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Search results

1000 results found for “NPM”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    NT 3 Mouse

    Description:

    Neurotrophin-3 Mouse Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

    Product # :

    CYT-688

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Neurotrophin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids and having a molecular mass of 13.6kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.02% TFA.

    Purity

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

    Biological Activity

    The activity, as determined by the dose-dependent proliferation of BaF3 cells transfected with the TrkB receptor, is typically in the range of 1-10 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      YAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

    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.

    Neurotrophin 3 Mouse
  • View Data Sheet

    Name :

    NT 4 Human

    Description:

    Neurotrophin-4 Human Recombinant

    NT4, NT5, NTF5, NT-4/5, NTF4, Neurotrophin-4, Neutrophic factor 4, Neurotrophin-5, NT-5.

    Product # :

    CYT-626

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • purity
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    • More Info

    Description

    Neurotrophin-4 Human Recombinant produced in E.Coli is a noncovalently linked homodimer, non-glycosylated polypeptide chain containing 2 x 130 amino acids (81-210 amino acids) and having a total molecular mass of 28 kDa. The NT-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer pH-7.4 and 150mM NaCl.

    Purity

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

    Biological Activity

    Determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures was found to be in the range of 20-50 ng/ml.

    More Info

    • Introduction

      NT-4 is part of the family of neurotrophic factors, neurotrophins, that are in charge for the survival and differentiation of mammalian neurons. NT-4 expression is dominant and less influenced by environmental signals. NT-4 deficient mice shows slight cellular deficits and develop normally to adulthood. NT-4 is a target-derived survival factor for peripheral sensory sympathetic neurons.NT-4 is involved in the proliferation and differentiation of periodontal ligament cells.

    • Synonyms

      NT4, NT5, NTF5, NT-4/5, NTF4, Neurotrophin-4, Neutrophic factor 4, Neurotrophin-5, NT-5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NT-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NT-4 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 NT-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GVSETAPASR RGELAVCDAV SGWVTDRRTA VDLRGREVEV LGEVPAAGGS PLRQYFFETR CKADNAEEGG PGAGGGGCRG VDRRHWVSEC KAKQSYVRAL TADAQGRVGW RWIRIDTACV CTLLSRTGRA.

    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.

    Nt 4 Human
  • View Data Sheet

    Name :

    HCV NS3

    Description:

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

    Product # :

    HCV-255

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • formulation
    • purity
    • More Info

    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).

    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 :

    Zika Envelope N

    Description:

    Zika Envelope N-Terminal Recombinant

    Product # :

    ZKV-009

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
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    • More Info

    Description

    Zika Envelope N protein is a peptide partially derived from zika envelope N terminal containing 270 amino acids, having an Mw of 30kDa and the Isoelectric point is 6.37. The Zika Envelope N protein is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Zika Envelope N protein solution contains PBS with 0.05% NaN3.

    Purity

    Zika Envelope N protein is >95% pure as determined by SDS-PAGE.

    More Info

    • Introduction

      Zika virus (ZIKV) belongs to the family Flaviviridae and the genus Flavivirus, it is transmitted by daytime-active Aedes mosquitoes, such as A. aegypti and A. albopictus. The Zika virus is related to the dengue, yellow fever, Japanese encephalitis, and West Nile viruses. Much like the other flaviviruses, Zika virus is enveloped and icosahedral and has a nonsegmented, single-stranded, positive-sense RNA genome. Zika fever is an infection, which often causes no symptoms or only mild ones, like a mild form of dengue fever, and it is treated by rest. As of February 2016, there has been mounting evidence that Zika fever in pregnant women can cause abnormal brain development in their fetuses by mother-to-child transmission, which may result in miscarriage or microcephaly, however it is not yet known whether Zika virus causes microcephaly. Furthermore, a connection has been established with neurologic conditions in infected adults, including Guillain–Barre syndrome. Since the 1950s, Zika virus has been detected only within a narrow equatorial belt from Africa to Asia. Between the years 2013 and 2014, Zika virus has spread eastward across the Pacific Ocean to French Polynesia, New Caledonia, the Cook Islands, and Easter Island, and in 2015 to Mexico, Central America, the Caribbean, and South America, where the Zika outbreak has reached pandemic levels.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      Zika Envelope N protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Each laboratory should determine an optimum working titer for use in its particular application.

    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.

    Zika Envelope N
  • View Data Sheet

    Name :

    HCV NS5 Genotype-2

    Description:

    Hepatitis C Virus NS5 Genotype-2 Recombinant

    Product # :

    HCV-229

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • formulation
    • purity
    • More Info

    Description

    The E.coli derived recombinant protein contains the HCV NS5 Genotype2 immunodominant regions.

    Formulation

    25mM Tris and 1mM EDTA, 1.5M urea & 50% glycerol.

    Purity

    HCV NS5 Genotype-2 protein is >95% pure as determined by 10% PAGE (coomassie staining).

    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 clear solution.

    • Stability

      HCV NS5 Genotype-2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV NS5 Genotype-2 antigen is syuitable 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 NS5 Genotype-2 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 Ns5 Genotype 2
  • View Data Sheet

    Name :

    CMV Pp38

    Description:

    Cytomegalo Virus Pp38 (UL80a) Recombinant

    Product # :

    CMV-213

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    Description

    The E.Coli derived 52.8kDa recombinant protein contains the CMV Pp38 (UL80a) immunodominant regions, 117-373 amino acids and fused to a GST-Tag at C-terminus.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml in 50mM Tris pH-7.2, 1mM EDTA and 50% glycerol.

    Purity

    CMV Pp38 protein is >95% pure as determined by 10% PAGE (coomassie staining).

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    • Introduction

      CMV belongs to the Betaherpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.

    • Stability

      CMV Pp38 Protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Purification Method

      CMV Pp38 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.

    Cmv Pp38
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    Name :

    CMV Pp52

    Description:

    Cytomegalo Virus Pp52 (UL44) Recombinant

    Product # :

    CMV-214

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    Description

    The E.coli derived 51 kDa recombinant protein contains the CMV Pp52 (UL44) immunodominant regions, 202-434 amino acids. Recombinant CMV-Pp52 is fused to a 26 kDa GST tag.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris pH 7.2, 1mM EDTA and 50% glycerol.

    Purity

    CMV Pp52 protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      CMV belongs to the Betaherpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.

    • Stability

      CMV Pp52 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      CMV Pp52 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of CMV-infected individuals.

    • Purification Method

      CMV Pp52 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.

    Cmv Pp52
  • View Data Sheet

    Name :

    NCR3LG1 Human

    Description:

    Natural Cytotoxicity Triggering Receptor 3 Ligand 1 Human Recombinant

    B7H6, B7-H6, B7 Homolog 6

    Product # :

    PRO-2762

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    Description

    NCR3LG1 Human Recombinant produced in HEK is a single, glycosylated polypeptide chain containing 477 amino acids (25-262 a.a) and having a molecular mass of 53.6 kDa. NCR3LG1 is fused to a 239 amino acid hIgG-His tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells

    Formulation

    NCR3LG1 protein solution (0.5mg/ml) containing 1X PBS (pH-7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Measured in a functional ELISA with Human NCR3. The ED50 range ≤500 ng/ml.

    More Info

    • Introduction

      The B7 proteins are crucial in the regulation of the adaptive immune system. Among them is NCR3LG1. NCR3LG1 is part of the B7 family and is expressed on tumor cells. NCR3LG1 Interaction with NKp30 protein results in cytotoxicity and natural killer cell activation.Humans and rats have a single NCR3LG1 gene; though, numerous B7H6 genes were detected in a single large cluster in the Xenopus genome. NCR3LG1, a ligand for the NK cell activating receptor NKp30, targest to produce CAR that targets multiple tumor types. NCR3LG1 is expressed on many primary human tumors, including leukemia, lymphoma and gastrointestinal stromal tumors, though it is not constitutively expressed on normal tissues.

    • Synonyms

      B7H6, B7-H6, B7 Homolog 6

    • 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

      DLKVEMMAGG TQITPLNDNV TIFCNIFYSQ PLNITSMGIT WFWKSLTFDK EVKVFEFFGD HQEAFRPGAI VSPWRLKSGD ASLRLPGIQL EEAGEYRCEV VVTPLKAQGT VQLEVVASPA SRLLLDQVGM KENEDKYMCE SSGFYPEAIN ITWEKQTQKF PHPIEISEDV ITGPTIKNMD GTFNVTSCLK LNSSQEDPGT VYQCVVRHAS LHTPLRSNFT LTAARHSLSE TEKTDNFS

      LE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH

    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.

    Ncr3Lg1 Human
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    Name :

    TNF a Rabbit

    Description:

    Tumor Necrosis Factor-Alpha Rabbit Recombinant

    Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2. 

    Product # :

    CYT-008

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    Description

    Tumor Necrosis Factor-a Rabbit Recombinant consists of three identical polypeptide chains of 158 amino acids combined to form a compact, bell-shaped homotrimer. TNF-alpha was produced in E.Coli is a non-glycosylated, polypeptide chain having a molecular mass of 17.4 kDa for the individual subunit. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF-alpha Rabbit was lyophilized after extensive dialysis against 20mM PB, pH7.4, 300mM NaCl.

    Purity

    Greater than 95% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is less than 0.03ng/ml, corresponding to a Specific Activity of 30,000,000 IU/mg.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha 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 Met-Ser-Ala-Ser-Arg.

    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.

    Tnf A Rabbit
  • View Data Sheet

    Name :

    PTH (1-84) N15 Human

    Description:

    Parathyroid Hormone (1-84) N15 Labeled Human Recombinant

    Parathyrin, PTH, Parathormone.

    Product # :

    HOR-002

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    Description

    PTH (1-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 84 amino acids and having a molecular mass of 9550 Dalton labeled by the stable isotope N15.The PTH (1-84) N15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTH (1-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 9,000 Units/mg.

    More Info

    • Introduction

      Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
      In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
      In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
      Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures.

    • Synonyms

      Parathyrin, PTH, Parathormone.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ.

    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.

    Pth 1 84 N15 Human
  • View Data Sheet

    Name :

    PTH (7-84) N15 Human

    Description:

    Parathyroid Hormone (7-84) N15 Labeled Human Recombinant

    Parathyrin, PTH, Parathormone.

    Product # :

    HOR-013

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    Description

    PTH (7-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8900 Dalton labeled by the stable isotope N15.The PTH (7-84) N15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTH (7-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.

    • Synonyms

      Parathyrin, PTH, Parathormone.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PTH (7-84) N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH (7-84) N15 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 PTH (7-84) N15 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ

    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.

    Pth 7 84 N15 Human
  • View Data Sheet

    Name :

    TXN1 E.Coli

    Description:

    Thioredoxin E.Coli Recombinant

    Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    Product # :

    PRO-334

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    Description

    Recombinant Thioredoxin was purified from E. coli harboring its gene.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 20mM phosphate buffer pH 7.4.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    TRX activity is assayed by measuring the change in absorbance at 650 nm at 25°C using 0.13µM bovine insulin containing 0.33mM DTT (pH 6.5).
    The specific activity was found to be 3IU/mg.

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    • Introduction

      Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase.Its Molecular Weight is 11.9kDa. and the pI is 4.67.

    • Synonyms

      Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    • Physical Appearance

      Sterile Lyophilized Powder.

    • Stability

      TRX although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TRX in sterile 18MΩ-cm H2O.

    • Amino Acid Sequence

      HMSDKIIHL TDDSFDTDVLKADGAIL VDFW AEWCGPCKMIAPILDEI GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGAL DANLA.

    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.

    Thioredoxin 1
  • View Data Sheet

    Name :

    NAT6 Human

    Description:

    N-Acetyltransferase 6 Human Recombinant

    Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.

    Product # :

    ENZ-410

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    Description

    Recombinant Human NAT6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-308 a.a.) and having a molecular mass of 35.9 kDa. NAT6 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The NAT6 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.

    • Synonyms

      Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQELTLSPGP AKLTPTLDPT HRMELILSTS PAELTLDPAC QPKLPLDSTC QPEMTFNPGP TELTLDPEHQ PEETPAPSLA ELTLEPVHRR PELLDACADL INDQWPRSRT SRLHSLGQSS DAFPLCLMLL SPHPTLEAAP VVVGHARLSR VLNQPQSLLV ETVVVARALR GRGFGRRLME GLEVFARARG FRKLHLTTHD QVHFYTHLGY QLGEPVQGLV FTSRRLPATL LNAFPTAPSP RPPRKAPNLT AQAAPRGPKG PPLPPPPPLP ECLTISPPVP SGPPSKSLLE TQYQNVRGRP IFWMEKDI.

    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.

    Nat6 Human
  • View Data Sheet

    Name :

    MGMT Human

    Description:

    O-6-Methylguanine-DNA Methyltransferase Human Recombinant

    Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, MGMT.

    Product # :

    ENZ-389

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    Description

    MGMT Human Recombinant fused to a 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 227 amino acids (1-207) and having a molecular mass of 23.8 kDa. The MGMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MGMT solution contains 20mM Tris-HCl pH-7.5, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MGMT is an enzyme that repairs O-6-methylguanine, a mutagenic DNA base damaged by endogenous and environmental alkylating agents and takes part in the cellular defense against the biological effects of O-6-methylguanine in DNA. MGMT repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. abnormal MGMT expression correlates with the prognosis in human solid cancers. MGMT decrease of expression is correlated with methylation. The human MGMT is a negative regulator of estrogen receptor-mediated transcription upon alkylation DNA damage. MGMT promoter hypermethylation plays an important role in the early steps of colorectal carcinogenesis. Abnormal promoter hypermethylation of MGMT gene is associated with oral squamous cell carcinomas.

    • Synonyms

      Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, MGMT.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDKDCEMKRT TLDSPLGKLE LSGCEQGLHE IKLLGKGTSA ADAVEVPAPA AVLGGPEPLM QCTAWLNAYF HQPEAIEEFP VPAFHHPVFQ QESFTRQVLW KLLKVVKFGE VISYQQLAAL AGNPKAARAV GGAMRGNPVP ILIPCHRVVC SSGAVGNYSG GLAVKEWLLA HEGHRLGKPG LGGSSGLAGA WLKGAGATSG SPPAGRN.

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    Name :

    ARTN Human

    Description:

    Artemin Human Recombinant

    ART, ARTN , EVN, NBN.

    Product # :

    CYT-306

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    Description

    Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

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    • Introduction

      The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.

    • Synonyms

      ART, ARTN , EVN, NBN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

    • Background

      Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications

      Abstract:

      Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.

      Introduction:

      Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.

      Artemin Signaling and Mechanisms:

      Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.

      Artemin in Neurological Disorders:

      Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.

      Therapeutic Potential of Artemin Human Recombinant:

      Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.

      Challenges and Future Directions:

      While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.

      Conclusion:

      Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.

      What is the molecular weight/Mw of ARTN Protein?
      ARTN Protein has a total Mw of 24.2kDa.

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

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

      What is the Biological Activity of ARTN Protein?
      The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

      What is the amino acid sequence of ARTN Protein?
      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

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

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

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    Artemin Human
  • View Data Sheet

    Name :

    MMP12 Human (1-33)

    Description:

    Matrix Metalloproteinase 12 (1-33 a.a.) Human Recombinant

    Product # :

    ENZ-1201

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    Description

    The MMP12 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MMP12 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 33 amino acid residues of the MMP12 Human, 1-33 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized MMP12 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Amino Acid Sequence

      MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFG.

    • Background

      Matrix Metalloproteinase 12 also known as MMP12 is 1 of the main enzymes in the MMP family which is primarily produced by macrophages and neutrophils. MMP12 is implicated in the breakdown of elastin and in the development of chronic inflammatory diseases, such as emphysema, COPD and atherosclerosis. MMP12 is upregulated and contributes to tissue remodeling in inflammatory responses which is essential for wound healing and immune defense. MMP12 catalyzes the cleavage of collagen, elastin and other ECM components. Its activity is regulated in normal tissues to avoid pathological degradation.

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    Mmp12 Enzyme
  • View Data Sheet

    Name :

    SARS Nucleocapsid, 1-49 a.a.

    Description:

    SARS-Associated Coronavirus Nuclecapsid (1-49 a.a.), Recombinant

    Product # :

    SARS-005

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    Description

    The E.coli derived recombinant protein contains the Nucleocapsid protein 1-49 amino acids immunodominant regions.

    Source

    Escherichia Coli.

    Formulation

    SARS Nucleocaspid protein solution is supplied in PBS.

    Purity

    Protein is >90% pure as determined SDS-PAGE.

    More Info

    • Introduction

      The SARS Nucleocaspid is a protein that has a crucial structural importance, by making the virions associates with the RNA genome and therefore create a nucleocapsid that has the specific helical form. There has been found 3 different domain structures to the nucleocapsid antigen. This protein contains 3 outer structural proteins, the membrane (M), envelope (E), and spike (S) proteins.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Protein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Specificity

      Immunoreactive with sera of SARS-infected individuals.

    • Purification Method

      Purified by proprietary chromatographic technique.

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  • View Data Sheet

    Name :

    UBE2M Human

    Description:

    Ubiquitin Conjugating Enzyme E2M Human Recombinant

    NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.

    Product # :

    ENZ-345

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    Description

    UBE2M Human Recombinant produced E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.5kDa.UBE2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2M solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      UbcH12 is functional in in vitro NEDDylation reactions. It has been shown to form a thioester linkage with NEDD8 in the presence of the NEDD8 activating enzyme complex Uba3/APP-BP1. APP-BP1 binds to the amyloid precursor protein (APP) carboxy terminal domain and is important in conjunction with Uba3 and UbcH12 in driving cells through the S to M checkpoint. It was demonstrated to be the E2 responsible for the NEDDylation of the Cul-1 component of the SCF (?-TRCP) complex which is important as the E3-ligase in the ubiquitinylation of I?B?. NEDDylation of Cul-1 is essential for conjugation and processing of NF-?B p105 by SCF (?-TRCP) following phosphorylation of the complex. A dominant negative form of UbcH12, previously demonstrated to sequester NEDD8 and inhibit its conjugation, inhibits both conjugation and processing of p105, which is alleviated by wild-type UbcH12.

    • Synonyms

      NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.

    • 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 MGSHMIKLFS LKQQKKEEES AGGTKGSSKK ASAAQLRIQK DINELNLPKT CDISFSDPDD LLNFKLVICP DEGFYKSGKF VFSFKVGQGY PHDPPKVKCE TMVYHPNIDL EGNVCLNILR EDWKPVLTIN SIIYGLQYLF LEPNPEDPLN KEAAEVLQNN RRLFEQNVQR SMRGGYIGST YFERCLK

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    Ube2M Human
  • View Data Sheet

    Name :

    MBP Human

    Description:

    Myelin Basic Protein Human Recombinant

    Myelin basic protein, MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein.

    Product # :

    PRO-1713

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    Description

    MBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197) and having a molecular mass of 23.9kDa.MBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MBP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MBP is a major component of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system, although, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs emerge from the long MBP gene which holds three additional exons located upstream of the classic MBP exons. The Golli mRNAs contain three exons unique to Golli-MBP, spliced in-frame to one or more MBP exons. The second family of transcripts contains only MBP exons and produces the well characterized myelin basic proteins. MBP transcription unit is an essential part of the Golli transcription unit and the arrangement is important for the function and/or regulation of these genes.

    • Synonyms

      Myelin basic protein, MBP, Myelin A1 protein, Myelin membrane encephalitogenic 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. 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 MGSMGNHAGK RELNAEKAST NSETNRGESE KKRNLGELSR TTSEDNEVFG EADANQNNGT SSQDTAVTDS KRTADPKNAW QDAHPADPGS RPHLIRLFSR DAPGREDNTF KDRPSESDEL QTIQEDSAAT SESLDVMASQ KRPSQRHGSK YLATASTMDH ARHGFLPRHR DTGILDSIGR FFGGDRGAPK RGSGKVSSEE

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    Mbp Protein
  • View Data Sheet

    Name :

    MUTM E.Coli

    Description:

    Formamidopyrimidine-DNA Glycosylase E.Coli Recombinant

    Formamidopyrimidine-DNA glycosylase, FPG.

    Product # :

    ENZ-589

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    Description

    MUTM Recombinant produced in E. coli is a single polypeptide chain containing 289 amino acids (1-269) and having a molecular mass of 32.4kDa.MUTM is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MUTM solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MUTM is a base excision repair enzyme that identifies and eliminates a large variety of oxidized purines from correspondingly impaired DNA. MUTM is nondismissable and essential to remove quickly its substrate lesions on the chromosome. MUTM, additionally, mends a large number of the lesions recognized by Endo III, signifying that MUTM takes a prominent part in the overall repair of both purine damage and pyrimidine damage in vivo.

    • Synonyms

      Formamidopyrimidine-DNA glycosylase, FPG.

    • 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 MPELPEVETS RRGIEPHLVG ATILHAVVRN GRLRWPVSEE IYRLSDQPVL SVQRRAKYLL LELPEGWIII HLGMSGSLRI LPEELPPEKH DHVDLVMSNG KVLRYTDPRR FGAWLWTKEL EGHNVLTHLG PEPLSDDFNG EYLHQKCAKK KTAIKPWLMD NKLVVGVGNI YASESLFAAG IHPDRLASSL SLAECELLAR VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK GEPCRVCGTP IVATKHAQRA TFYCRQCQK

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    Mutm
  • View Data Sheet

    Name :

    DNAJC24 Human

    Description:

    DnaJ (Hsp40) Homolog, Subfamily C, Member 24 Human Recombinant

    DnaJ homolog subfamily C member 24, DNAJC24, DPH4, JJJ3, ZCSL3, CSL-type zinc finger-containing protein 3, Diphthamide biosynthesis protein 4.

    Product # :

    HSP-056

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    Description

    DNAJC24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-149 a.a.) and having a molecular mass of 19.5kDa. DNAJC24 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DNAJC24 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      DnaJ homolog subfamily C member 24 (DNAJC24) belongs to the ZCSL family of proteins and each contain one DPH-type zinc finger. DNAJC24 is involved in the synthesis of diphthamide, a protein found on translation elongation factor EF-2 which is the target of bacterial ADP-ribosylating toxins. DNAJC24 stimulates the ATPase activity of few Hsp70-type chaperones. DNAJC24 detected in heart, brain, spleen, lung, liver, kidney and testis.

    • Synonyms

      DnaJ homolog subfamily C member 24, DNAJC24, DPH4, JJJ3, ZCSL3, CSL-type zinc finger-containing protein 3, Diphthamide biosynthesis protein 4.

    • 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 MGSMMAVEQM PKKDWYSILG ADPSANISDL KQKYQKLILM YHPDKQSTDV PAGTVEECVQ KFIEIDQAWK ILGNEETKRE YDLQRCEDDL RNVGPVDAQV YLEEMSWNEG DHSFYLSCRC GGKYSVSKDE AEEVSLISCD TCSLIIELLH YN.

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    Dnajc24 Human
  • View Data Sheet

    Name :

    DPP4 Human, HEK

    Description:

    Dipeptidyl-Peptidase 4 Human Recombinant, HEK

    CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    Product # :

    ENZ-1187

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    Description

    DPP4 Human Recombinant is a single, glycosylated polypeptide chain containing 977 amino acids (29-766a.a) and having a molecular mass of 112.1kDa (calculated). DPP4 is fused to a 239 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    DPP4 protein solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

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

    Biological Activity

    Specific activity is > 15,000 pmol/min/ug in which one unit defined as the amount of enzyme that hydrolyze 1pmole of H-Gly-Pro-AMC.HBr to H-Gly-Pro and AMC per minute at pH 8.0 at 37℃.

     The ED50 range ≤250 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike S1 Subunit (CAT# sars-052)..

    The ED50 range ≤200 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike RBD (CAT# sars-054).

    The ED50 range ≤120 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike (CAT# sars-051).

    More Info

    • Synonyms

      CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    • 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

      DGSMNKGTDD ATADSRKTYT LTDYLKNTYR LKLYSLRWIS DHEYLYKQEN NILVFNAEYG NSSVFLENST FDEFGHSIND YSISPDGQFI LLEYNYVKQW RHSYTASYDI YDLNKRQLIT EERIPNNTQW VTWSPVGHKL AYVWNNDIYV KIEPNLPSYR ITWTGKEDII YNGITDWVYE EEVFSAYSAL WWSPNGTFLA YAQFNDTEVP LIEYSFYSDE SLQYPKTVRV PYPKAGAVNP TVKFFVVNTD SLSSVTNATS IQITAPASML IGDHYLCDVT WATQERISLQ WLRRIQNYSV MDICDYDESS GRWNCLVARQ HIEMSTTGWV GRFRPSEPHF TLDGNSFYKI ISNEEGYRHI CYFQIDKKDC TFITKGTWEV IGIEALTSDY LYYISNEYKG MPGGRNLYKI QLSDYTKVTC LSCELNPERC QYYSVSFSKE AKYYQLRCSG PGLPLYTLHS SVNDKGLRVL EDNSALDKML QNVQMPSKKL DFIILNETKF WYQMILPPHF DKSKKYPLLL DVYAGPCSQK ADTVFRLNWA TYLASTENII VASFDGRGSG YQGDKIMHAI NRRLGTFEVE DQIEAARQFS KMGFVDNKRI AIWGWSYGGY VTSMVLGSGS GVFKCGIAVA PVSRWEYYDS VYTERYMGLP TPEDNLDHYR NSTVMSRAEN FKQVEYLLIH GTADDNVHFQ QSAQISKALV DVGVDFQAMW YTDEDHGIAS STAHQHIYTH MSHFIKQCFS LPKLLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGK.

    • Background

      DPP4 protein, also known as Dipeptidyl peptidase-4 or CD26, is a cell surface protease with diverse functions in cell signaling and metabolism. This research aims to investigate the role of DPP4 protein in various physiological processes and its implications in disease pathogenesis. Understanding the biological significance of DPP4 can provide insights into its potential as a therapeutic target for several disorders.

      Function of DPP4 Protein:

      DPP4 protein is involved in the cleavage and regulation of several peptide hormones and chemokines, influencing their bioactivity and half-life. It is widely expressed in various tissues, including immune cells, endothelial cells, and epithelial cells. DPP4 can modulate immune responses, glucose metabolism, and neuropeptide signaling through enzymatic and non-enzymatic activities.

      Role of DPP4 Protein in Immune Regulation:

      DPP4 protein plays a role in immune cell activation and regulation. It is expressed on the surface of T cells, where it functions as a co-stimulatory molecule. DPP4 engagement on T cells promotes T cell activation, cytokine production, and adhesion to endothelial cells. Additionally, DPP4 can cleave and inactivate certain chemokines, thereby influencing chemotaxis and immune cell recruitment.

      Implications of DPP4 Protein in Metabolic Disorders:

      DPP4 protein is involved in glucose metabolism and insulin regulation. It cleaves incretin hormones, such as glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP), which play crucial roles in glucose homeostasis. Inhibition of DPP4 activity can enhance the action of these incretin hormones, leading to improved glycemic control. Therefore, DPP4 inhibitors have been developed as antidiabetic drugs.

      Association of DPP4 Protein with Cardiovascular Diseases:

      DPP4 protein has been implicated in the pathogenesis of cardiovascular diseases. Elevated DPP4 levels have been observed in patients with heart failure, atherosclerosis, and hypertension. DPP4 can contribute to endothelial dysfunction, inflammation, and vascular remodeling, which are key factors in the development and progression of cardiovascular disorders. Inhibition of DPP4 activity has shown potential as a therapeutic strategy in preclinical studies.

      Given its involvement in various biological processes and disease pathogenesis, DPP4 protein has emerged as a potential therapeutic target. DPP4 inhibitors, which prevent the enzymatic activity of DPP4, have been developed for the treatment of type 2 diabetes. These inhibitors enhance the action of incretin hormones, leading to improved glycemic control. Additionally, ongoing research aims to explore the therapeutic potential of DPP4 inhibitors in other conditions, such as immune-mediated disorders and cardiovascular diseases.

      Conclusion:

      The investigation of DPP4 protein provides insights into its diverse functions in cell signaling, immune regulation, and metabolism. Understanding the role of DPP4 in disease pathogenesis opens avenues for the development of targeted therapies for conditions such as diabetes, cardiovascular diseases, and immune-mediated disorders. Further research on DPP4 protein and its associated pathways may uncover new therapeutic opportunities and improve patient outcomes.

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    Dpp4 Human Hek
  • View Data Sheet

    Name :

    NENF Human

    Description:

    Neudesin Neurotrophic Factor Human Recombinant

    Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

    Product # :

    CYT-778

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    Description

    NENF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 32-172) containing 151 amino acids including a 10 a.a N-terminal His tag and having a molecular mass of 16.9kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neudesin Neurotrophic Factor (NENF) is a member of the cytochrome b5 family, MAPR subfamily. NENF contains 1 cytochrome b5 heme-binding domain. NENF exhibits neurotrophic activity and activates phosphorylation of MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT in primary cultured neurons. NENF doesn’t have mitogenic activity in primary cultured astrocytes. NENF may play a part in neuronal differentiation and may have a transient influence on neural cell proliferation in neural precursor cells. NENF neurotrophic activity is increased by binding to heme. NENF is up-regulated in immortal cells and induced in estrogen receptor positive breast cancer expressing progesterone receptor.

    • Synonyms

      Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHASGQTPRPAERG PPVRLFTEEE LARYGGEEED QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL TGKDSTRGVA KMSLDPADLT HDTTGLTAKE LEALDEVFTK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F.

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    Nenf Human
  • View Data Sheet

    Name :

    SNRPD Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide D1, D2, D3 Human Recombinant

    Product # :

    PRO-997

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    • source
    • formulation
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    • More Info

    Description

    SNRPD Human Recombinant produced in SF9 insect cells, is a mixed protein complex containing the SNRPD1 (16 kDa), SNRPD2 (18 kDa) and SNRPD3 (18 kDa) proteins. Each protein (SNRPD1+ SNRPD2+ SNRPD3) is individually fused to a -6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    SNRPD is supplied in 20mM HEPES buffer pH-7.5, 400mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative samples).

    • coating concentration

      0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western blot with:
      a) Anti-Sm positive patient sera.
      b) Monoclonal anti-hexa-His-tag antibody.

    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.

    Snrpd Human
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