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Search results

1000 results found for “cytohesin”

Name

Description

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  • View Data Sheet

    Name :

    NME2 Human

    Description:

    Non-Metastatic Cells 2 Human Recombinant

    Nucleoside diphosphate kinase B, NDPK-B, NDPKB, NM23-H2, NM23B, EC 2.7.4.6, NDP kinase B, C-myc purine-binding transcription factor PUF, NDK B, NME2, puf, MGC111212.

    Product # :

    PKA-363

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    Quantity :

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    Description

    NME2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (1-152 a.a.) and having a molecular mass of 17.2kDa. The NME2 is purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The NME2 protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NME2 takes an important part in the synthesis of nucleoside triphosphates other than ATP. NME2 negatively controls Rho activity by interacting with AKAP13/LBC. NME2 acts as a transcriptional activator of the MYC gene. NME2 binds DNA non-specifically. NME2 is a heterodimeric enzyme functioning as a nucleoside diphosphate kinase. NME1 and NME2 contain 152 amino acids, A and B polypeptide chains of the NM23 enzyme, respectively. NME2 is identical to the beta subunit of human erythrocyte NDP kinase. NDP kinases participate in the synthesis of nucleoside triphosphates, and NM23 is involved in the regulation of signal transduction by complexing with G proteins, causing activation/inactivation of developmental pathways.

    • Synonyms

      Nucleoside diphosphate kinase B, NDPK-B, NDPKB, NM23-H2, NM23B, EC 2.7.4.6, NDP kinase B, C-myc purine-binding transcription factor PUF, NDK B, NME2, puf, MGC111212.

    • 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

      MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS DSVKSAEKEI SLWFKPEELV DYKSCAHDWV YE.

    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.

    Nme2 Human
  • View Data Sheet

    Name :

    BCL2L2 Human, His

    Description:

    BCL2 Like 2 Human Recombinant, His Tag

    B-Cell Lymphoma Protein 2, BCL2 Like 2, BCL2 Like protein 2, BCLW, Bcl2-L-2, Apoptosis regulator Bcl-W, BCL2L2, BCL-W, KIAA0271.

    Product # :

    PRO-768

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    Description

    BCL2L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-172 a.a.) and having a molecular weight of 20.9kDa.The BCL2L2 is fused to a 20 a.a His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCL2L2 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BCL2L2 promotes cell survival and blocks dexamethasone-induced apoptosis. BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. BCL2L2 is part of the BCL-2 protein family which form hetero- or homodimers and play an important role as anti and proapoptotic regulators. BCL2L2 causes reduced cell apoptosis under cytotoxic conditions. BCL2L2 is involved in the survival of NGF- and BDNF-dependent neurons. BCL2L2 plays an important role in adult spermatogenesis.

    • Synonyms

      B-Cell Lymphoma Protein 2, BCL2 Like 2, BCL2 Like protein 2, BCLW, Bcl2-L-2, Apoptosis regulator Bcl-W, BCL2L2, BCL-W, KIAA0271.

    • 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 MATPASAPDT RALVADFVGY KLRQKGYVCG AGPGEGPAAD PLHQAMRAAG DEFETRFRRT FSDLAAQLHV TPGSAQQRFT QVSDELFQGG PNWGRLVAFF VFGAALCAES VNKEMEPLVG QVQEWMVAYL ETRLADWIHS SGGWAEFTAL YGDGALEEAR RLREGNWASV RT.

    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.

    Bcl2L2 Human
  • View Data Sheet

    Name :

    Leptin qA Human, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Human Recombinant

    Product # :

    CYT-1251

    Price :

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    Description

    Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Human Qa Peg
  • View Data Sheet

    Name :

    Leptin tA Mouse, PEG

    Description:

    Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant

    Product # :

    CYT-566

    Price :

    Quantity :

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    Description

    Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
    Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Ta Mouse Peg
  • View Data Sheet

    Name :

    pGH 22kDa Human

    Description:

    Growth Hormone Placental 22kDa Human Recombinant

    GHL, GHV, GH-V, hGH-V, PGH.

    Product # :

    CYT-235

    Price :

    Quantity :

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    • Citations

    Description

    Placental HGH 22kDa Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 22367 Dalton. Predicted pI=7.80. Placental Growth Hormone has dimished lactogenic (prolactin receptor mediated) activity characteristic to pituitary GHs. GH Placental Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3 previously adjusted pH 8-9.

    Purity

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

    Citations

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GHL, GHV, GH-V, hGH-V, PGH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH placental although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization HGH placental can be stored at 4°C for up to 4 weeks. For long term storage and more diluted solutions 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 Placental HGH in 0.4% NaHCO3or water adjusted to pH 9, not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Phe-Pro-Thr-Ile.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.18 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GH-22K-placental as a Reference Standard.

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

    Placental Gh 22K Human
  • View Data Sheet

    Name :

    HCV NS3

    Description:

    Hepatitis C Virus NS3 (1450-1643 a.a.) Recombinant

    Product # :

    HCV-255

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    Description

    The E.coli derived 22kDa recombinant protein contains the HCV NS3 genotype 1b immunodominant regions, amino acids 1450-1643. The protein is fused with b-galactosidase (114 kDa) at N-terminus, pI 5.43.

    Formulation

    20mM Tris-HCl pH-8, 8M urea & 10mM B-ME.

    Purity

    HCV NS3 protein is >95% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

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

    • Stability

      HCV NS3 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV NS3 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV NS3 protein was purified by proprietary chromatographic technique.

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

    Hcv Ns3
  • View Data Sheet

    Name :

    GHK-Cu

    Description:

    GHK-Cu

    Copper Tripeptide-1

    Product # :

    HOR-063

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    Description

    GHK-Cu is a synthetic single, non-glycosylated polypeptide chain containing 3 amino acids, having a molecular mass of 401.91 Dalton and a Molecular formula of C14H22N6O4Cu.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Gly-His-Lys.

    • Background

      GHK-Cu is located in human plasma and has an ability to modify gene expression to a healthier state, influencing more than 4,000 human genes. GHK-Cu can change pathological gene expression to a healthy mode, mainly in chronic conditions as metastatic cancer, COPD and Ulcerative Colitis. GHK-Cu was discovered to be effective in systemic repair and neuroprotection.

      What is the molecular weight/Mw of GHK-CU Protein?
      GHK-CU Protein has a total Mw of 0.40kDa.

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

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

      What is the amino acid sequence of GHK-CU Protein?
      Gly-His-Lys.

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

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

      Who supplies GHK-CU that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of GHK-CU?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    GHK-Cu
  • View Data Sheet

    Name :

    METRN Mouse

    Description:

    Meteorin Mouse Recombinant

    Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

    Product # :

    PRO-2241

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    Description

    METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.

    • Synonyms

      Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

    • 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

      GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.

    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.

    Metrn Mouse
  • View Data Sheet

    Name :

    C-JUN Human (241 a.a.)

    Description:

    Jun Proto-Oncogene (1-241 a.a.) Human Recombinant

    Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.

    Product # :

    PKA-001

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    Description

    C-JUN 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 261 amino acids (1-241 a.a.) and having a molecular mass of 27.3kDa. The C-JUN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C-JUN solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.

    • Synonyms

      Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.

    • 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 MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP P.

    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.

    Cjun Human
  • View Data Sheet

    Name :

    SCGB1A1 Rat

    Description:

    Uteroglobin Rat Recombinant

    Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

    Product # :

    CYT-820

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    Description

    SCGB1A1 Rat Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains consisting of two 77 amino acids and having a molecular mass of 17.0kDa.

    Source

    Escherichia Coli.

    Formulation

    SCGB1A1 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. 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 5.0 ?g/ml, corresponding to a specific activity of >200IU/mg.

    Citations

    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 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SCGB1A1 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 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SSDICPGFLQ VLEALLLGSE SNYEAALKPF NPASDLQNAG TQLKRLVDTL PQETRINIVK LTEKILTSPL CEQDLRV

    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 Rat
  • View Data Sheet

    Name :

    HUS1 Human

    Description:

    HUS1 Checkpoint Homolog Human Recombinant

    HUS1 Checkpoint Homolog (S. pombe), Checkpoint Protein HUS1, Hus1+-like protein.

    Product # :

    PRO-039

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    Description

    HUS1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 300 amino acids (1-280a.a.) and having a molecular mass of 33.8kDa.HUS1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HUS1 protein solution (0.25mg/ml) is formulated in 20 mM Tris-HCl Buffer (pH 8.0), 100 mM NaCl and 40% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HUS1 is a component of an evolutionarily conserved, genotoxin-activated checkpoint complex. HUS1 protein connects with Rad9 and Rad1 to form the 9-1-1(RAD9-RAD1-HUS1) complex, that confines to DNA lesions and promotes DNA damage signaling and repair or apoptosis, cell cycle arrest. The trimeric complex is structurally similar to the proliferating cell nuclear antigen (PCNA) sliding clamp and interacts with Rad17 as a clamp-clamp loader pair during the DNA damage response.

    • Synonyms

      HUS1 Checkpoint Homolog (S. pombe), Checkpoint Protein HUS1, Hus1+-like protein.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKFRAKIVDG ACLNHFTRIS NMIAKLAKTC TLRISPDKLN FILCDKLANG GVSMWCELEQ ENFFNEFQME GVSAENNEIY LELTSENLSR ALKTAQNARA LKIKLTNKHF PCLTVSVELL SMSSSSRIVT HDIPIKVIPR KLWKDLQEPV VPDPDVSIYL PVLKTMKSVV EKMKNISNHL VIEANLDGEL NLKIETELVC VTTHFKDLGN PPLASESTHE DRNVEHMAEV HIDIRKLLQF LAGQQVNPTK ALCNIVNNKM VHFDLLHEDV SLQYFIPALS

    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.

    Hus1 Human
  • View Data Sheet

    Name :

    Sincalide

    Description:

    Sincalide

    Product # :

    HOR-274

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    Description

    Sincalide also called CCK-8 has a molecular formula of C49H62N10O16S3 , H-Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2 having an Mw of 1143.29 Dalton.

    Formulation

    The Sincalide was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

    Greater than 99.0% as determined by RP-HPLC.

    Citations

    More Info

    • Introduction

      Sincalide corresponds to the C-terminal octapeptide of cholecystokinin (CCK) which acts on receptors within the gallbladder wall causing it to contract.
      Cholecystokinin (CCK) is a hormone originally isolated from porcine intestinal mucosa and described as a linear 33-amino acid peptide containing a sulfated tyrosine, which is essential for its biological activity. It has been found in mammals in both the digestive tract and the central nervous system. Among its multiple biological functions, this hormone stimulates pancreatic exocrine secretion, gallbladder contraction, and intestine motility and may also act as a neurotransmitter/neuromodulator in the central nervous system.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Sincalide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCK-8 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 Sincalide in sterile 18MΩ-cm H2O at a concentration of 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Sincalide
  • View Data Sheet

    Name :

    IL12 Mouse

    Description:

    Interleukin-12 Mouse Recombinant

    NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    Product # :

    CYT-144

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    Description

    Interleukin-12 Mouse Recombinant produced in HEK 293 cells is a glycosylated disulfide linked heterodimeric polypeptide containing 506 amino acids and having a molecular weight of 75 kDa comprised of disulfide-bonded 35 kDa (p35) and 40 kDa (p40) subunits.The IL-12 is purified by proprietary chromatographic techniques.

    Source

    HEK-293 Cells.

    Formulation

    The protein was lyophilized from 0.5xPBS, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    IL-12 Mouse has full biological activity when compared to standards. The ED50 is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x105 units/mg.

    Citations

    More Info

    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.

    • Synonyms

      NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized mouse IL-12 although stable at room temperature for 3 weeks, should be stored below -18°C. Upon reconstitution IL12 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 murine IL12 in sterile distilled pyrogen free water at 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.

      p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
      WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.

    • Background

      What is the molecular weight/Mw of IL12 MOUSE Protein?
      IL12 MOUSE Protein has a total Mw of 75kDa.

      What is the source or expression system of IL12 MOUSE Protein?
      HEK-293 Cells.

      What is the Purity of IL12 MOUSE Protein?
      IL12 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12 MOUSE Protein?
      IL-12 Mouse has full biological activity when compared to standards. The ED50 is determined by the dose-dependent induces secretion of SEAP in HEK-Blue IL-12 cells is 2.302 ng/ml corresponding to a specific activity of 4.3x105 units/mg.

      What is the amino acid sequence of IL12 MOUSE Protein?
      p35 Subunit: RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV VTINRVMGYL SSA.
      p40 Subunit: MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS
      WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS.

      What applications can IL12 MOUSE Protein be used in?
      IL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12 MOUSE Protein?
      The endotoxin level is minimal, IL12 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL12 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il12 Mouse
  • View Data Sheet

    Name :

    ProMatrilysin

    Description:

    ProMatrix Metalloproteinase-7 Recombinant

    Product # :

    ENZ-272

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    • Citations

    Description

    Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

    Source

    Escherichia Coli.

    Formulation

    The protein contains the following additives 25mM Tris-HCl (pH 7.5),150mM NaCl, 5mM CaCl2, 0.01% Brij-35 and 0.02% NaN3.

    Purity

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

    Biological Activity

    The specific activity was found to be 1400 IU/mg.

    Citations

    More Info

    • Physical Appearance

      Sterile clear liquid 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.

    • Unit Definition

      One unit is defined as the digestion of 1 µg Azocoll/min at 37°C.

    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.

    Promatrilysin
  • View Data Sheet

    Name :

    Resistin Human

    Description:

    Resistin Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-456

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    Description

    Resistin Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 93 amino acids and having a total molecular weight of 19.7kDa.The Resistin Human Recombinant protein is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 0.1% Trifluoroacetic Acis (TFA).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
      Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppresses the ability to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • 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 reconstitute the lyophilized Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP

    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.

    Resistin Human
  • View Data Sheet

    Name :

    PNC-27

    Description:

    PNC-27

    Product # :

    HOR-038

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    Description

    PNC-27 Synthetic is a single, non-glycosylated polypeptide chain containing 32 amino acids, having a molecular mass of 4031.72 Dalton and a Molecular formula of C188H293N53O44S.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    HPLC, MS

    PNC-27 HPLC - Product image 1
    pnc-27 mass spec - Product image 2

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PNC-27 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PNC-27 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 PNC-27 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Pro-Pro-Leu-Ser-Gln-Glu-Thr-Phe-Ser-Asp-Leu-Trp-Lys-Leu-Leu-Lys-Lys-Trp-Lys-Met-Arg-Arg-Asn-Gln-Phe-Trp-Val-Lys-Val-Gln-Arg-Gly-OH

    • Background

      PNC-27, a promising anticancer peptide, has gained attention due to its selective cytotoxicity against cancer cells without harming normal cells. This paper aims to elucidate the biochemical characteristics of PNC-27 and explore its potential therapeutic applications in the field of oncology.

      PNC-27, a novel anticancer peptide, holds great promise in the treatment of cancer due to its unique mechanism of action and selective cytotoxicity towards cancer cells (Goldberg et al., 2010). This paper seeks to delve into the biochemical attributes of PNC-27 and its therapeutic potential in cancer treatment.

      Derived from the p53 tumor-suppressor protein, PNC-27 exhibits a unique binding affinity for the MDM-2 protein found in the membranes of cancer cells. This binding triggers membrane pore formation, leading to cell lysis and death, leaving normal cells unaffected (Goldberg et al., 2010).

      Preclinical studies have highlighted the potential of PNC-27 in treating various types of cancers. Its ability to induce cell death in cancer cells without harming normal cells presents a promising direction for cancer therapeutics. For instance, studies have shown PNC-27 to be effective against lung and breast cancers (Hoshino et al., 2011; Sarafraz-Yazdi et al., 2010).

      The promising potential of PNC-27 warrants further exploration in clinical trials to evaluate its efficacy and safety in humans. Furthermore, investigation into its synergistic effects with other cancer treatments could provide a more holistic approach to cancer therapeutics. In conclusion, PNC-27 presents an exciting avenue for cancer research, offering a novel and targeted approach to cancer treatment.

    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.

    Pnc 27
  • View Data Sheet

    Name :

    HCV Core NS3

    Description:

    Hepatitis C Virus Nucleocapsid (core) NS3 Recombinant

    Product # :

    HCV-008

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    Description

    Recombinant HCV protein produced in E.Coli containing the Core (130 a.a.) and NS3 (236 a.a.) excluding NS4 and NS5 domains having a total Mw of 45kDa and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered solution containing PBS, 1M urea and 25mM Arginine.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

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    Hcv Core Ns3
  • View Data Sheet

    Name :

    HCV NS4 a+b, Fluoroscein

    Description:

    Hepatitis C Virus NS4 a+b. Fluoroscein Recombinant

    Product # :

    HCV-268

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    Description

    The E.coli derived 19 kDa recombinant protein Fluoroscien labeled contains the HCV NS4 immunodominant regions, amino acids 1658-1863. The protein is fused with b-galactosidase (114 kDa) at N-terminus.

    Formulation

    20mM Tris-Hcl pH 8, 8M urea & 10mM B-ME.

    Purity

    HCV NS4 a+b Fluoroscein protein is >95% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

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

    • Stability

      HCV NS4 a+b Fluoroscein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV NS4 a+b Fluoroscein antigen in ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV NS4 a+b Fluoroscein protein was purified by proprietary chromatographic technique.

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

    Hcv Ns4 Ab Fluoroscein
  • View Data Sheet

    Name :

    AHSG Mouse

    Description:

    Alpha-2-HS-Glycoprotein Mouse Recombinant

    Alpha-2-HS-glycoprotein, Countertrypin, Fetuin-A.

    Product # :

    PRO-2220

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    Description

    AHSG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 333 amino acids (19-345.a.) and having a molecular mass of 36.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). AHSG is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.

    • Synonyms

      Alpha-2-HS-glycoprotein, Countertrypin, Fetuin-A.

    • 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

      APQGTGLGFR ELACDDPEAE QVALLAVDYL NNHLLQGFKQ VLNQIDKVKV WSRRPFGVVY EMEVDTLETT CHALDPTPLA NCSVRQLTEH AVEGDCDFHI LKQDGQFRVM HTQCHSTPDS AEDVRKLCPR CPLLTPFNDT NVVHTVNTAL AAFNTQNNGT YFKLVEISRA QNVPLPVSTL VEFVIAATDC TAKEVTDPAK CNLLAEKQHG FCKANLMHNL GGEEVSVACK LFQTQPQPAN ANAVGPVPTA NAALPADPPA SVVVGPVVVP RGLSDHRTYH DLRHAFSPVA SVESASGETL HSPKVGQPGA AGPVSPMCPG RIRHFKIHHH HHH.

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

    Ahsg Mouse Sf9
  • View Data Sheet

    Name :

    ALDH3A1 Human

    Description:

    Aldehyde Dehydrogenase 3 Family Member A1 Human Recombinant

    Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.

    Product # :

    ENZ-479

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    Description

    ALDH3A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 473 amino acids (1-453 a.a.) and having a molecular mass of 52.5 kDa. ALDH3A1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ALDH3A1 solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity was found to be < 1 units/ml. Activity was obtained by measuring the increase of NADP in absorbance at 340 nm resulting from the reduction of NAD. 1 unit will oxidize 1umole of acetaldehyde to acetic acid per minute at pH 8 at 25°C in the presence of beta-NAD, potassium and thiols.

    Citations

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    • Introduction

      ALDH3A1 is involved in the detoxification of alcohol-derived acetaldehyde. ALDH3A1 participates in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. ALDH3A1 oxidizes aromatic aldehyde substrates and toxic aldehydes. ALDH3A1 forms a cytoplasmic homodimer that oxidizes aromatic and medium-chain saturated and unsaturated aldehyde substrates. ALDH3A1 promotes resistance to UV and 4-hydroxy-2-nonenal-induced oxidative damage in the cornea.

    • Synonyms

      Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.

    • 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 MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA DLHKNEWNAY YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI HSEPLGVVLV IGTWNYPFNL TIQPMVGAIA AGNAVVLKPS ELSENMASLL ATIIPQYLDK DLYPVINGGV PETTELLKER FDHILYTGST GVGKIIMTAA AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS GQTCVAPDYI LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVLPIVCVRSLEE AIQFINQREK PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL PFGGVGNSGM GSYHGKKSFE TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM TQH.

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    Aldh3A1 Human
  • View Data Sheet

    Name :

    HK1 Human

    Description:

    Hexokinase-1 Human Recombinant

    Hexokinase-1, EC 2.7.1.1, Hexokinase type I, HK I, Brain form hexokinase, HK1-ta, HK1-tb, HXK1, HK1.

    Product # :

    PKA-226

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    Description

    HK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain fused to a 20 amino acids His tag at the N-terminal encoding the sequence of 937 amino acids and having a molecular mass of 104.6 kDa. HXK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >2 units/ml obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. In the coupled mode, one unit will produce 1.0 umole of NADPH per minute as glucose is phosphorylated by ATP at pH 7.4 at 25C.

    Citations

    More Info

    • Introduction

      Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase1 encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of HXK1 results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein.

    • Synonyms

      Hexokinase-1, EC 2.7.1.1, Hexokinase type I, HK I, Brain form hexokinase, HK1-ta, HK1-tb, HXK1, HK1.

    • 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). Please avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH GSGSQLFDHV AECLGDFMEK RKIKDKKLPV GFTFSFPCQQ SKIDEAILIT WTKRFKASGV EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT KDMLLEVKKR MRAEMELGLR KQTHNNAVVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF TFSFPCQQTS LDAGILITWT KGFKATDCVG HDVVTLLRDA IKRREEFDLD VVAVVNDTVG TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD IRTHYDRLVD EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISETLKTRG IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG AALITAVGVR LRTEASS.

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    Hk1 Human
  • View Data Sheet

    Name :

    HK2 Human

    Description:

    Hexokinase-2 Human Recombinant

    Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.

    Product # :

    PKA-227

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    Description

    HK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-917) fused to a 20 His tag at the N-terminal encoding the sequence of 937 amino acids in total and having a molecular mass of 104.1 kDa.HXK2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl pH8.0 and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 3-4 units/ml obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. In the coupled mode, one unit will produce 1.0 umole of NADPH per minute as glucose is phosphorylated by ATP at pH 7.4 at 30C.

    Citations

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    • Introduction

      Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.

    • Synonyms

      Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.

    • 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). Please avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL GFTFSFPCHQTKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDISDIEGEKDGIR KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKENKGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG KGAAMVTAVAYRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS KETHASAPVK MLPTYVCATPDGTEKGDFLA LDLGGTNFRV LLVRVRNGKW GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG AALITAVACR IREAGQR.

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    Hk2 Human
  • View Data Sheet

    Name :

    MYL6 Human

    Description:

    Myosin Light Chain 6 Human Recombinant

    Myosin light polypeptide 6, 17 kDa myosin light chain, LC17, Myosin light chain 3, MLC-3, Myosin light chain alkali 3, Myosin light chain A3, Smooth muscle and nonmuscle myosin light chain alkali 6, MYL6, ESMLC, LC17A, LC17B, MLC1SM, MLC3NM, MLC3SM, LC17-GI, LC17-NM.

    Product # :

    PRO-171

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    Quantity :

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    • description
    • source
    • formulation
    • purity
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    • Citations

    Description

    MYL6 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 171 amino acids (1-151 a.a.) and having a molecular mass of 19.1kDa. The MYL6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MYL6 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Myosin light polypeptide 6 (MYL6) is a hexameric ATPase cellular motor protein. MYL6 is composed of 2 heavy chains, 2 nonphosphorylatable alkali light chains, and 2o phosphorylatable regulatory light chains. MYL6 is a myosin alkali light chain which is expressed in smooth muscle and non-muscle tissues. MYL6 partakes in generating the force for cellular movements, thus having an imperative role in overall cellular function.

    • Synonyms

      Myosin light polypeptide 6, 17 kDa myosin light chain, LC17, Myosin light chain 3, MLC-3, Myosin light chain alkali 3, Myosin light chain A3, Smooth muscle and nonmuscle myosin light chain alkali 6, MYL6, ESMLC, LC17A, LC17B, MLC1SM, MLC3NM, MLC3SM, LC17-GI, LC17-NM.

    • 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 MCDFTEDQTA EFKEAFQLFD RTGDGKILYS QCGDVMRALG QNPTNAEVLK VLGNPKSDEM NVKVLDFEHF LPMLQTVAKN KDQGTYEDYV EGLRVFDKEG NGTVMGAEIR HVLVTLGEKM TEEEVEMLVA GHEDSNGCIN YEELVRMVLN G.

    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.

    Myl6 Human
  • View Data Sheet

    Name :

    MYL9 Human

    Description:

    Myosin Light Chain 9 Human Recombinant

    Myosin regulatory light polypeptide 9, 20 kDa myosin light chain, LC20, MLC-2C, Myosin RLC, Myosin regulatory light chain 2, smooth muscle isoform, Myosin regulatory light chain 9, Myosin regulatory light chain MRLC1, MYL9, MLC2, MRLC1, MYRL2, MGC3505.

    Product # :

    PRO-107

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    • description
    • source
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    Description

    MYL9 Human Recombinant fused with a20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing192 amino acids (1-172 a.a.) and having a molecular mass of 21.9kDa. The MYL9 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MYL9 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MYL9 is one of the numerous regulatory myosin light chains. Myosin which is a structural component of the muscle consists of 2 heavy chains and 4 light chains. MYL9 is a myosin light chain regulates muscle contraction by modulating the ATPase activity of myosin heads. MYL9 binds calcium and is activated by myosin light chain kinase. Regulatory myosin light chains regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of regulatory myosin light chains is catalyzed by MLCK in the presence of calcium and calmodulin and it increases the actin-activated myosin ATPase activity, thus regulates the contractile activity.

    • Synonyms

      Myosin regulatory light polypeptide 9, 20 kDa myosin light chain, LC20, MLC-2C, Myosin RLC, Myosin regulatory light chain 2, smooth muscle isoform, Myosin regulatory light chain 9, Myosin regulatory light chain MRLC1, MYL9, MLC2, MRLC1, MYRL2, MGC3505.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS LGKNPTDEYL EGMMSEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE DHLRELLTTM GDRFTDEEVD EMYREAPIDK KGNFNYVEFT RILKHGAKDK DD.

    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.

    Myl9 Human
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