recombinant

    HBI, p52, Hsp56, FKBP52, FKBP59, PPIase, FKBP4, FK506-binding protein 4, Peptidyl-prolyl cis-trans isomerase, HSP-binding immunophilin, FKBP52 protein, 52 kDa FK506-binding protein, p59 protein.

    Product # :

    ENZ-412

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    Description

    FKBP4 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 479 amino acids (1-459 a.a.) and having a molecular mass of 53.9 kDa.FKBP4 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FKBP4 protein solution contains 20mM Tris-HCl, pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH 8.0 using chymotrypsin.

    More Info

    • Introduction

      FKBP4 is part of the immunophilin protein family, which takes part in immunoregulation and necessary cellular processes concerning protein folding and trafficking. FKBP4 is a cis-trans prolyl isomerase that connects to the immunosuppressants FK506 and rapamycin. FKBP4 has high structural and functional similarity to FKBP1A, though, FKBP4 does not have immunosuppressant activity when complexed with FK506. FKBP4 is known to connect with phytanoyl-CoA alpha-hydroxylase. FKBP4 associates with HSP90 & HSP70 thus takes part in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. FKBP4 highly associates with adeno-associated virus type 2 vectors (AAV) resulting in a considerable increase in AAV-mediated transgene expression in human cell lines. FKBP4 is involved in the optimal use of AAV vectors in human gene therapy.

    • Synonyms

      HBI, p52, Hsp56, FKBP52, FKBP59, PPIase, FKBP4, FK506-binding protein 4, Peptidyl-prolyl cis-trans isomerase, HSP-binding immunophilin, FKBP52 protein, 52 kDa FK506-binding protein, p59 protein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MTAEEMKATE SGAQSAPLPM EGVDISPKQD EGVLKVIKRE GTGTEMPMIG DRVFVHYTGW LLDGTKFDSS LDRKDKFSFDLGKGEVIKAW DIAIATMKVG EVCHITCKPE YAYGSAGSPP KIPPNATLVF EVELFEFKGE DLTEEEDGGI IRRIQTRGEG YAKPNEGAIV EVALEGYYKDKLFDQRELRF EIGEGENLDL PYGLERAIQR MEKGEHSIVY LKPSYAFGSV GKEKFQIPPN AELKYELHLK SFEKAKESWE MNSEEKLEQS TIVKERGTVYFKEGKYKQAL LQYKKIVSWL EYESSFSNEE AQKAQALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS NNEKGLFRRG EAHLAVNDFE LARADFQKVLQLYPNNKAAK TQLAVCQQRI RRQLAREKKL YANMFERLAE EENKAKAEAS SGDHPTDTEM KEEQKSNTAG SQSQVETEA.

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    Fkbp4 Human
  • View Data Sheet

    Name :

    BMP6 Human

    Description:

    Bone Morphogenetic protein-6 Human Recombinant

    Bone morphogenetic protein 6, BMP-6, VG-1-related protein, VG-1-R, VGR-1, BMP6, VGR, VGR1.

    Product # :

    CYT-754

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    • sds-page

    Description

    BMP6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (375-513) and having a molecular mass of 18kDa.BMP6 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BMP6 solution (0.25mg/ml) contains 10mM Sodium citrate buffer (pH 3.5) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    BMP6-sds-page - Product image 1

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules, which can induce ectopic bone growth. Various BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were initially identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based upon its expression early in embryogenesis, BMP6 has a suggested role in early development. Moreover, the fact that the BMP6 is closely related to BMP5 and BMP7 leads to an assumption of possible bone inductive activity.

    • Synonyms

      Bone morphogenetic protein 6, BMP-6, VG-1-related protein, VG-1-R, VGR-1, BMP6, VGR, VGR1.

    • 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 MGSHMSASSR RRQQSRNRST QSQDVARVSS ASDYNSSELK TACRKHELYV SFQDLGWQDW IIAPKGYAAN YCDGECSFPL NAHMNATNHA IVQTLVHLMN PEYVPKPCCA PTKLNAISVL YFDDNSNVIL KKYRNMVVRA CGCH.

    • Background

      Bone Morphogenetic Protein-6 Human Recombinant: Unraveling its Therapeutic Potential in Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-6 (BMP-6) human recombinant is a critical member of the bone morphogenetic protein family, known for its pivotal role in tissue development, repair, and regeneration. This research paper aims to provide a comprehensive analysis of BMP-6, including its characteristics, signaling pathways, and potential therapeutic applications. Moreover, innovative methodologies for the production and optimization of BMP-6 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine have emerged as promising approaches to address the challenges associated with tissue repair and regeneration. BMP-6, a prominent member of the BMP family, plays a key role in regulating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-6 and presents novel approaches for the production and optimization of BMP-6 human recombinant, aiming to unlock its therapeutic potential in diverse regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-6 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling pathways. BMP-6 signaling cascades, including Smad-dependent and Smad-independent pathways, orchestrate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.

      Production of BMP-6 Human Recombinant:

      Efficient production methodologies are vital for harnessing the therapeutic potential of BMP-6 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been employed for the production of functional BMP-6. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been implemented to enhance the yield and bioactivity of BMP-6 recombinant protein.

      Potential Therapeutic Applications:

      BMP-6 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its regulatory role in bone formation, cartilage regeneration, and wound healing positions it as a potential therapeutic candidate for the treatment of skeletal disorders, osteoarthritis, and tissue injuries. Furthermore, the ability of BMP-6 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in various regenerative processes.

      Conclusion:

      BMP-6 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in bone and cartilage formation, as well as wound healing, BMP-6 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.

      What is the molecular weight/Mw of BMP6 Protein?
      BMP6 Protein has a total Mw of 18kDa.

      What is the source or expression system of BMP6 Protein?
      Escherichia Coli.

      What is the Purity of BMP6 Protein?
      BMP6 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP6 Protein?
      The biological functionality of BMP6 Protein will be determined in the future.

      What is the amino acid sequence of BMP6 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMSASSR RRQQSRNRST QSQDVARVSS ASDYNSSELK TACRKHELYV SFQDLGWQDW IIAPKGYAAN YCDGECSFPL NAHMNATNHA IVQTLVHLMN PEYVPKPCCA PTKLNAISVL YFDDNSNVIL KKYRNMVVRA CGCH.

      What applications can BMP6 Protein be used in?
      BMP6 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP6 Protein?
      The endotoxin level is minimal, BMP6 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.

    Bmp6 Human
  • View Data Sheet

    Name :

    ING2 Human

    Description:

    Inhibitor of Growth Family, Member 2 Human Recombinant

    Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

    Product # :

    PRO-1739

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    Description

    ING2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 35.2kDa.ING2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ING2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).

    • Synonyms

      Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

    • 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 MGSMLGQQQQ QLYSSAALLT GERSRLLTCY VQDYLECVES LPHDMQRNVS VLRELDNKYQ ETLKEIDDVY EKYKKEDDLN QKKRLQQLLQ RALINSQELG DEKIQIVTQM LELVENRARQ MELHSQCFQD PAESERASDK AKMDSSQPER SSRRPRRQRT SESRDLCHMA NGIEDCDDQP PKEKKSKSAK KKKRSKAKQE REASPVEFAI DPNEPTYCLC NQVSYGEMIG CDNEQCPIEW FHFSCVSLTY KPKGKWYCPK CRGDNEKTMD KSTEKTKKDR RSR.

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    Ing2 Human
  • View Data Sheet

    Name :

    UCHL1 Mouse, Active

    Description:

    Ubiquitin Carboxyl-Terminal Esterase L1 Mouse Recombinant, Active

    Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.

    Product # :

    PRO-2424

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    Description

    UCHL1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 27.2kDa. UCHL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UCHL1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 70 pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of ubiquitin-AMC per minute at pH 7.5, at 37°C.

    More Info

    • Introduction

      Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.

    • Synonyms

      Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.

    • 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 MGSMQLKPME INPEMLNKVL AKLGVAGQWR FADVLGLEEE TLGSVPSPAC ALLLLFPLTA QHENFRKKQI EELKGQEVSP KVYFMKQTIG NSCGTIGLIH AVANNQDKLE FEDGSVLKQF LSETEKLSPE DRAKCFEKNE AIQAAHDSVA QEGQCRVDDK VNFHFILFNN VDGHLYELDG RMPFPVNHGA SSEDSLLQDA AKVCREFTER EQGEVRFSAV ALCKAA.

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    Uchl 1 Mouse
  • View Data Sheet

    Name :

    ICAM3 Human

    Description:

    Intercellular Adhesion Molecule-3 Human Recombinant

    ICAM3, Intercellular adhesion molecule 3, ICAM-3, CD50, CDW50, ICAM-R, intercellular adhesion molecule 3 isoform 1

    Product # :

    PRO-2637

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    Description

    ICAM3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 698 amino acids (30-485 a.a) and having a molecular mass of 76.7kDa.ICAM3 is fused to a 242 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The ICAM3 solution (0.25mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by the ability of the immobilized protein to support the adhesion of HL-60 human promyelocytic cells.  When cells are added to Human ICAM-3/CD50 coated plates, the ED50 range ≤4ug/ml.

    More Info

    • Introduction

      ICAM-3/CD50, or CD50 or Cluster of Differentiation 50 is a protein, part of the intercellular adhesion molecule superfamily. every ICAM peptides are type I transmembrane glycoproteins, bind to leukocyte adhesion LFA-1 & has 2-9 immunoglobulinlike C2-type domains. ICAM-3/CD50 can be found in every leukocyte and acts as a crucial ligand for LFA-1 in the start of the immune system response. ICAM-3/CD50 acts as an adhesion molecule and is also a potent signaling protein.

    • Synonyms

      ICAM3, Intercellular adhesion molecule 3, ICAM-3, CD50, CDW50, ICAM-R, intercellular adhesion molecule 3 isoform 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

      ADLQEFLLRV EPQNPVLSAG GSLFVNCSTD CPSSEKIALE TSLSKELVAS GMGWAAFNLS NVTGNSRILC SVYCNGSQIT GSSNITVYRL PERVELAPLP PWQPVGQNFT LRCQVEDGSP RTSLTVVLLR WEEELSRQPA VEEPAEVTAT VLASRDDHGA PFSCRTELDM QPQGLGLFVN TSAPRQLRTF VLPVTPPRLV APRFLEVETS WPVDCTLDGL FPASEAQVYL ALGDQMLNAT VMNHGDTLTA TATATARADQ EGAREIVCNV TLGGERREAR ENLTVFSFLG PIVNLSEPTA HEGSTVTVSC MAGARVQVTL DGVPAAAPGQ PAQLQLNATE SDDGRSFFCS ATLEVDGEFL HRNSSVQLRV LYGPKIDRAT CPQHLKWKDK TRHVLQCQAR GNPYPELRCL KEGSSREVPV GIPFFVNVTH NGTYQCQASS SRGKYTLVVV MDIEAGSSHV EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH

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    Icam3 Human
  • View Data Sheet

    Name :

    AFP Protein

    Description:

    Alpha Fetoprotein Human Recombinant

    Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.

    Product # :

    PRO-2229

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    Description

    AFP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 600 amino acids (19-609a.a.) and having a molecular mass of 67.5kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa). AFP is expressed with a ADP at N-terminus and 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.

    • Synonyms

      Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.

    • 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

      ADPRTLHRNEYGI ASILDSYQCT AEISLADLAT IFFAQFVQEA TYKEVSKMVK DALTAIEKPT GDEQSSGCLE NQLPAFLEEL CHEKEILEKY GHSDCCSQSE EGRHNCFLAH KKPTPASIPL FQVPEPVTSC EAYEEDRETF MNKFIYEIAR RHPFLYAPTI LLWAARYDKI IPSCCKAENA VECFQTKAAT VTKELRESSL LNQHACAVMK NFGTRTFQAI TVTKLSQKFT KVNFTEIQKL VLDVAHVHEH CCRGDVLDCL QDGEKIMSYI CSQQDTLSNK ITECCKLTTL ERGQCIIHAE NDEKPEGLSP NLNRFLGDRD FNQFSSGEKN IFLASFVHEY SRRHPQLAVS VILRVAKGYQ ELLEKCFQTE NPLECQDKGE EELQKYIQES QALAKRSCGL FQKLGEYYLQ NAFLVAYTKK APQLTSSELM AITRKMAATA ATCCQLSEDK LLACGEGAAD IIIGHLCIRH EMTPVNPGVG QCCTSSYANR RPCFSSLVVD ETYVPPAFSD DKFIFHKDLC QAQGVALQTM KQEFLINLVK QKPQITEEQL EAVIADFSGL LEKCCQGQEQ EVCFAEEGQK LISKTRAALG VHHHHHH.

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    Afp Human
  • View Data Sheet

    Name :

    ORM1

    Description:

    Orosomucoid 1 Human Recombinant

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

    Product # :

    PRO-889

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    Description

    ORM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (19-201) and having a molecular mass of 21.7 kDa.The ORM1 is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ORM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • 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

      MQIPLCANLV PVPITNATLD QITGKWFYIA SAFRNEEYNK SVQEIQATFF YFTPNKTEDT IFLREYQTRQ DQCIYNTTYL NVQRENGTIS RYVGGQEHFA HLLILRDTKT YMLAFDVNDE KNWGLSVYAD KPETTKEQLG EFYEALDCLR IPKSDVVYTD WKKDKCEPLE KQHEKERKQE EGES.

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    Orm1 Human
  • View Data Sheet

    Name :

    FABP1 Mouse, His

    Description:

    Fatty Acid Binding Protein-1, His Tag Mouse Recombinant

    Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein, Fatty acid-binding protein, liver.

    Product # :

    PRO-2512

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    Description

    FABP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 150 amino acids (1-127 a.a.) and having a molecular mass of 16.6 kDa. The FABP1 is fused to a 23 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FABP1 solution (0.25mg/ml) contains PBS (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.

    • Synonyms

      Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein, Fatty acid-binding protein, liver.

    • 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 MGSMNFSGKY QLQSQENFEP FMKAIGLPED LIQKGKDIKG VSEIVHEGKK IKLTITYGPK VVRNEFTLGE ECELETMTGE KVKAVVKLEG DNKMVTTFKG IKSVTELNGD TITNTMTLGD IVYKRVSKRI.

    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.

    Fabp 1 Mouse
  • View Data Sheet

    Name :

    CDK16 Human

    Description:

    Cyclin-dependent kinase 16 Human Recombinant

    Cyclin-Dependent Kinase 16, PCTK1, Serine/Threonine-Protein Kinase,  Serine/Threonine-Protein Kinase PCTAIRE-1, Cell Division Protein Kinase 16, PCTAIRE Protein Kinase 1, PCTAIRE, PCTGAIRE, EC 2.7.11.22, EC 2.7.11, PCTAIRE-Motif Protein Kinase 1, PCTAIRE1.

    Product # :

    PKA-324

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    Description

    CDK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (158-496aa) and having a molecular mass of 41.1kDa.CDK16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDK16 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDK16 is a member of the CDK family of serine/threonine protein kinases which are known to regulate the cell cycle. These proteins have a core kinase domain flanked by unique amino- and carboxy- terminal domains. CDK16, which is expressed mainly in mammalian brain, cooperates with an assortment of proteins, and is a part of a multiple signal transduction cascade.

    • Synonyms

      Cyclin-Dependent Kinase 16, PCTK1, Serine/Threonine-Protein Kinase, Serine/Threonine-Protein Kinase PCTAIRE-1, Cell Division Protein Kinase 16, PCTAIRE Protein Kinase 1, PCTAIRE, PCTGAIRE, EC 2.7.11.22, EC 2.7.11, PCTAIRE-Motif Protein Kinase 1, PCTAIRE1.

    • 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 MGSGFGKLET YIKLDKLGEG TYATVYKGKS KLTDNLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV TLHDIIHTEK SLTLVFEYLD KDLKQYLDDC GNIINMHNVK LFLFQLLRGL AYCHRQKVLH RDLKPQNLLI NERGELKLAD FGLARAKSIP TKTYSNEVVT LWYRPPDILL GSTDYSTQID MWGVGCIFYE MATGRPLFPG STVEEQLHFI FRILGTPTEE TWPGILSNEE FKTYNYPKYR AEALLSHAPR LDSDGADLLT KLLQFEGRNR ISAEDAMKHP FFLSLGERIH KLPDTTSIFA LKEIQLQKEA SLRSSSMPDS GRPAFRVVDT EF

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    Cdk16 Human
  • View Data Sheet

    Name :

    CYGB Human

    Description:

    Cytoglobin Human Recombinant

    HGB, STAP, Cytoglobin, CYGB.

    Product # :

    PRO-842

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    Description

    CYGB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190 a.a.) and having a molecular mass of 23.5kDa. The CYGB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CYGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytoglobin is a globin protein found in the brain and is mainly utilized in marine mammals. CYGB acts a a protector under conditions of hypoxia. The suggested function of CYGB is the modulation of oxygen and nitric oxide metabolism or scavenging free radicals within a cell.

    • Synonyms

      HGB, STAP, Cytoglobin, CYGB.

    • 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 MEKVPGEMEI ERRERSEELS EAERKAVQAM WARLYASCED VGVAILVRFF VNFPSAKQYF SQFKHMEDPL EMERSPQLRK HACRVMGALN TVVENLHDPD KVSSVLALVG KAHALKHKVE PVYFKILSGV ILEVVAEEFA SDFPPETQRA WAKLRGLIYS HVTAAYKEVG WVQQVPNATT PPATLPSSGP.

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    Cygb Human
  • View Data Sheet

    Name :

    CXCL16 Human

    Description:

    CXCL16 Human Recombinant

    Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.

    Product # :

    CHM-029

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    Description

    CXCL16 Human Recombinant (30-118 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids and having a molecular mass of 10kDa.The CXCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL16 protein was lyophilized from a 0.2µm filtered solution in PBS.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.

    More Info

    • Introduction

      CXC chemokine ligand 16 (CXCL16) is a type I membrane protein, which contains a non-ELR motif-containing CXC chemokine domain in its extracellular region. Human and Mouse CXCL16 share a 70% a.a. sequence similarity within their chemokine domains and 49% overall a.a. sequence identity. Functional CXCL16 can be dropped from the cell surface as an approximately 35kDa soluble protein. CXCR6 is the functional receptor for CXCL16. CXCL16 functions as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), proposing that CXCL16 may be involved in pathophysiology such as atherogenesis. In addition, CXCL16 induces a strong chemotactic response and calcium mobilization. CXCL16 binds to CXCR6/Bonzo.

    • Synonyms

      Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 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 CXCL16 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.

    • Background

      What is the molecular weight/Mw of CXCL16 HUMAN Protein?
      CXCL16 HUMAN Protein has a total Mw of 10kDa.

      What is the source or expression system of CXCL16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL16 HUMAN Protein?
      CXCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL16 HUMAN Protein?
      The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.

      What is the amino acid sequence of CXCL16 HUMAN Protein?
      NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.

      What applications can CXCL16 HUMAN Protein be used in?
      CXCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL16 HUMAN Protein?
      The endotoxin level is minimal, CXCL16 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.

    Cxcl16 Human
  • View Data Sheet

    Name :

    CKMB Human Active

    Description:

    Creatine Kinase MB Active Human Recombinant

    CKMB, CK-MB 

     

    Product # :

    CKI-200

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    Shipped at Room temp

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    • description
    • source
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    • More Info

    Description

    CKMB Human Recombinant produced in E. coli is a noncovalently-linked heterodimer consists of CK-M and CK-B each containing 381 amino acids and having a total molecular mass of 85.7kDa (43.10 kDa and 42.64 kDa respectively). CKMB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.

    Purity

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

    Biological Activity

    The specific activity ranges from 500-600 units/mg and was measured kinetically by the CK-NAC assay at 37°C.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      CKM
      MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
      CKB
      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.

    • Background

      CKMB is used in cardiovascular research as a biomarker for myocardial injury and to investigate the molecular mechanisms of cardiac muscle damage and repair.
      CKMB is also used in Immunoassay development, Aptamer screening, Biosensor validation and Point-of-care diagnostic assay development

      What is the molecular weight / Mw of CKMB Protein?
      CKMB Protein is a non covalently heterodimer having a total Mw of 85.7ka

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

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

      What is the Biological Activity of CKMB Protein?
      The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.


      What is the amino acid sequence of CKMB Protein?
      CKM
      MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
      CKB
      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K

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


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

    CKMB Human Active
  • View Data Sheet

    Name :

    TSFM Human

    Description:

    Ts Translation Elongation Factor Mitochondrial Human Recombinant

    Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.

    Product # :

    PRO-1971

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    Quantity :

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    • description
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    • purity
    • More Info

    Description

    TSFM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (46-346 a.a) and having a molecular mass of 32.9kDa.TSFM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TSFM is a mitochondrial translation elongation factor which is linked with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. TSFM stays bound to the aminoacyl-tRNA.EF-Tu.GTP complex until the GTP hydrolysis stage on the ribosome. Mutations in TSFM are related with combined oxidative phosphorylation deficiency-3 syndrome.

    • Synonyms

      Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.

    • 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

      MSKELLMKLR RKTGYSFVNC KKALETCGGD LKQAEIWLHK EAQKEGWSKA AKLQGRKTKE GLIGLLQEGN TTVLVEVNCE TDFVSRNLKF QLLVQQVALG TMMHCQTLKD QPSAYSKVQW LTPVNLALWE AEAGGSLEGF LNSSELSGLP AGPDREGSLK DQLALAIGKL GENMILKRAA WVKVPSGFYV GSYVHGAMQS PSLHKLVLGK YGALVICETS EQKTNLEDVG RRLGQHVVGM APLSVGSLDD EPGGEAETKM LSQPYLLDPS ITLGQYVQPQ GVSVVDFVRF ECGEGEEAAE TE.

    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.

    Tsfm Human
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