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Search results

1000 results found for “sclerostin”

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  • View Data Sheet

    Name :

    SULT1B1 Human

    Description:

    Sulfotransferase Family, Cytosolic, 1B, Member 1 Human Recombinant

    Sulfotransferase family cytosolic 1B member 1, Thyroid hormone sulfotransferase, Sulfotransferase 1B1, Sulfotransferase 1B2, ST1B1, EC 2.8.2.-, SULT1B2.

    Product # :

    ENZ-610

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    Description

    SULT1B1 Human Recombinant produced in E. coli is a single polypeptide chain containing 320 amino acids (1-296) and having a molecular mass of 37.4kDa.SULT1B1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SULT1B1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SULT1B1 enzyme in humans is encoded by the SULT1B1 gene. SULT1B1 holds a binding site for 3-prime-phosphoadenosine 5-prime-phosphosulfate, a sulfate donor, in addition to a cysteine residue conserved in the ST1 gene family of sulfotransferases. Sulfotransferases like SULT1B1 catalyze the biotransformation of a great amount of endogenous amalgams such as bile acids, neurotransmitters, steroids, and thyroid hormones, in addition to drugs and xenobiotics.

    • Synonyms

      Sulfotransferase family cytosolic 1B member 1, Thyroid hormone sulfotransferase, Sulfotransferase 1B1, Sulfotransferase 1B2, ST1B1, EC 2.8.2.-, SULT1B2.

    • 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 MGSHMLSPKD ILRKDLKLVH GYPMTCAFAS NWEKIEQFHS RPDDIVIATY PKSGTTWVSE IIDMILNDGD IEKCKRGFIT EKVPMLEMTL PGLRTSGIEQ LEKNPSPRIV KTHLPTDLLP KSFWENNCKM IYLARNAKDV SVSYYHFDLM NNLQPFPGTW EEYLEKFLTG KVAYGSWFTH VKNWWKKKEE HPILFLYYED MKENPKEEIK KIIRFLEKNL NDEILDRIIH HTSFEVMKDN PLVNYTHLPT TVMDHSKSPF MRKGTAGDWK NYFTVAQNEK FDAIYETEMS KTALQFRTEI

    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.

    Sult1B1 Human
  • View Data Sheet

    Name :

    CXCL8 Porcine (1-72)

    Description:

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

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

    Product # :

    CHM-340

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    Description

    Interleukin-8 Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 9.1kDa. The IL8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    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 a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 20-200 ng/ml.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.

    • Background

      What is the molecular weight/Mw of CXCL8 PORCINE (1-72) Protein?
      CXCL8 PORCINE (1-72) Protein has a total Mw of 9.1kDa.

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

      What is the Purity of CXCL8 PORCINE (1-72) Protein?
      CXCL8 PORCINE (1-72) Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 PORCINE (1-72) Protein?
      The biological activity was determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 20-200 ng/ml.

      What is the amino acid sequence of CXCL8 PORCINE (1-72) Protein?
      ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.

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

      What is the endotoxin level for CXCL8 PORCINE (1-72) Protein?
      The endotoxin level is minimal, CXCL8 PORCINE (1-72) Protein was purified using conventional chromatography techniques.


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

    Il 8 72 Porcine
  • View Data Sheet

    Name :

    CCL6 Rat

    Description:

    C-10 Rat Recombinant (CCL6)

    Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.

    Product # :

    CHM-268

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    Description

    C-10 Rat Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 94 amino acids and having a total molecular mass of 10.4kDa. C-10 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25 ug/ml.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 6 (CCL6) is a small cytokine belonging to the CC chemokine family that has only been identified in rodents.
      In mice, CCL6 is expressed in cells from neutrophil and macrophage lineages, and can be greatly induced under conditions suitable for myeloid cell differentiation. It is highly expressed in bone marrow cultures that have been stimulated with the cytokine GM-CSF. Some low levels of gene expression also occur in certain cell lines of myeloid origin (e.g. the immature myeloid cell lines DA3 and 32D cl3, and the macrophage cell line P388D) that can also be greatly induced in culture with GM-CSF. However, in activated T cell lines, expression of CCL6 is greatly reduced. CCL6 can also be induced in the mouse lung by the cytokine interleukin 13. Mouse CCL6 is located on chromosome 11. The cell surface receptor for CCL6 is believed to be the chemokine receptor CCR1.

    • Synonyms

      Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized C-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution C-10 should be stored at 4C between 2-7 days and for future use below -18C.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 C-10 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GLIQDTVKED RPFNPTIIHQ GFQDSSDCCF SYASQIPCSR FIYYFPTSGG CTKPGIIFVT RKRKRVCANP SDQRVQTCIS TLKLGPRSGN SAIA.

    • Background

      What is the molecular weight/Mw of CCL6 RAT Protein?
      CCL6 RAT Protein has a total Mw of 10.4kDa.

      What is the source or expression system of CCL6 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL6 RAT Protein?
      CCL6 RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL6 RAT Protein?
      Determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25 ug/ml.

      What is the amino acid sequence of CCL6 RAT Protein?
      GLIQDTVKED RPFNPTIIHQ GFQDSSDCCF SYASQIPCSR FIYYFPTSGG CTKPGIIFVT RKRKRVCANP SDQRVQTCIS TLKLGPRSGN SAIA.

      What applications can CCL6 RAT Protein be used in?
      CCL6 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL6 RAT Protein?
      The endotoxin level is minimal, CCL6 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.

    C 10 Rat
  • View Data Sheet

    Name :

    TCL1A Human

    Description:

    T-cell Leukemia/Lymphoma 1A Human Recombinant

    T-cell leukemia/lymphoma protein 1A, Protein p14 TCL1, Oncogene TCL-1, Oncogene TCL1, TCL1A, TCL1.

    Product # :

    PRO-726

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    Description

    TCL1A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids (1-114 a.a.) and having a molecular mass of 13.4kDa.The TCL1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TCL1A protein solution contains 50mM Tris-HCl buffer (pH7.5) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TCL1A (T-cell leukemia/lymphoma 1A) is a protein with a possible role in intracellular regulation of T cell signaling. TCL1A enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival. TCL1A is restricted in the T-cell lineage to immature thymocytes and activated peripheral lymphocytes. TCL1A is preferentially expressed early in T and B-lymphocyte differentiation. Chromosomal anomalies activating TCL1A are found in chronic T-cell leukemias (T-CLL).
      TCL1A enhances the phosphorylation and activation of AKT1, AKT2 and AKT3. TCL1A promotes nuclear translocation of AKT1. TCL1A binds to the pleckstrin homology domain of Akt (protein kinase B) family proteins, which facilitates Akt dimerization and activity. By increasing Akt activity, TCL1A can enhance the serine/threonine phosphorylation of major Akt signaling substrates, for example Ikk complex, mTOR, BAD, p70S6 kinase, FOXO transcription factors and GSK3b. These substrates regulate cellular differentiation, growth, survival, and metabolism.

    • Synonyms

      T-cell leukemia/lymphoma protein 1A, Protein p14 TCL1, Oncogene TCL-1, Oncogene TCL1, TCL1A, TCL1.

    • 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

      MAECPTLGEA VTDHPDRLWA WEKFVYLDEK QHAWLPLTIE IKDRLQLRVL LRREDVVLGR PMTPTQIGPS LLPIMWQLYP DGRYRSSDSS FWRLVYHIKI DGVEDMLLEL LPDD.

    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.

    Tcl1A Human
  • View Data Sheet

    Name :

    CAPNS1 Human

    Description:

    Calpain, Small Subunit 1 Human Recombinant

    Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    Product # :

    PRO-1965

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    Description

    CAPNS1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (84-268) and having a molecular mass of 23.8 kDa.CAPNS1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CAPNS1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calpain, Small Subunit 1 (CAPNS1) belongs to the calpain small subunit family. Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases, widely distributed in mammalian cells. Calpain families are implicated in neurodegenerative processes, considering that their activation can be triggered by calcium influx and oxidative stress. Calpains function as heterodimers, comprising a specific large catalytic subunit (calpain 1 subunit in Calpain I, and calpain 2 subunit in Calpain II), and a common small regulatory subunit encoded by the CAPNS1 gene. The CAPNS1 protein is vital for the stability and function of both calpain heterodimers, whose proteolytic activities influence numerous cellular functions including apoptosis, proliferation, migration, adhesion, and autophagy.

    • Synonyms

      Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    • 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 MGSRTHYSNI EANESEEVRQ FRRLFAQLAG DDMEVSATEL MNILNKVVTR HPDLKTDGFG IDTCRSMVAV MDSDTTGKLG FEEFKYLWNN IKRWQAIYKQ FDTDRSGTIC SSELPGAFEA AGFHLNEHLY NMIIRRYSDE SGNMDFDNFI SCLVRLDAMF RAFKSLDKDG TGQIQVNIQE WLQLTMYS.

    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.

    Capns1 Human
  • View Data Sheet

    Name :

    CBR1 Human

    Description:

    Carbonyl Reductase-1 Human Recombinant

    CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.

    Product # :

    ENZ-415

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    Description

    Recombinant Human CBR1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-277 a.a) and having a molecular mass of 30 kDa. CBR1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CBR1 protein contains 20mM Tris-HCl buffer pH-8.5, and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.

    • Synonyms

      CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.

    • 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

      MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP TPFHIQAEVT MKTNFFGTRD VCTELLPLIK PQGRVVNVSS IMSVRALKSC SPELQQKFRS ETITEEELVG LMNKFVEDTK KGVHQKEGWP SSAYGVTKIG VTVLSRIHAR KLSEQRKGDK ILLNACCPGW VRTDMAGPKA TKSPEEGAET PVYLALLPPD AEGPHGQFVS EKRVEQW.

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    Cbr1 Human
  • View Data Sheet

    Name :

    CCL28 Human, His

    Description:

    Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28), His Tag

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-366

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    Description

    CCL28 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 126 amino acids (23-127 a.a.) and having a molecular mass of 14.3 kDa. The CCL28 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL28 protein contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • 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 MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.

    • Background

      What is the molecular weight/Mw of CCL28 HUMAN, HIS Protein?
      CCL28 HUMAN, HIS Protein has a total Mw of 14.3kDa.

      What is the source or expression system of CCL28 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL28 HUMAN, HIS Protein?
      CCL28 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 HUMAN, HIS Protein?
      The biological functionality of CCL28 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL28 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.

      What applications can CCL28 HUMAN, HIS Protein be used in?
      CCL28 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL28 HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

    Ccl28 Human His
  • View Data Sheet

    Name :

    CCL28 Rat

    Description:

    Mucosae-Associated Epithelial Chemokine (CCL28) Rat Recombinant

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-278

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    Description

    MEC Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13.1kDa. The Rat MEC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and150mM NaCl.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract murine lymphocytes using a concentration range of 1.0-10.0 ng/ml.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MEC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution MEC should be stored at 4C between 2-7 days and for future use below -18C.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 MEC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SEAILPIASS CCTEVSHHIP RRLLERVNSC SIQRADGDCD LAAVILHVKR RRICVSPHNP TLKRWMSASE MKNGKENLCP RKKQDSGKDR KGHTPRKHGK HGTRRIHGTH DHEAPR.

    • Background

      What is the molecular weight/Mw of CCL28 RAT Protein?
      CCL28 RAT Protein has a total Mw of 13.1kDa.

      What is the source or expression system of CCL28 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL28 RAT Protein?
      CCL28 RAT Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 RAT Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 1.0-10.0 ng/ml.

      What is the amino acid sequence of CCL28 RAT Protein?
      SEAILPIASS CCTEVSHHIP RRLLERVNSC SIQRADGDCD LAAVILHVKR RRICVSPHNP TLKRWMSASE MKNGKENLCP RKKQDSGKDR KGHTPRKHGK HGTRRIHGTH DHEAPR.

      What applications can CCL28 RAT Protein be used in?
      CCL28 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 RAT Protein?
      The endotoxin level is minimal, CCL28 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.

    Ccl28 Rat
  • View Data Sheet

    Name :

    ITGB1 Human

    Description:

    Integrin Beta 1 Human Recombinant

    Integrin beta-1, Fibronectin receptor subunit beta, Glycoprotein IIa, GPIIA, VLA-4 subunit beta, CD29, ITGB1, FNRB, MDF2, MSK12, Integrin beta 1, CD29, VLAB.

    Product # :

    PRO-1817

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    Description

    ITGB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 462 amino acids (21-461) and having a molecular mass of 51.2 kDa.ITGB1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ITGB1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Integrins are heterodimeric proteins consist of alpha and beta subunits. There are more than 18 alpha and 8 beta subunits discovered in mammals. Integrin family members are membrane receptors that participates in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. ITGB1 encodes a beta subunit.

    • Synonyms

      Integrin beta-1, Fibronectin receptor subunit beta, Glycoprotein IIa, GPIIA, VLA-4 subunit beta, CD29, ITGB1, FNRB, MDF2, MSK12, Integrin beta 1, CD29, VLAB.

    • 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 MQTDENRCLK ANAKSCGECI QAGPNCGWCT NSTFLQEGMP TSARCDDLEA LKKKGCPPDD IENPRGSKDI KKNKNVTNRS KGTAEKLKPE DITQIQPQQL VLRLRSGEPQ TFTLKFKRAE DYPIDLYYLM DLSYSMKDDL ENVKSLGTDL MNEMRRITSD
      FRIGFGSFVE KTVMPYISTT PAKLRNPCTS EQNCTSPFSY KNVLSLTNKG EVFNELVGKQ RISGNLDSPE GGFDAIMQVA VCGSLIGWRN VTRLLVFSTD AGFHFAGDGK LGGIVLPNDG QCHLENNMYT MSHYYDYPSI AHLVQKLSEN NIQTIFAVTE EFQPVYKELK NLIPKSAVGT LSANSSNVIQ LIIDAYNSLS SEVILENGKL SEGVTISYKS YCKNGVNGTG ENGRKCSNIS IGDEVQFEIS ITSNKCPKKD SDSFKIRPLG FTEEVEVILQ YI.

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    Itgb1 Human
  • View Data Sheet

    Name :

    GALK1 Human

    Description:

    Galactokinase 1 Human Recombinant

    Galactose kinase, GK1, GALK, EC 2.7.1.6, GALK1.

    Product # :

    PKA-264

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    Description

    GALK1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 44.4 kDa. The GALK1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GALK1 Human (0.5mg/ml) solution containing 20% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      GALK1 enzyme is needed in the first step of the galactose metabolism pathway.
      (ATP + D-galactose = ADP + alpha-D-galactose 1-phosphate). GALK1 deficinecy lead galactosemia II which is an autosomal recessive deficiency known by congenital cataracts during infancy and presenile cataracts in the adult population. The cataracts are secondary to accumulation of galactitol in the lenses.

    • Synonyms

      Galactose kinase, GK1, GALK, EC 2.7.1.6, GALK1.

    • 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 MAALRQPQVA ELLAEARRAF REEFGAEPEL AVSAPGRVNL IGEHTDYNQG LVLPMALELM TVLVGSPRKD GLVSLLTTSE GADEPQRLQF PLPTAQRSLE PGTPRWANYV KGVIQYYPAA PLPGFSAVVV SSVPLGGGLS SSASLEVATY TFLQQLCPDS GTIAARAQVC QQAEHSFAGM PCGIMDQFIS LMGQKGHALL IDCRSLETSL VPLSDPKLAV LITNSNVRHS LASSEYPVRR RQCEEVARAL GKESLREVQL EELEAARDLV SKEGFRRARH VVGEIRRTAQ AAAALRRGDY RAFGRLMVES HRSLRDDYEV SCPELDQLVE AALAVPGVYG SRMTGGGFGG CTVTLLEASA APHAMRHIQE HYGGTATFYL SQAADGAKVL CL.

    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.

    Galk1 Human
  • View Data Sheet

    Name :

    CXCL2 Human

    Description:

    GRO-Beta Human Recombinant (CXCL2)

    Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    Product # :

    CHM-309

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    Description

    GRO-Beta Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7908 Dalton. The CXCL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Biological Activity

    The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

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    • Introduction

      Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

    • Synonyms

      Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GRO-beta Human 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-Pro-Leu-Ala-Thr.

    • Background

      What is the molecular weight/Mw of CXCL2 HUMAN Protein?
      CXCL2 HUMAN Protein has a total Mw of 7.9kDa.

      What is the source or expression system of CXCL2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL2 HUMAN Protein?
      CXCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL2 HUMAN Protein?
      The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CXCL2 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Leu-Ala-Thr.

      What applications can CXCL2 HUMAN Protein be used in?
      CXCL2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL2 HUMAN Protein?
      The endotoxin level is minimal, CXCL2 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.

    Gro Beta Human
  • View Data Sheet

    Name :

    PSMF1 Human

    Description:

    Proteasome Inhibitor Subunit 1 Human Recombinant

    Proteasome inhibitor PI31 subunit, hPI31, PSMF1, PI31.

    Product # :

    ENZ-224

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    Description

    PSMF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 291 amino acids (1-271) and having a molecular mass of 31.9kDa.PSMF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PSMF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PSMF1 is a protein which hinders the activation of the proteasome by the 11S and 19S regulators. The 26S proteasome is a multicatalytic proteinase complex with an extremely ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is comprised of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits.

    • Synonyms

      Proteasome inhibitor PI31 subunit, hPI31, PSMF1, PI31.

    • 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 MAGLEVLFAS AAPAITCRQD ALVCFLHWEV VTHGYCGLGV GDQPGPNDKK SELLPAGWNN NKDLYVLRYE YKDGSRKLLV KAITVESSMI LNVLEYGSQQ VADLTLNLDD YIDAEHLGDF HRTYKNSEEL RSRIVSGIIT PIHEQWEKAN VSSPHREFPP ATAREVDPLR IPPHHPHTSR QPPWCDPLGP FVVGGEDLDP FGPRRGGMIV DPLRSGFPRA LIDPSSGLPN RLPPGAVPPG ARFDPFGPIG TSPPGPNPDH LPPPGYDDMY L.

    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.

    Psmf1 Human
  • View Data Sheet

    Name :

    CMC4 Human

    Description:

    CX9C Motif Containing 4 Human Recombinant

    C-X(9)-C Motif Containing 4, C-X(9)-C Motif Containing 4 Homolog, Mature T-Cell Proliferation 1 Neighbor Protein, MTCP1NB, MTCP1, Mature T-Cell Proliferation-1 Type A, Protein P8 MTCP-1, p8MTCP1, MTCP-1 Type A, C6.1B.

    Product # :

    PRO-1769

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    Description

    CMC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-68 a.a) and having a molecular mass of 10.4kDa.CMC4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CMC4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CMC4 is a downstream 8kDa protein restricts to mitochondria which was identified by participation in some t(X;14) translocations related with mature T-cell proliferations. This region has a compound gene structure, with a common promoter and 5’ exon spliced to two different groups of 3’ exons which encode 2 separate proteins.

    • Synonyms

      C-X(9)-C Motif Containing 4, C-X(9)-C Motif Containing 4 Homolog, Mature T-Cell Proliferation 1 Neighbor Protein, MTCP1NB, MTCP1, Mature T-Cell Proliferation-1 Type A, Protein P8 MTCP-1, p8MTCP1, MTCP-1 Type A, C6.1B.

    • 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 MGSEFMPQKD PCQKQACEIQ KCLQANSYME SKCQAVIQEL RKCCAQYPKG RSVVCSGFEK EEEENLTRKS ASK

    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.

    Cmc4 Human
  • View Data Sheet

    Name :

    HSF1 Antibody

    Description:

    Heat Shock Transcription Factor-1, Mouse Anti Human

    HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.

    Product # :

    ANT-328

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    • More Info

    Formulation

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

    More Info

    • Introduction

      The transcription of heat-shock genes is rapidly induced after temperature stress in response to environmental changes, and it is also involved in oogenesis, spermatogenesis, and placental development. Hsp90, is a major repressor of HSF1 gene. HSF1 is known for its participation in heat shock response. HSF1 protein regulates the transcription of hundreds of targets, such as genes involved in protein folding, detoxification, energy generation, carbohydrate metabolism, and cell wall organization. HSF1 binds to MTA1 in vitro & in breast carcinoma. Suppression of estrogen-dependent transcription may contribute to role of HSF1 in cancer. Human cancer lines of diverse origins express higher dependence on HSF1 function to maintain proliferation and survival than their non-transformed counterparts. HSF1 induces anticoagulation and relaxation factors in vascular endothelial cells and could therefore be used to treat cardiovascular disease. HSF1 is directly involved in the regulation of HO1 havi

    • Synonyms

      HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.

    • Immunogen

      Anti-human HSF1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSF1 amino acids 1-529 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PJ7F9AT.

    • Applications

      HSF1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      HSF1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Hsf1 Antibody
  • View Data Sheet

    Name :

    Streptavidin Antibody

    Description:

    Streptavidin, Mouse Antibody

    Product # :

    ANT-345

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    Formulation

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

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    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti Streptavidin mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant Streptavidin amino acids 25-183 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      P1C2AT.

    • Applications

      Streptavidin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Antibody Monoclonal.

    • Storage Procedures

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

    • Purification Method

      Streptavidin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Streptavidin Antibody
  • View Data Sheet

    Name :

    Leptin tA Mouse

    Description:

    Leptin Antagonist Triple Mutant Mouse Recombinant

    Product # :

    CYT-354

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    Description

    Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    ProSpec’s Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting Leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • 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 quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Mouse
  • View Data Sheet

    Name :

    KRT18 Human

    Description:

    Cytokeratin 18 Human Recombinant

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    PRO-349

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    Description

    Cytokeratin 18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a calculated molecular mass of 48,201 Dalton, showing a 45kDa band on SDS-page, pI-5.7.The KRT18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

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

    More Info

    • Introduction

      KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CK-18 although stable at room temperature for 3 weeks, should be stored between 2-8°C. Upon reconstitution CK-18 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 1mg CK-18 in sterile 18MΩ-cm H2O not less than 700µl, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

      Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

    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.

    Krt18 Human
  • View Data Sheet

    Name :

    KRT20 Human

    Description:

    Cytokeratin 20 Human Recombinant

    Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.

    Product # :

    PRO-351

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    Description

    Cytokeratin 20 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain having a molecular mass of 48,553 Dalton. The KRT20 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/1ml) was lyophilized after from a sterile solution containing 30mM Tris-HCL pH-8, 9.5M urea, 2mM DDT, 2mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KRT20 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21.

    • Synonyms

      Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KRT20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT20 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 KRT20 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Reconstitution to filaments

      Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5 M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4 M urea and then to low salt condition (50 mM NaCI, 2 mM dithiothreitol, 10 mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

    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.

    Krt20 Human
  • View Data Sheet

    Name :

    GM-CSF Rat

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Rat Recombinant

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    Product # :

    CYT-395

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14590.65 Dalton. GM-CSF Rat Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF Rat was lyophilized with no additives.

    Purity

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

    Biological Activity

    The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI

      QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE

      VTTFEDFIKN LKGFLFDIPF DCWKPVQK.

    • Background

      What is the molecular weight/Mw of GM-CSF RAT Protein?
      GM-CSF RAT Protein has a total Mw of 14.59kDa.

      What is the source or expression system of GM-CSF RAT Protein?
      Escherichia Coli.

      What is the Purity of GM-CSF RAT Protein?
      GM-CSF RAT Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF RAT Protein?
      The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.

      What is the amino acid sequence of GM-CSF RAT Protein?
      MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
      QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
      VTTFEDFIKN LKGFLFDIPF DCWKPVQK.

      What applications can GM-CSF RAT Protein be used in?
      GM-CSF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GM-CSF RAT Protein?
      The endotoxin level is minimal, GM-CSF 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.

    Gm Csf Rat
  • View Data Sheet

    Name :

    Buserelin

    Description:

    Buserelin

    Product # :

    HOR-255

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    Description

    Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.

    Formulation

    The Buserelin peptide was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Buserelin
  • View Data Sheet

    Name :

    GDF3 Human

    Description:

    Growth Differentiation Factor-3 Human Recombinant

    Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

    Product # :

    CYT-694

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    Description

    GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated solution (0.5mg/ml) containing 30mM Acetate buffer pH-4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.

    • Synonyms

      Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF3 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 GDF3 in sterile 100mM Acetate buffer pH-4 at a concentration of 0.5mg/ml. For the dilution into higher pH values, it is recommended to dilute the protein to a concentration of 10μg/ml. Please note that in higher concentrations the solubility of GDF3 is limited. The protein is not sterile! Please sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

    • Background

      What is the molecular weight/Mw of GDF3 HUMAN Protein?
      GDF3 HUMAN Protein has a total Mw of 14.15XkDa.

      What is the source or expression system of GDF3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GDF3 HUMAN Protein?
      GDF3 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF3 HUMAN Protein?
      The biological functionality of GDF3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GDF3 HUMAN Protein?
      MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

      What applications can GDF3 HUMAN Protein be used in?
      GDF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF3 HUMAN Protein?
      The endotoxin level is minimal, GDF3 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.

    Gdf3 Human
  • View Data Sheet

    Name :

    SEMAX

    Description:

    SEMAX

    Product # :

    HOR-033

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    Description

    SEMAX Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 813.92 Dalton and a Molecular formula of C37H51N19O1S.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-Met-Glu-His-Phe-Pro-Gly-Pro-OH.

    • Background

      Semax, also known as ACTH(4-10) Pro-Gly-Pro, is a synthetic peptide that has been the subject of extensive research due to its potential neuroprotective and nootropic effects. This heptapeptide, derived from the adrenocorticotropic hormone (ACTH), has been shown to possess a wide range of biological activities, including enhancing memory, learning, and neurogenesis.

      Semax is unique in its ability to cross the blood-brain barrier and exert its effects directly on the central nervous system. It has been shown to stimulate the release of brain-derived neurotrophic factor (BDNF), a protein that plays a crucial role in the survival of neurons and the growth of new neurons and synapses. Studies by Dolotov et al. (2006) have demonstrated that Semax can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.

      In addition to its nootropic effects, Semax has been shown to possess neuroprotective properties. Research by Stavchansky et al. (2008) found that Semax could protect neurons from oxidative stress and apoptosis, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

      Given its nootropic and neuroprotective effects, Semax has been proposed as a potential therapeutic agent for a variety of conditions, including cognitive disorders, stroke, and optic nerve disease. For instance, a study by Myasoedov et al. (2010) found that Semax could improve outcomes in patients with ischemic stroke, indicating its potential as a therapeutic agent in stroke recovery.

      While research on Semax is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of Semax in humans. However, the existing body of research suggests that Semax could be a promising tool in the treatment of cognitive disorders and neurodegenerative diseases.

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

    Semax
  • View Data Sheet

    Name :

    Ipamorelin

    Description:

    Ipamorelin

    Ipamorelin

    Product # :

    HOR-024

    Price :

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    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    • description
    • formulation
    • purity
    • More Info

    Description

    Ipamorelin Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 711.85 Dalton and a Molecular formula of C38H49N9O5.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Ipamorelin is a peptide selective agonist of the ghrelin/growth hormone secretagogue receptor and a growth hormone secretagogue. Ipamorelin is a pentapeptide that was derived from GHRP1. Ipamorelin significantly increases plasma growth hormone levels in both animals and humans. Like pralmorelin and GHRP-6, ipamorelin does not affect prolactin, FSH, LH or TSH levels. However, unlike GHRP2 and GHRP6, but as growth hormone-releasing hormone (GHRH), ipamorelin does not stimulate the secretion of adrenocorticotropic hormone (ACTH) or cortisol, and is highly selective for inducing the secretion only of GH.

    • Synonyms

      Ipamorelin

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Aib-His-D-2-Nal-D-Phe-Lys-NH2.

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

    Ipamorelin
  • View Data Sheet

    Name :

    CEA Protein

    Description:

    Carcinoembryonic Antigen Human

    CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    Product # :

    PRO-2801

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.

    Source

    Liver tissue.

    Formulation

    CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal 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.

    • Applications

      Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.

    • Background

      Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.

      Structural Complexity of CEA:

      CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.

      CEA in Cancer Biology:

      CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.

      Beyond Cancer: CEA in Development and Inflammation:

      While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.

      CEA as a Diagnostic and Therapeutic Target:

      The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.

    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.

    Cea Human
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