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Search results

1000 results found for “epigen”

Name

Description

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  • 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

    Price :

    Quantity :

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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.

    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.

    Product Image
  • View Data Sheet

    Name :

    MIP 1b Rat

    Description:

    Macrophage Inflammatory Protein-1 beta Rat Recombinant (CCL4)

    C-C motif chemokine 4, Macrophage inflammatory protein 1-beta, MIP-1-beta, Small-inducible cytokine A4, Ccl4, Mip1b, Scya4.

    Product # :

    CHM-003

    Price :

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    Description

    MIP-1b Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids and having a molecular mass of 7.8 kDa. The MIP-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human monocytes using a concentration range of 0.01-1.0 µg/ml.

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1? and MIP-1? that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-? from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

    • Synonyms

      C-C motif chemokine 4, Macrophage inflammatory protein 1-beta, MIP-1-beta, Small-inducible cytokine A4, Ccl4, Mip1b, Scya4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CCL4 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 Mouse MIP-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APIGSDPPTS CCFSYTSRKI HRNFVMDYYE TSSLCSQPAV VFLTKKGRQI CADPSEPWVN EYVNDLELN.

    • Background

      What is the molecular weight/Mw of MIP 1B RAT Protein?
      MIP 1B RAT Protein has a total Mw of 7.8kDa.

      What is the source or expression system of MIP 1B RAT Protein?
      Escherichia Coli.

      What is the Purity of MIP 1B RAT Protein?
      MIP 1B RAT Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1B RAT Protein?
      Determined by its ability to chemoattract human monocytes using a concentration range of 0.01-1.0 µg/ml.

      What is the amino acid sequence of MIP 1B RAT Protein?
      APIGSDPPTS CCFSYTSRKI HRNFVMDYYE TSSLCSQPAV VFLTKKGRQI CADPSEPWVN EYVNDLELN.

      What applications can MIP 1B RAT Protein be used in?
      MIP 1B RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1B RAT Protein?
      The endotoxin level is minimal, MIP 1B RAT Protein was purified using conventional chromatography techniques.


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

    Mip 1B Rat
  • View Data Sheet

    Name :

    Leptin Porcine

    Description:

    Leptin Porcine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-503

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
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    • purity
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    • More Info

    Description

    Leptin Porcine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and additional Ala at N-terminus, having a molecular mass of 16kDa. The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 recombinant porcine leptin in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.57 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 calibrated solution of Leptin Porcine 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.

    Leptin Porcine
  • View Data Sheet

    Name :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile water or 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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).

    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
  • View Data Sheet

    Name :

    Leptin Bovine

    Description:

    Leptin Bovine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-502

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    Description

    Leptin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation 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. 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 Bovine
  • View Data Sheet

    Name :

    EBV p18, GST

    Description:

    Epstein - Barr virus (HHV-4) p18 Recombinant, GST Tag

    Product # :

    EBV-277

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    Description

    The E.Coli derived recombinant protein contains the HHV-4 p18 regions, having a molecular mass of 35.4kDa which includes GST tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    3.8mg/ml in 50mM Tris-HCl, pH 8.0.

    Purity

    Protein is >90% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virus of the herpes family (which includes Herpes simplex virus and Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expression which can be broadly categorized as being lytic cycle or latent cycle. The lytic cycle or productive infection results in staged expression of a host of viral proteins with the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cell as EBV virions are produced by budding from the infected cell. The latent cycle (lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen (EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins (LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs (EBERs).

    • Stability

      EBV p18, GST although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      ASAGTGALAS SAPSTAVAQS ATPSVSSSIS SLRAATSGAT AAASAAAAVD TGSGGGGQPH DTAPRGARKK Q.

    • Purification Method

      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.

    Ebv P18 Gst
  • View Data Sheet

    Name :

    MIF Rat

    Description:

    Macrophage Migration Inhibitory Factor Rat Recombinant

    Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    Product # :

    CYT-193

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    Description

    MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

    Purity

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

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

    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.

    Mif Rat
  • View Data Sheet

    Name :

    MIP 3a Mouse

    Description:

    Macrophage Inflammatory Protein-3 alpha Mouse Recombinant (CCL20)

    Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.

    Product # :

    CHM-236

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    Description

    Macrophage Inflammatory Protein-3 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.9 kDa. The MIP-3a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.

    More Info

    • Introduction

      CCL20 is a chemotactic factor that draws lymphocytes & neutrophils, rather than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria.
      MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission.

    • Synonyms

      Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL-20 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 MIP-3a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.

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

    Mip 3A Mouse
  • View Data Sheet

    Name :

    NRG1 A Human

    Description:

    Neuregulin-1/Heregulin Alpha (EGF Domain) Human Recombinant

    Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.

    Product # :

    CYT-736

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    Description

    Recombinant Human Neuregulin-1/Heregulin Alpha (EGF Domain) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 65 amino acids and having a total molecular mass of 7.4kDa. NRG1-A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 6.0 and 150mM NaCl.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 40 ng/ml, corresponding to a specific activity of > 2.5×104 units/mg.

    More Info

    • Introduction

      Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms act to induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.

    • Synonyms

      Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NRG1-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-A should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NRG1-A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK.

    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.

    Nrg1 A Human
  • View Data Sheet

    Name :

    AGA Human

    Description:

    Aspartylglucosaminidase Human Recombinant

    Aspartylglucosaminidase, AGU, ASRG, GA.

    Product # :

    ENZ-854

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    Description

    AGA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (24-346 a.a.) and having a molecular mass of 37kDa.AGA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    AGA protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.

    • Synonyms

      Aspartylglucosaminidase, AGU, ASRG, GA.

    • 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 MGSSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCI.

    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.

    Aga Human
  • View Data Sheet

    Name :

    IDH3G Human

    Description:

    Isocitrate Dehydrogenase 3 (NAD+) Gamma Human Recombinant

    Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial, Isocitric dehydrogenase subunit gamma, NAD(+)-specific ICDH subunit gamma, IDH3G, H-IDHG.

    Product # :

    ENZ-205

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    Description

    IDH3G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (40-393) and having a molecular mass of 41.1kDa.IDH3G is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IDH3G solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Isocitrate dehydrogenase [NAD] subunit gamma (IDH3G) mitochondrial is a member of the isocitrate and isopropylmalate dehydrogenases family. Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. The IDH3G is a gamma subunit of one isozyme of isocitrate dehydrogenase which belongs to a distinct subclass, which utilizes NAD(+) as the electron acceptor, and is restricted to the mitochondrial matrix.

    • Synonyms

      Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial, Isocitric dehydrogenase subunit gamma, NAD(+)-specific ICDH subunit gamma, IDH3G, H-IDHG.

    • 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 MFSEQTIPPS AKYGGRHTVT MIPGDGIGPE LMLHVKSVFR HACVPVDFEE VHVSSNADEE DIRNAIMAIR RNRVALKGNI ETNHNLPPSH KSRNNILRTS LDLYANVIHC KSLPGVVTRH KDIDILIVRE NTEGEYSSLE HESVAGVVES LKIITKAKSL RIAEYAFKLA QESGRKKVTA VHKANIMKLG DGLFLQCCRE VAARYPQITF ENMIVDNTTM QLVSRPQQFD VMVMPNLYGN IVNNVCAGLV GGPGLVAGAN YGHVYAVFET ATRNTGKSIA NKNIANPTAT LLASCMMLDH LKLHSYATSI RKAVLASMDN ENMHTPDIGG QGTTSEAIQD VIRHIRVING RAVEA.

    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.

    Idh3G Human
  • View Data Sheet

    Name :

    EDAR Human, Sf9

    Description:

    Ectodysplasin A Receptor Human Recombinant, Sf9

    Ectodysplasin A Receptor, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Downless Homolog, EDA-A1 Receptor, DL, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, Ectodysplasin-A Receptor, ECTD10A, ECTD10B, EDA-A1R, EDA1R, ED1R, EDA3, HRM1, ED5, ED3.

    Product # :

    PRO-2510

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    Description

    EDAR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (27-187a.a.) and having a molecular mass of 45.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).EDAR is expressed with a 249 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.

    • Synonyms

      Ectodysplasin A Receptor, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Downless Homolog, EDA-A1 Receptor, DL, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, Ectodysplasin-A Receptor, ECTD10A, ECTD10B, EDA-A1R, EDA1R, ED1R, EDA3, HRM1, ED5, ED3.

    • 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

      ADPEYSNCGE NEYYNQTTGL CQECPPCGPG EEPYLSCGYG TKDEDYGCVP CPAEKFSKGG YQICRRHKDC EGFFRATVLT PGDMENDAEC GPCLPGYYML ENRPRNIYGM VCYSCLLAPP NTKECVGATS GASANFPGTS GSSTLSPFQH AHKELSGQGH LATAAAAFES ACSLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH 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.

    Edar Protein
  • View Data Sheet

    Name :

    IFNAR1 Mouse

    Description:

    Interferon Alpha And Beta Receptor Mouse Recombinant

    IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.

    Product # :

    CYT-994

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    • SDS-PAGE

    Description

    IFNAR1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 411 amino acids (27-429a.a) and having a molecular mass of 46.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IFNAR1 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IFNAR1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    IFNAR1 Mouse - Product image 1

    More Info

    • Introduction

      Interferon Alpha And Beta Receptor, also known IFNAR1, belongs to the class II cytokine receptor family. IFNAR1 protein forms one of the two chains of a receptor for interferons alpha as well as beta. IFNAR1 binds and activates the receptor which stimulates Janus protein kinases, which in turn phosphorylate some proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also functions as an antiviral factor.

    • Synonyms

      IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.

    • 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

      ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H

    • Background

      What is the molecular weight/Mw of IFNAR1 MOUSE Protein?
      IFNAR1 MOUSE Protein has a total Mw of 46.8kDa.

      What is the source or expression system of IFNAR1 MOUSE Protein?
      Sf9, Baculovirus cells.
      What is the Purity of IFNAR1 MOUSE Protein?
      IFNAR1 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNAR1 MOUSE Protein?
      The biological functionality of IFNAR1 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of IFNAR1 MOUSE Protein?
      ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H

      What applications can IFNAR1 MOUSE Protein be used in?
      IFNAR1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNAR1 MOUSE Protein?
      The endotoxin level is minimal, IFNAR1 MOUSE Protein was purified using conventional chromatography techniques.


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

    Ifnar1 Mouse
  • View Data Sheet

    Name :

    EGFL6 Mouse

    Description:

    EGF Like Domain Multiple 6 Mouse Recombinant

    Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg.

    Product # :

    CYT-1105

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    Description

    EGFL6 Mouse Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 273 amino acids (287-550a.a.) and having a molecular mass of 31.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EGFL6 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    EGFL6 protein solution ( 0.5mg/ml ) contains Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Epidermal Growth Factor­like Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.

    • Synonyms

      Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg.

    • 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

      ADLTMKKKVK LKMVTPRPAS TRVPKVNLPY SSEEGVSRGR NYDGEQKKKE EGKRERLEEE
      KGEKTLRNEV EQERTLRGDV FSPKVNEAED LDLVYVQRKE LNSKLKHKDL NISVDCSFDL
      GVCDWKQDRE DDFDWHPADR DNDVGYYMAV PALAGHKKNI GRLKLLLPNL TPQSNFCLLF
      DYRLAGDKVG KLRVFVKNSN NALAWEETKN EDGRWRTGKI QLYQGIDTTK SVIFEAERGK GKTGEIAVDG VLLVSGLCPD DFLSVEGHHH HHH.

    • Background

      Title: EGF-Like Domain Multiple 6 Mouse Recombinant: Insights into its Biological Significance and Potential Applications

      Abstract:


      EGF-Like Domain Multiple 6 (EGFL6) is a critical protein involved in various biological processes, including development, tissue homeostasis, and cancer progression. This research paper provides a comprehensive analysis of mouse recombinant EGFL6, focusing on its production, characterization, and potential applications in studying its biological functions. The paper highlights the significance of EGFL6 in cellular processes and its role in disease pathogenesis. Furthermore, it discusses ongoing research and potential therapeutic applications of recombinant EGFL6 in cancer and regenerative medicine. The information presented in this paper aims to enhance our understanding of mouse recombinant EGFL6 and its utility as a research tool and a potential therapeutic agent.

      Introduction:


      EGF-Like Domain Multiple 6 (EGFL6) is a secreted protein that belongs to the epidermal growth factor (EGF) family. Mouse recombinant EGFL6, produced through genetic engineering techniques, provides a valuable tool for investigating its biological functions and potential therapeutic applications.

      Production and Characterization:


      Recombinant EGFL6 is typically generated using expression systems such as bacteria or mammalian cells. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EGFL6.

      Biological Significance:


      EGFL6 plays a crucial role in diverse cellular processes, including angiogenesis, tissue regeneration, and cell proliferation. It is involved in the modulation of signaling pathways, such as the Wnt/β-catenin pathway, and interacts with extracellular matrix components. Recombinant EGFL6 offers a valuable tool for investigating the molecular mechanisms underlying its biological functions and its involvement in disease pathogenesis.

      Role in Cancer:


      EGFL6 is implicated in cancer progression and metastasis. It promotes tumor angiogenesis, invasion, and resistance to chemotherapy. Studies utilizing recombinant EGFL6 can contribute to a better understanding of its role in tumor microenvironment remodeling and the development of targeted therapeutic strategies.

      Therapeutic Implications:


      Given its involvement in various cellular processes and disease pathogenesis, EGFL6 has emerged as a potential therapeutic target. Recombinant EGFL6-based therapies, such as antibody-based approaches or small molecule inhibitors, hold promise for cancer treatment and regenerative medicine. Ongoing research is focused on developing strategies to modulate EGFL6 activity for therapeutic benefit.

      Conclusion:


      Mouse recombinant EGFL6 serves as a valuable research tool for studying its biological functions and exploring its therapeutic potential. Its production, characterization, and applications in understanding cellular processes and disease pathogenesis contribute to our knowledge of EGFL6 biology and the development of targeted interventions. Continued research and clinical investigations exploring the therapeutic applications of recombinant EGFL6 offer promising avenues for improving outcomes in cancer and regenerative medicine.

      What is the molecular weight/Mw of EGFL6 MOUSE Protein?
      EGFL6 MOUSE Protein has a total Mw of 31.1kDa.

      What is the source or expression system of EGFL6 MOUSE Protein?
      Sf9, Insect cells.

      What is the Purity of EGFL6 MOUSE Protein?
      EGFL6 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of EGFL6 MOUSE Protein?
      The biological functionality of EGFL6 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of EGFL6 MOUSE Protein?
      EGFL6 MOUSE Protein is composed from 273 amino acids.

      What applications can EGFL6 MOUSE Protein be used in?
      EGFL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EGFL6 MOUSE Protein?
      The endotoxin level is minimal, EGFL6 MOUSE Protein was purified using conventional chromatography techniques.

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

    Egfl6 Mouse
  • View Data Sheet

    Name :

    GAGE2A Human

    Description:

    G Antigen 2A Human Recombinant

    G Antigen 2A, G Antigen 2A/2B, Cancer/Testis Antigen Family 4, Cancer/Testis Antigen Family 4, Member 2, GAGE-2A, Member 2, CT4.2, GAGE-2.

    Product # :

    PRO-1705

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    Description

    GAGE2A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.2kDa.GAGE2A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GAGE2A solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GAGE2A is a member of a multigene family expressed in a large variety of tumors while in normal tissues; expression is limited to germ cells. These genes organized in clustered repeats, have a high degree of predicted sequence identity, however differ by scattered single nucleotide change. Their sequences have either the antigenic peptide YRPRPRRY or YYWPRPRRY which is recognized by cytotoxic T-cells.

    • Synonyms

      G Antigen 2A, G Antigen 2A/2B, Cancer/Testis Antigen Family 4, Cancer/Testis Antigen Family 4, Member 2, GAGE-2A, Member 2, CT4.2, GAGE-2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSWRGRS TYRPRPRRYV EPPEMIGPMR PEQFSDEVEP ATPEEGEPAT QRQDPAAAQE GQDEGASAGQ GPKPEAHSQE QGHPQTGCEC EDGPDGQEMD PPNPEEVKTP EEGEKQSQC

    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.

    Gage2A Human
  • View Data Sheet

    Name :

    KRT17 Human

    Description:

    Cytokeratin 17 Human Recombinant

    Keratin 17, PCHC1, 39.1, CK-17, K17, PC2, PC, cytokeratin-17, Keratin 17 Epitope S1, Keratin 17 Epitope S2, Keratin 17 Epitope S4, Keratin, Type I Cytoskeletal 1, keratin-17, Cytokeratin-17, Keratin-17.

    Product # :

    PRO-1883

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    Description

    KRT17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (1-432 a.a) and having a molecular mass of 50.5kDa.KRT17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 17 also known as KRT17 is a type I cytokeratin. KRT17 is found in nail beds, hair follicles, sebaceous glands, and other epidermal appendages. Mutations in KRT17 lead to Jackson-Lawler type pachyonychia congenita and steatocystoma multiplex. KRT17 takes part in the formation and maintenance of a variety of skin appendages, particularly in determining shape and orientation of hair. KRT17 also modulates the function of TNF-alpha in the precise context of hair cycling. Moreover, KRT17 regulates protein synthesis and epithelial cell growth all through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway.

    • Synonyms

      Keratin 17, PCHC1, 39.1, CK-17, K17, PC2, PC, cytokeratin-17, Keratin 17 Epitope S1, Keratin 17 Epitope S2, Keratin 17 Epitope S4, Keratin, Type I Cytoskeletal 1, keratin-17, Cytokeratin-17, Keratin-17.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTTSIRQ FTSSSSIKGS SGLGGGSSRT SCRLSGGLGA GSCRLGSAGG LGSTLGGSSY SSCYSFGSGG GYGSSFGGVD GLLAGGEKAT MQNLNDRLAS YLDKVRALEE ANTELEVKIR DWYQRQAPGP ARDYSQYYRT IEELQNKILT ATVDNANILL QIDNARLAAD DFRTKFETEQ ALRLSVEADI NGLRRVLDEL TLARADLEMQ IENLKEELAY LKKNHEEEMN ALRGQVGGEI NVEMDAAPGV DLSRILNEMR DQYEKMAEKN RKDAEDWFFS KTEELNREVA TNSELVQSGK SEISELRRTM QALEIELQSQ LSMKASLEGN LAETENRYCV QLSQIQGLIG SVEEQLAQLR CEMEQQNQEY KILLDVKTRL EQEIATYRRL LEGEDAHLTQ YKKEPVTTRQ VRTIVEEVQD GKVISSREQV HQTTR

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    Krt17 Human
  • View Data Sheet

    Name :

    CETN1 Human

    Description:

    Centrin-1 Human Recombinant

    Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.

    Product # :

    PRO-1104

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    Description

    CETN1 Human Recombinant produced E. coli is a single polypeptide chain containing 196 amino acids (1-172) and having a molecular mass of 22.1kDa.CETN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CETN1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.

    • Synonyms

      Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.

    • 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 MGSHMASGFK KPSAASTGQK RKVAPKPELT EDQKQEVREA FDLFDVDGSG TIDAKELKVA MRALGFEPRK EEMKKMISEV DREGTGKISF NDFLAVMTQK MSEKDTKEEI LKAFRLFDDD ETGKISFKNL KRVANELGEN LTDEELQEMI DEADRDGDGE VNEEEFLRIM KKTSLY

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    Cetn1 Human
  • View Data Sheet

    Name :

    CIDEC Human

    Description:

    Cell Death-Inducing DFFA-Like Effector C Human Recombinant

    Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    Product # :

    PRO-2026

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    Description

    CIDEC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu2-Gln238) containing 247 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 28kDa.

    Source

    Escherichia Coli.

    Formulation

    CIDEC filtered (0.4µm) solution at a concentration of 0.4mg/ml in 30mM acetate buffer and 10mM dithiothreitol, pH 4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cell Death-Inducing DFFA-Like Effector C (CIDEC) belongs to the cell death-inducing DNA fragmentation factor-like effector family, whose members have significant roles in apoptosis. CIDEC is expressed mainly in adipocytes, intestine, heart, stomach, and weakly in the brain, kidney and liver. CIDEC overexpression in preadipocytes induces apoptosis. CIDEC regulates enlargement of lipid droplets.

    • Synonyms

      Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    • Physical Appearance

      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

      MKHHHHHHASEYAMKSLSLL YPKSLSRHVS VRTSVVTQQL LSEPSPKAPR ARPCRVSTAD RSVRKGIMAY SLEDLLLKVR DTLMLADKPF FLVLEEDGTT VETEEYFQAL AGDTVFMVLQ KGQKWQPPSE QGTRHPLSLS HKPAKKIDVA RVTFDLYKLN PQDFIGCLNV KATFYDTYSL SYDLHCCGAK RIMKEAFRWA LFSMQATGHV LLGTSCYLQQ LLDATEEGQP PKGKASSLIP TCLKILQ.

    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.

    Cidec Human
  • View Data Sheet

    Name :

    Avidin Recombinant

    Description:

    Avidin Recombinant

    Avidin, AVD, AVID.

    Product # :

    PRO-2597

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    Description

    Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.

    Source

    Corn (Zea Mays).

    Purity

    Greater than 90% as visualized by SDS-PAGE.

    Biological Activity

    13.5 units/mg protein, 1 unit binds 1µg biotin.

    More Info

    • Introduction

      Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

    • Synonyms

      Avidin, AVD, AVID.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Recombinant Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant Avidin 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 Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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.

    Avidin Recombinant
  • View Data Sheet

    Name :

    Eotaxin Mouse

    Description:

    Eotaxin Mouse Recombinant (CCL11)

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

    Product # :

    CHM-308

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    Description

    Eotaxin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8403.2 Dalton. The CCL11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin 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 His-Pro-Gly-Ser-Ile.

    • Background

      What is the molecular weight/Mw of EOTAXIN MOUSE Protein?
      EOTAXIN MOUSE Protein has a total Mw of 8.4kDa.

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

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

      What is the Biological Activity of EOTAXIN MOUSE Protein?
      The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.

      What is the amino acid sequence of EOTAXIN MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be His-Pro-Gly-Ser-Ile.

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

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


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

    Eotaxin Mouse
  • View Data Sheet

    Name :

    AIMP1 Human

    Description:

    Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein 1 Human Recombinant

    Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.

    Product # :

    CYT-021

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    • sds-page

    Description

    AIMP1 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 356 amino acids (1-336 a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear higher). The AIMP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AIMP1 solution (0.25mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    AIMP1 Human-sds-page - Product image 1

    More Info

    • Introduction

      AIMP1 (EMPA2 or p43) is a cytokine that is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of the AIMP1 cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. Furthermore, AIMP1 is involved in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.

    • Synonyms

      Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.

    • 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 MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

    • Background

      What is the molecular weight/Mw of AIMP1 HUMAN Protein?
      AIMP1 HUMAN Protein has a total Mw of 39.2kDa.

      What is the source or expression system of AIMP1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of AIMP1 HUMAN Protein?
      AIMP1 HUMAN Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of AIMP1 HUMAN Protein?
      The biological functionality of AIMP1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of AIMP1 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

      What applications can AIMP1 HUMAN Protein be used in?
      AIMP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for AIMP1 HUMAN Protein?
      The endotoxin level is minimal, AIMP1 HUMAN Protein was purified using conventional chromatography techniques..

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

    Aimp1 Human
  • View Data Sheet

    Name :

    MIP 1a Human

    Description:

    Macrophage Inflammatory Protein-1 Alpha Human Recombinant (CCL3)

    Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.

    Product # :

    CHM-233

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    • description
    • source
    • formulation
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    • More Info

    Description

    Macrophage Inflammatory Protein-1 alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 0.55 mg/ml solution containing no additives.

    Purity

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

    Biological Activity

    The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophilsand basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

    • Synonyms

      Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

      What is the molecular weight/Mw of MIP 1A HUMAN Protein?
      MIP 1A HUMAN Protein has a total Mw of 7.82kDa.

      What is the source or expression system of MIP 1A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of MIP 1A HUMAN Protein?
      MIP 1A HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1A HUMAN Protein?
      The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of MIP 1A HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Ser-Leu-Ala-Ala.

      What applications can MIP 1A HUMAN Protein be used in?
      MIP 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1A HUMAN Protein?
      The endotoxin level is minimal, MIP 1A HUMAN Protein was purified using conventional chromatography techniques.


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

    Mip 1A Human
  • View Data Sheet

    Name :

    MIP 3b Mouse

    Description:

    Macrophage Inflammatory Protein-3 Beta Mouse Recombinant (CCL19)

    Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433, Epstein-Barr virus-induced molecule 1 ligand chemokine, EBI1-ligand chemokine.

    Product # :

    CHM-341

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    Description

    Macrophage Inflammatory Protein-3 beta Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9216 Dalton. The MIP-3b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to chemoattract human PBL, is less than 100ng/ml. 

    More Info

    • Introduction

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

    • Synonyms

      Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433, Epstein-Barr virus-induced molecule 1 ligand chemokine, EBI1-ligand chemokine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL19 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-3b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GANDAEDCCL SVTQRPIPGN IVKAFRYLLN EDGCRVPAVV FTTLRGYQLC APPDQPWVDR IIRRLKKSSA KNKGNSTRRS PVLE.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.91 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 MIP-3b 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.

    Mip 3B Mouse
  • View Data Sheet

    Name :

    DGCR6 Human

    Description:

    DiGeorge Syndrome Critical Region Gene 6 Human Recombinant

    DiGeorge syndrome critical region gene 6, Protein DGCR6, DGCR6.

    Product # :

    PRO-1372

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    Description

    DGCR6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27kDa. DGCR6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    DGCR6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      DiGeorge syndrome critical region gene 6 (DGCR6) shares homology with the Drosophila melanogaster gonadal protein, that participates in gonadal and germ cell development, and also with the gamma-1 subunit of human laminin. DGCR6 is involved in DiGeorge syndrome pathology and in schizophrenia.

    • Synonyms

      DiGeorge syndrome critical region gene 6, Protein DGCR6, DGCR6.

    • 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 MGSMERYAGA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVLQA AQQRELEAVE HRIREEQRAM DQKIVLELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCWAGKAA LGLGGPWQLP AAQCDQKGSP VPP.

    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.

    Dgcr6 Human
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