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Search results

1000 results found for “Prolactin PRL”

Name

Description

Product #

Price

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  • 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

    Price :

    Quantity :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info

    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 :

    PCSK1N Human

    Description:

    Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant

    ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    Product # :

    PRO-1819

    Price :

    Quantity :

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    Description

    PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.

    • Synonyms

      ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    • 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 MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP P.

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

    Pcsk1N Human
  • View Data Sheet

    Name :

    ProMatrilysin

    Description:

    ProMatrix Metalloproteinase-7 Recombinant

    Product # :

    ENZ-272

    Price :

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    • description
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    • biological activity
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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Physical Appearance

      Sterile clear liquid solution.

    • Stability

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

    • Unit Definition

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

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

    Promatrilysin
  • View Data Sheet

    Name :

    GH Antagonist Rat

    Description:

    Growth Hormone Anatagonist Rat Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-1250

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    Rat Growth Hormone Anatagonist produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. GH Antagonist Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

    Greater than 98.0% as determined by:

    (a) Analysis by RP-HPLC

    (b) Analysis by Gel Filtration.

    (c) Analysis by SDS-PAGE.

    Biological Activity

    Plays a role as antagonist using an in vitro bioassay in PDF-P1 3B9 cells stably transfected with rabbit GH receptors. It is capable of forming a 1:1 complex with the recombinant ovine growth hormone receptor extracellular domain and binds to this ECD with affinity similar the the wild type rGH.

    More Info

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH Antagonist Rat although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GH Antagonist Rat in 0.4% NaHCO3 or water adjusted to pH 9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

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

    • Background

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with 4 other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which was evolved by a series of gene duplications. The 5 genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the 5 growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other 4 genes in the growth hormone locus.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman analysis program of protein sequences.

    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.

    Growth Hormone Antagonist Rat
  • View Data Sheet

    Name :

    PLGF3 Human

    Description:

    Placental Growth Factor-3 Human Recombinant

    Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

    Product # :

    CYT-969

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
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    • More Info

    Description

    PLGF3 Human Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2x204 amino acids and having a total molecular mass of 45.8kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.

    • Synonyms

      Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PLGF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF-3 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 PLGF-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLPAVPPQQW ALSAGNGSSE VEVVPFQEVW GRSYCRALER LVDVVSEYPS EVEHMFSPSC VSLLRCTGCC GDENLHCVPV ETANVTMQLL KIRSGDRPSY VELTFSQHVR CECRHSPGRQ SPDMPGDFRA DAPSFLPPRR SLPMLFRMEW GCALTGSQSA VWPSSPVPEE IPRMHPGRNG KKQQRKPLRE KMKPERCGDA VPRR.

    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.

    Human Plgf3
  • View Data Sheet

    Name :

    Globular Adiponectin Human

    Description:

    Globular Adiponectin Human Recombinant

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-615

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    Description

    gAcrp30 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 145 amino acids and having a molecular mass of 16.7kDa. The gAcrp30 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 10mM sodium phosphate & 0.5mM DTT, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.

    More Info

    • Introduction

      gAcrp30 globular protein, exists as a result of proteolytic processing of adiponectin. Adiponectin is manufactured and secreted solely by adipocytes, and is a highly obtained plasma protein, accounting for up to 0.05% of total serum protein. Similar to Adiponectin, gAcrp30 is able of lowering hyperglycemia and reversing INS resistance. In addition, gAcrp30 is an significant protein that is involved in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids. AdipoR1 & AdipoR2 are the 2 signaling receptors for adiponectin and gAcrp30 that were recently been identified.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Stability

      For long term, store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time two weeks.

    • Solubility

      We recommended reconstituting gAcrp30 at a concentration of 0.1mg per ml with 10mM sodium phosphate & 0.5mM DTT, pH 7.5. which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

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

      What is the Biological Activity of ADIPONECTIN Protein?
      gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.

      What is the amino acid sequence of ADIPONECTIN Protein?
      MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.

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

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

    Globular Adiponectin Human
  • View Data Sheet

    Name :

    PROCR Human

    Description:

    Protein-c Receptor Human Recombinant

    Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA

    Product # :

    PRO-1938

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    Description

    PROCR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (18-210) and having a molecular mass of 24.4 kDa.PROCR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PROCR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein-c Receptor (PROCR) is a receptor for activated protein C, a serine protease activated by and involved in the blood coagulation pathway. The PROCR protein is an N-glycosylated type I membrane protein which enhances the activation of protein C. PROCR gene mutations are linked with venous thromboembolism and myocardial infarction, as well as with late fetal loss during pregnancy. In addition, PROCR may have a role in malarial infection and has been linked with cancer.

    • Synonyms

      Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA

    • 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 MGSSQDASDG LQRLHMLQIS YFRDPYHVWY QGNASLGGHL THVLEGPDTN TTIIQLQPLQ EPESWARTQS GLQSYLLQFH GLVRLVHQER TLAFPLTIRC FLGCELPPEG SRAHVFFEVA VNGSSFVSFR PERALWQADT QVTSGVVTFT LQQLNAYNRT RYELREFLED TCVQYVQKHI SAENTKGSQT SRSYTS.

    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.

    Procr Human
  • View Data Sheet

    Name :

    S100A6 Human

    Description:

    S100 Calcium Binding Protein A6 Human Recombinant

    Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

    Product # :

    PRO-148

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    Description

    S100A6 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 110 amino acids (1-90 a.a.) and having a molecular mass of 12.3kDa. The S100A6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A6 function in stimulation of prolactin secretion and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

    • Synonyms

      Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

    • 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 MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG.

    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.

    S100A6 Human
  • View Data Sheet

    Name :

    Protein-L, His

    Description:

    Protein L Recombinant, His Tag

    Product # :

    PRO-1930

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    Description

    Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 372 amino acids in total and having a molecular mass of 41.5kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AG.

    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.

    Protein L His
  • View Data Sheet

    Name :

    Leptin Human, PEG

    Description:

    Leptin Human Recombinant, PEG

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1108

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    Description

    Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.

    More Info

    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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 Pegylated leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • 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 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 Mutant
  • View Data Sheet

    Name :

    FGL1 Human

    Description:

    Fibrinogen Like 1 Human Recombinant

    Fibrinogen-like protein 1, HP-041, Hepassocin, Hepatocyte-derived fibrinogen-related protein 1, HFREP-1, Liver fibrinogen-related protein 1, LFIRE-1, FGL1, HFREP1.

    Product # :

    PRO-2580

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    Description

    FGL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 23-312) containing 300 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 35.3kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    FGL1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in in 100 mM carbonate buffer, pH 9.2.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FGL1 belongs to the fibrinogen family. Fibrinogen Like 1 is homologous to the carboxy terminus of the fibrinogen beta- and gamma- subunits which comprises the 4 conserved cysteines of fibrinogens and fibrinogen related proteins. FGL1 lacks the platelet-binding site, cross-linking region and a thrombin-sensitive site which are necessary for fibrin clot formation. Fibrinogen takes part in the development of hepatocellular carcinomas.

    • Synonyms

      Fibrinogen-like protein 1, HP-041, Hepassocin, Hepatocyte-derived fibrinogen-related protein 1, HFREP-1, Liver fibrinogen-related protein 1, LFIRE-1, FGL1, HFREP1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FGL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS LEDCAQEQMR LRAQVRLLET RVKQQQVKIK QLLQENEVQF LDKGDENTVI DLGSKRQYAD CSEIFNDGYK LSGFYKIKPL QSPAEFSVYC DMSDGGGWTV IQRRSDGSEN FNRGWKDYEN GFGNFVQKHG EYWLGNKNLH FLTTQEDYTL KIDLADFEKN SRYAQYKNFK VGDEKNFYEL NIGEYSGTAG DSLAGNFHPE VQWWASHQRM KFSTWDRDHD NYEGNCAEED QSGWWFNRCH SANLNGVYYS GPYTAKTDNG IVWYTWHGWW YSLKSVVMKI RPNDFIPNVI.

    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.

    Fgl1 Human
  • View Data Sheet

    Name :

    GHBP Rat

    Description:

    GH Binding Protein Rat Recombinant

    GHBP, GH receptor.

    Product # :

    CYT-933

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    Description

    GHBP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 255 amino acids (19-265.a.) and having a molecular mass of 29.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).GHBP is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GH receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, GH performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

    • Synonyms

      GHBP, GH receptor.

    • 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

      FPGSGATPAT LGKASPVLQR INPSLRESSS GKPRFTKCRS PELETFSCYW TEGDDHNLKV PGSIQLYYAR RIAHEWTPEW KECPDYVSAG ANSCYFNSSY TSIWIPYCIK LTTNGDLLKE KCFTVDEIVQ PDPPIGLNWT LLNISLPGIR GDIQVSWQPP PSADVLKGWI ILEYEIQYKE VNETKWKTMS PIWSTSVPLY SLRLDKEHEV RVRSRQRSFE KYSEFSEVLR VTFPQMDTLA ACEEDFRLEH HHHHH.

    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.

    Ghr Rat
  • View Data Sheet

    Name :

    Globular Adiponectin Human, His

    Description:

    Adiponectin Globular Recombinant, His Tag

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-277

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    Description

    Acrp30 Human has a total of 171 amino acids. N-terminal underlined amino acids are His-tag and the protease cleavage site (31AA-Underlined). The AA sequence of Acrp30 Human is homologous to the 105-244 amino acid sequence of the Human full-length Adiponectin (Swiss-prot entry Q15848).

    Source

    Escherichia Coli.

    Formulation

    Acrp30 Human is a filtered powder, lyophilized from 0.6mg/ml in PBS buffer.

    Purity

    Purity of Acrp30 Human is greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      Adiponectin is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Stability

      For long term, store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized Acrp30 Human remains stable for 24 months when stored at -20°C.

    • Solubility

      Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.

    • Amino Acid Sequence

      MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

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

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

    Gacrp30 Human His
  • View Data Sheet

    Name :

    Gly m 4.0101

    Description:

    Stress-Induced Protein SAM22 Recombinant

    Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    Product # :

    PRO-2278

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    Description

    Recombinant Stress-Induced Protein SAM22 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 19,484 Dalton. Gly m 4.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Gly m 4.0101 is supplied in in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.

    • Synonyms

      Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Gly M 40101
  • View Data Sheet

    Name :

    ANGPTL3 Human

    Description:

    Angiopoietin Like Protein 3 Human Recombinant

    Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.

    Product # :

    CYT-248

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    Description

    The ANGPTL3 Human Recombinant is produced with N-terminal fusion of His-Tag. The Angiopoietin-like protein 3 His Tagged Fusion Protein is 26kDa containing 207 amino acid residues of the ANGPTL3 Human (26-233 a.a.) and 16 additional amino acid residues – His-Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    ANGPTL3 Human filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Angiopoietin 5 purity is greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.

    • Synonyms

      Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.

    • Stability

      Store lyophilized ANGPTL3 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Angiopoietin 5 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add 0.1M Acetate buffer pH-4 and let the lyophilized pellet of ANGPTL3 Human dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of Angiopoietin 5 is limited.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAP.

    • Background

      Angiopoietin-Like Protein 3 Human Recombinant: An Emerging Target in Metabolic and Cardiovascular Disorders

      Abstract:


      Angiopoietin-like protein 3 (ANGPTL3) is a key regulator of lipid metabolism and has garnered considerable attention for its involvement in metabolic and cardiovascular disorders. ANGPTL3 plays a crucial role in lipid homeostasis, including the regulation of triglycerides, cholesterol, and lipoprotein metabolism. The availability of human recombinant ANGPTL3 protein has provided a valuable tool for investigating its biological functions and therapeutic potential. This review aims to provide a comprehensive overview of the role of ANGPTL3 in metabolic disorders, cardiovascular diseases, and lipid metabolism, highlighting the potential of ANGPTL3 human recombinant protein as a therapeutic target.

      Introduction:


      Metabolic disorders, such as dyslipidemia and obesity, significantly contribute to the development of cardiovascular diseases. ANGPTL3, a member of the angiopoietin-like protein family, has emerged as a key player in lipid metabolism and cardiovascular health. ANGPTL3 regulates lipoprotein metabolism, affecting triglyceride-rich lipoproteins, low-density lipoproteins (LDL), and high-density lipoproteins (HDL).

      Molecular Mechanisms of ANGPTL3 Action:


      ANGPTL3 exerts its effects through inhibition of lipoprotein lipase (LPL) and endothelial lipase (EL), key enzymes involved in lipoprotein metabolism. By inhibiting LPL and EL activities, ANGPTL3 increases plasma triglyceride and LDL cholesterol levels. ANGPTL3 also influences hepatic cholesterol metabolism and HDL metabolism through modulation of the receptor-mediated uptake of lipoproteins.

      Role of ANGPTL3 in Metabolic Regulation:


      ANGPTL3 plays a critical role in metabolic regulation, particularly in lipid metabolism and dyslipidemia. Loss-of-function mutations in the ANGPTL3 gene result in decreased plasma triglycerides, LDL cholesterol, and total cholesterol levels, highlighting the potential therapeutic relevance of ANGPTL3 inhibition. Conversely, elevated ANGPTL3 levels are associated with increased cardiovascular risk and atherogenic lipid profiles.

      ANGPTL3 in Cardiovascular Health and Disease:


      ANGPTL3 has emerged as a key modulator of cardiovascular diseases, including atherosclerosis and coronary artery disease. ANGPTL3 influences vascular endothelial function, inflammation, and plaque formation through its effects on lipoprotein metabolism and lipid accumulation. Inhibition of ANGPTL3 has shown promising results in preclinical studies, reducing atherosclerosis and improving cardiovascular outcomes.

      Therapeutic Potential of ANGPTL3 Human Recombinant Protein:


      The development of ANGPTL3 human recombinant protein provides a novel avenue for therapeutic interventions targeting metabolic and cardiovascular disorders. Inhibition of ANGPTL3 using monoclonal antibodies or other approaches has demonstrated efficacy in lowering plasma lipid levels, particularly triglycerides and LDL cholesterol. Clinical trials investigating the safety and efficacy of ANGPTL3 inhibition are underway.

      Conclusion:


      ANGPTL3 is a key regulator of lipid metabolism and a promising therapeutic target for metabolic and cardiovascular disorders. The availability of ANGPTL3 human recombinant protein has facilitated in-depth investigations into its biological functions and therapeutic potential. Targeting ANGPTL3 holds promise for improving lipid profiles, reducing cardiovascular risk, and managing metabolic disorders.

      What is the molecular weight/Mw of ANGPTL3 Protein?
      ANGPTL3 Protein has a total Mw of 26kDa.

      What is the source or expression system of ANGPTL3 Protein?
      Escherichia Coli.

      What is the Purity of ANGPTL3 Protein?
      ANGPTL3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of ANGPTL3 Protein?
      The biological functionality of ANGPTL3 Protein will be determined in the future.

      What is the amino acid sequence of ANGPTL3 Protein?
      MRGSHHHHHH GMASHMSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAP.

      What applications can ANGPTL3 Protein be used in?
      ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ANGPTL3 Protein?
      The endotoxin level is minimal, ANGPTL3 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.

    Angptl3 Human
  • View Data Sheet

    Name :

    Pleiotrophin Human, His

    Description:

    Pleiotrophin Human Recombinant, His Tag

    PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

    Product # :

    CYT-451

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    Description

    Pleiotrophin Human Recombinant contains His-Tagged Fusion Protein, produced in E. coli, its molecular weight is 17.3 kDa protein containing 136 amino acid residues of the OSF-1 human and 16 additional amino acid residues - HisTag, thrombin cleavage site (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5 mg/ml in 0.1M phosphate buffer and 0.1M NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pleiotrophin (Osteoblast-Specific Factor-1, OSF-1) contains 136 amino acid residues. The sequence is very rich in cationic amino acids (24% of the residues); lysine cluster sequences are found in the N-terminal and C-terminal ends of the structure.
      The OSF-1 gene was shown by Northern blotting analysis to be expressed in mouse calvarial osteoblast-enriched cells and in mouse brain tissues, but not in thymus, spleen, kidney, liver, lung, testis or heart. Pleiotrophin has the ability to promote adhesion, migration, expansion, and differentiation of human osteoprogenitor cells. In addition to certain types of cancer, the embryonic growth and differentiation factor pleiotrophin is found also in adults in inflammatory diseases. In osteoarthritis, pleiotrophin is especially expressed in early stages, and its concentrations in the synovial fluid could serve as a marker for the progress of the disease. Pleitrophin might be involved in cartilage repair in osteoarthritis, in particular, in earlier stages.

    • Synonyms

      PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add PBS pH 7.2 and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHHM LVPRGSGKKE KPEKKVKKSD CGEWQWSVCV PTSGDCGLGT REGTRTGAEC KQTMKTQRCK IPCNWKKQFG AECKYQFQAW GECDLNTALK TRTGSLKRAL HNAECQKTVT ISKPCGKLTK PKPQAESKKK KKEGKKQEKM LD.

    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.

    Pleiotrophin Human
  • View Data Sheet

    Name :

    LGALS2 Mouse, Active

    Description:

    Galectin-2, BioActive Mouse Recombinant

    Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.

    Product # :

    CYT-1155

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    Description

    LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.

    More Info

    • Introduction

      Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.

    • Synonyms

      Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.

    • 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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE

    • Background

      What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
      LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.

      What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
      Escherichia Coli.

      What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
      LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
      Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.

      What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.

      What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
      LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
      The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE 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.

    Galectin 2 Mouse
  • View Data Sheet

    Name :

    SHBG Protein

    Description:

    Sex Hormone-Binding Globulin Human

    Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.

    Product # :

    PRO-2757

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    Description

    SHBG is a protein of approximately 45kD.

    Source

    Human serum.

    Formulation

    The protein is supplied in 0.01M HEPES, PH 7.4 and 0.15M NaCl.

    More Info

    • Introduction

      Sex-hormone-binding globulin (SHBG) is a beta-globulin which specifically binds steroid hormones; it is involved in the transport of sex steroids in plasma. The main site of SHBG synthesis is assumed to be the hepatocytes. The production of SHBG is regulated by androgen/estrogen balance, thyroid hormones, insulin and dietary factors, among others. The concentration of SHBG is a key factor regulating their distribution between protein-bound and free states. SHBG concentration determination is primarily significant in the evaluation of mild disorders of androgen metabolism and it allows detection of women with hirsutism who are likely to react to estrogen therapy. Testosterone/SHBG-ratios correlate well with both measured and calculated values for free testosterone thus aid to distinguish between subjects with excessive androgen activity and normal individuals. SHBG gene polymorphisms are linked with polycystic ovary syndrome and type 2 diabetes mellitus.

    • Synonyms

      Sex hormone-binding globulin, SHBG, Sex steroid-binding protein, SBP, Testis-specific androgen-binding protein, ABP, Testosterone-estradiol-binding globulin, TeBG, Testosterone-estrogen-binding globulin, SHBG.

    • Physical Appearance

      Streile filtered colorless solution.

    • Stability

      Upon arrival, Store at -20°C. Please prevent freeze-thaw cycles.

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, Parvovirus B19, HBc, HBV, HIV and Syphilis.

    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.

    Shbg Protein
  • View Data Sheet

    Name :

    S100A6 Mouse

    Description:

    S100 Calcium Binding Protein A6 Mouse Recombinant

    Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.

    Product # :

    PRO-240

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    Description

    S100A6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89 a.a) and having a molecular mass of 12.2kDa.S100A6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.
      S100A6 may function in stimulation prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

    • Synonyms

      Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.

    • 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 MACPLDQAIG LLVAIFHKYS GKEGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMDDL DRNKDQEVNF QEYVAFLGAL ALIYNEALK.

    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.

    S100A6 Mouse
  • View Data Sheet

    Name :

    NECTIN1 Human

    Description:

    Nectin Cell Adhesion Molecule 1 Human Recombinant

    PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.

    Product # :

    PRO-2648

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    Description

    NECTIN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 334amino acids (31-355a.a) and having a molecular mass of 37.3kDa.NECTIN1 is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The NECTIN1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.

    • Synonyms

      PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.

    • 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

      ADPQVVQVND SMYGFIGTDV VLHCSFANPL PSVKITQVTW QKSTNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSRLELE DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL
      TCKADANPPA TEYHWTTLNG SLPKGVEAQN RTLFFKGPIN YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAHH HHHH

    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.

    Nectin1 Human
  • View Data Sheet

    Name :

    Thymosin β4

    Description:

    Thymosin-b4 Human Recombinant

    Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.

    Product # :

    HOR-003

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    Description

    Thymosin b4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 43 amino acids and having a molecular mass of 4.9kDa.The Thymosin b4 Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2um filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    More Info

    • Introduction

      CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.

    • Synonyms

      Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin B4 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymosin B4 Human 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 Thymosin B4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES

    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.

    Thymosin B4
  • View Data Sheet

    Name :

    CTLA4 Human, Sf9

    Description:

    Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant, Sf9

    Cytotoxic T-Lymphocyte Associated Protein 4, Cytotoxic T-Lymphocyte-Associated Protein 4, Insulin-Dependent Diabetes Mellitus 12, Celiac Disease 3, CTLA-4, CD152, Ligand And Transmembrane Spliced Cytotoxic T Lymphocyte Associated Antigen 4, Cytotoxic T Lymphocyte Associated Antigen 4 Short Spliced Form, Cytotoxic T-Lymphocyte-Associated Serine Esterase-4, Cytotoxic T-Lymphocyte-Associated Antigen 4, CD152 Isoform, CD152 Antigen, CELIAC3, IDDM12, ALPS5, GRD4, GSE, CD, Cytotoxic T-lymphocyte protein 4, CTLA4.

    Product # :

    CYT-952

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    • sds-page

    Description

    CTLA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 135 amino acids (36-161a.a.) and having a molecular mass of 14.6kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). CTLA4 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTLA4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Determined by IL-2 ELISA via Jurkat human acute T cell leukemia cells. The ED50 range ≤ 150 ng/ml with Human B7-1/CD80.

    sds-page

    CTLA4-sds-page - Product image 1

    More Info

    • Introduction

      CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.

    • Synonyms

      Cytotoxic T-Lymphocyte Associated Protein 4, Cytotoxic T-Lymphocyte-Associated Protein 4, Insulin-Dependent Diabetes Mellitus 12, Celiac Disease 3, CTLA-4, CD152, Ligand And Transmembrane Spliced Cytotoxic T Lymphocyte Associated Antigen 4, Cytotoxic T Lymphocyte Associated Antigen 4 Short Spliced Form, Cytotoxic T-Lymphocyte-Associated Serine Esterase-4, Cytotoxic T-Lymphocyte-Associated Antigen 4, CD152 Isoform, CD152 Antigen, CELIAC3, IDDM12, ALPS5, GRD4, GSE, CD, Cytotoxic T-lymphocyte protein 4, CTLA4.

    • 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

      ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDH HHHHH.

    • Background

      What is the molecular weight/Mw of CTLA4 Protein?
      CTLA4 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of CTLA4 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CTLA4 Protein?
      CTLA4 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTLA4 Protein?
      Determined by IL-2 ELISA via Jurkat human acute T cell leukemia cells. The ED50 range ≤ 150 ng/ml with Human B7-1/CD80.


      What is the amino acid sequence of CTLA4 Protein?
      ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDH HHHHH.

      What applications can CTLA4 Protein be used in?
      CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTLA4 Protein?
      The endotoxin level is minimal, CTLA4 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.

    Ctla4 Human Sf9
  • View Data Sheet

    Name :

    HERC5 Human

    Description:

    HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant

    HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.

    Product # :

    ENZ-797

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    • description
    • source
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    Description

    HERC5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (681-1024 a.a.) and having a molecular mass of 43kDa. HERC5 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    HERC5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 (HERC5) is a member of the HERC family of ubiquitin ligases, found in a cluster of HERC family genes on chromosome 4. HERC5 is a protein with a HECT domain and 5 RCC1 repeats. The HERC5 protein localizes to the cytoplasm and perinuclear region and serves as an INF-induced E3 protein ligase that mediates ISGylation of protein targets. HERC5 exhibits antiviral activity towards HIV-1, influenza A virus and human papillomavirus. HERC5 is a major E3 ligase for ISG15 conjugation. HERC5 also serves as a positive regulator of innate antiviral response in cells induced by INF. Pro-inflammatory cytokines upregulate HERC5 in endothelial cells. HERC5 is physically connected with polyribosomes, broadly modifies recently synthesized proteins in a cotranslational fashion.

    • Synonyms

      HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSFDLTVRR NHLIEDVLNQ LSQFENEDLR KELWVSFSGE IGYDLGGVKK EFFYCLFAEM IQPEYGMFMY PEGASCMWFP VKPKFEKKRY FFFGVLCGLS LFNCNVANLP FPLALFKKLL DQMPSLEDLK ELSPDLGKNL QTLLDDEGDN FEEVFYIHFN VHWDRNDTNL IPNGSSITVN QTNKRDYVSK YINYIFNDSV KAVYEEFRRG FYKMCDEDII KLFHPEELKD VIVGNTDYDW KTFEKNARYE PGYNSSHPTI VMFWKAFHKL TLEEKKKFLV FLTGTDRLQM KDLNNMKITF CCPESWNERD PIRALTCFSV LFLPKYSTME TVEEALQEAI NNNRGFG.

    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.

    Herc5 Human
  • View Data Sheet

    Name :

    NCALD Human

    Description:

    Neurocalcin Delta Recombinant Human

    Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.

    Product # :

    PRO-093

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    Description

    NCALD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-193.a.a) and having a molecular mass of 24.4kDa. NCALD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NCALD protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCALD belongs to the neuronal calcium sensor (NCS) family. NCALD is cytosolic at inactive calcium levels; but, high intracellular calcium levels induce a conformational transformation which exposes the myristoyl group, causing protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is a regulator of signal transduction by G protein-coupled receptor.

    • Synonyms

      Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.

    • 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 MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA GQF.

    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.

    Ncald Human
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