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Search results

1000 results found for “mumps”

Name

Description

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  • View Data Sheet

    Name :

    DTYMK Human

    Description:

    Deoxythymidylate Kinase Human Recombinant

    Deoxythymidylate Kinase (Thymidylate Kinase), DTMP Kinase, CDC8, TMPK, TYMK, Thymidylate (DTMP) Kinase, EC 2.7.4.9, PP3731, Thymidylate kinase.

    Product # :

    PKA-005

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    Description

    DTYMK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212 a.a) and having a molecular mass of 26kDa. DTYMK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    DTYMK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymidylate kinase (DTYMK) is involved in pyrimidine metabolism. Specifically, DTYMK catalyzes the ATP-dependent conversion of dTMP (deoxythymidine monophosphate) to dTDP (deoxythymidine diphosphate), which then acts as one of the 4 nucleotides in DNA. Through its role in the catalytic creation of dTDP, DTYMK has an imperative role in the pathway of DNA synthesis and is assumed to be involved in cell cycle progression and cell growth.

    • Synonyms

      Deoxythymidylate Kinase (Thymidylate Kinase), DTMP Kinase, CDC8, TMPK, TYMK, Thymidylate (DTMP) Kinase, EC 2.7.4.9, PP3731, Thymidylate kinase.

    • 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 MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA SKSIEAVHED IRVLSEDAIR TATEKPLGEL WK.

    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.

    Dtymk Human
  • View Data Sheet

    Name :

    NIPSNAP1 Human

    Description:

    Nipsnap Homolog 1 Human Recombinant

    Nipsnap Homolog 1 (C. Elegans), 4 Nitrophenylphosphatase Domain And Non-Neuronal SNAP25-Like 1, NIPSNAP, C. Elegans, Homolog, Protein NipSnap Homolog 1, NipSnap1.

    Product # :

    PRO-1745

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    Description

    NIPSNAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-284a.a) and having a molecular mass of 35.7kDa.NIPSNAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NIPSNAP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nipsnap Homolog 1 (NIPSNAP1) belongs to the NipSnap family. NIPSNAP1 may take part in vesicular transport. A similar protein in mice inhibits the calcium channel TRPV6, and it is localized to the inner mitochondrialmembrane as well, where it may be involved in mitochondrial DNA maintenance. A pseudogene of NIPSNAP1 is located onthe short arm of chromosome 17. Among the diseases associated with NIPSNAP1 are maple syrup urine disease, and phenylketonuria.

    • Synonyms

      Nipsnap Homolog 1 (C. Elegans), 4 Nitrophenylphosphatase Domain And Non-Neuronal SNAP25-Like 1, NIPSNAP, C. Elegans, Homolog, Protein NipSnap Homolog 1, NipSnap1.

    • 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 MGSMAPRLCS ISVTARRLLG GPGPRAGDVA SAAAARFYSK DNEGSWFRSL FVHKVDPRKD AHSTLLSKKE TSNLYKIQFH NVKPEYLDAY NSLTEAVLPK LHLDEDYPCS LVGNWNTWYG EQDQAVHLWR FSGGYPALMD CMNKLKNNKE YLEFRRERSQMLLSRRNQLL LEFSFWNEPQ PRMGPNIYEL RTYKLKPGTM IEWGNNWARA IKYRQENQEA VGGFFSQIGE LYVVHHLWAY KDLQSREETR NAAWRKRGWD ENVYYTVPLV RHMESRIMIP LKISPLQ

    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.

    Nipsnap1 Human
  • View Data Sheet

    Name :

    CCL28 Human

    Description:

    Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28)

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

    Product # :

    CHM-353

    Price :

    Quantity :

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    • source
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    • More Info

    Description

    CCL28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids and having a molecular mass of 12.3 kDa. The CCL28 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM PBS and 150mM NaCl.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    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 CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.

    • Background

      What is the molecular weight/Mw of CCL28 HUMAN Protein?
      CCL28 HUMAN Protein has a total Mw of 12.3kDa.

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

      What is the Purity of CCL28 HUMAN Protein?
      CCL28 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 HUMAN Protein?
      Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CCL28 HUMAN Protein?
      SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.

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

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

    Ccl28 Human
  • View Data Sheet

    Name :

    GALE Human

    Description:

    UDP-Galactose-4-Epimerase Human Recombinant

    UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.

    Product # :

    ENZ-537

    Price :

    Quantity :

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    • description
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    Description

    GALE Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40.4 kDa. The GALE is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GALE Human solution containing 20mM Tris pH-8, 5mM DTT, 0.1M NaCl, 1mM EDTA & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.

    • Synonyms

      UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.

    • 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 MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA.

    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.

    Gale Human
  • View Data Sheet

    Name :

    MCEE Human

    Description:

    Methylmalonyl CoA Epimerase Human Recombinant

    GLOD2, Methylmalonyl CoA Epimerase, Glyoxalase Domain Containing 2, DL-methylmalonyl-CoA Racemase.

    Product # :

    ENZ-013

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    Description

    MCEE produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (37-176a.a.) and having a molecular mass of 17.3kDa.MCEE is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MCEE protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT, 0.1mM PMSF and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MCEE catalyzes the interconversion of D- and L-methylmalonyl-CoA throughout the degradation of branched chain amino acids, odd chain-length fatty acids, and other metabolites. MCEE protein deficiency is an autosomal recessive inborn error of amino acid metabolism, involving valine, threonine, isoleucine and methionine. This organic aciduria can appear in the neonatal period with life-threatening metabolic acidosis, hyperammonemia, feeding difficulties, pancytopenia and coma.

    • Synonyms

      GLOD2, Methylmalonyl CoA Epimerase, Glyoxalase Domain Containing 2, DL-methylmalonyl-CoA Racemase.

    • 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 MQVTGSVWNL GRLNHVAIAV PDLEKAAAFY KNILGAQVSE AVPLPEHGVS VVFVNLGNTK MELLHPLGRD SPIAGFLQKN KAGGMHHICI EVDNINAAVM DLKKKKIRSL SEEVKIGAHG KPVIFLHPKD CGGVLVELEQ A

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    Mcee Human
  • View Data Sheet

    Name :

    RSV Human

    Description:

    Respiratory Syncytial Virus Human Recombinant

    Product # :

    RSV-001

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    Description

    Recombinant Human Respiratory Syncytial Virus produced in E. coli having a Mw of 44kDa. RSV Human is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    RSV protein solution contains 0.25% sodium azide, 10mM K2CO3 and PBS.

    Purity

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

    More Info

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

      HMALSKVKLNDTLNKDQLLSSSKYTIQRSTGDSIDTPNYDVQKHINKLCGMLLITEDANHKFT GLIGMLYAMSRLGREDTIKILRDAGYHVKANGVDVTTHRQDINGKEMKFEVLTLASLTTEI QINIEIESRKSYKKMLKEMGEVAPEYRHDSPDCGMIILCIAALVITKLAAGDRSGLTAVI RRANNVLKNEMKRYKGLLPKDIANSFYEVFEKHPHFIDVFVHFGIAQSSTRGGSRVEGIFAG LFMNAYGAGQV MLRWGVLAKSVKNIMLGHASVQAEMEQVVEVYEYAQKLGGEAGFYHIL NNPKASLLSLTQFPHFSSVVLGNAAGLGIMGEYRGTPRNQDLYDAAKAYAEQLKENGV

    • Background

      Respiratory Syncytial Virus (RSV) remains a formidable pathogen, especially in vulnerable populations such as infants and the elderly, causing significant morbidity and mortality worldwide. The pursuit of effective preventive and therapeutic strategies has led to the exploration of RSV Recombinant Protein as a key player in the molecular battle against this respiratory pathogen. This research aims to unravel the intricacies of RSV Recombinant Protein, shedding light on its structural features, immunogenic potential, and its applications in vaccine development and antiviral therapies. By dissecting the properties of RSV Recombinant Protein, scientists seek to fortify our defenses against RSV and advance the prospects for improved clinical outcomes.

      Structural Insights into RSV Recombinant Protein:

      RSV Recombinant Protein, engineered to mimic key viral antigens, offers a controlled and standardized tool for studying the virus's structural components. Understanding the protein's three-dimensional structure and conformational characteristics is paramount for elucidating its interactions with the immune system, guiding the design of effective vaccines, and unraveling potential targets for antiviral drugs.

      Immunogenic Potential and Vaccine Development:

      The quest for an effective RSV vaccine has been challenged by the virus's ability to elude natural immunity. RSV Recombinant Protein, designed to trigger robust immune responses, is a promising candidate for vaccine development. By presenting viral antigens to the immune system in a controlled manner, the recombinant protein aims to induce protective immune responses, particularly neutralizing antibodies, that guard against RSV infection and its associated complications.

      Application in Passive Immunization and Therapeutics:

      Beyond vaccination, RSV Recombinant Protein holds promise in the realm of passive immunization and antiviral therapies. Monoclonal antibodies derived from the recombinant protein can be employed to provide immediate, targeted immunity against RSV. This approach is particularly relevant for individuals at high risk, such as premature infants or immunocompromised patients, offering a bridge to protection until their own immune responses can be activated.

      Challenges and Future Directions:

      While RSV Recombinant Protein represents a beacon of hope in the fight against RSV, challenges persist. The virus's ability to mutate and evade immune detection necessitates ongoing research to refine and adapt recombinant strategies. Additionally, considerations of vaccine safety, optimal dosing, and potential side effects demand thorough investigation to ensure the translational success of RSV Recombinant Protein-based interventions.

      RSV Recombinant Protein emerges as a key protagonist in the scientific narrative against Respiratory Syncytial Virus. Its structural insights, immunogenic potential, and applications in vaccine development and antiviral therapies mark it as a pivotal tool in our arsenal. As researchers continue to decipher the molecular intricacies of RSV Recombinant Protein, they pave the way for innovative strategies that may revolutionize RSV prevention and treatment, ultimately shaping the landscape of respiratory virus control and global health.

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    Rsv Human
  • View Data Sheet

    Name :

    MAPKSP1 antibody

    Description:

    MAPK Scaffold Protein 1, Mouse Anti Human

    MAPBP, MP1, MAPK Scaffold Protein 1, Interacting Protein 1, MEK binding partner 1, Mitogen-Activated Protein Kinase kinase 1.

    Product # :

    ANT-734

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    Formulation

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

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    • Introduction

      MAPKSP1 is a scaffold protein which operates in the extracellular signal-regulated kinase (ERK) cascade. MAPKSP1 protein is restricted to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2.

    • Synonyms

      MAPBP, MP1, MAPK Scaffold Protein 1, Interacting Protein 1, MEK binding partner 1, Mitogen-Activated Protein Kinase kinase 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human MAPKSP1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human MAPKSP1 protein 1-124 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT1F10AT.

    • Applications

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

    • 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

      MAPKSP1 antibody was purified from mouse ascitic fluids by protein-A 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.

    Mapksp1 Antibody 2
  • View Data Sheet

    Name :

    CD21 Antibody

    Description:

    CD21, Mouse Anti-Human

    Complement receptor type 2, Cr2, Complement C3d receptor, Epstein-Barr virus receptor, EBV receptor, CD21 antigen, CR2, C3DR, CD21, SLEB9.

    Product # :

    ANT-257

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    Formulation

    1mg/ml in PBS (after reconstitution).

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    • Introduction

      CD21 is expressed strongly on mature B cells, follicular dentritic cells and weakly on immature thymocytes and T lymphocytes. In B-cell ontogeny, CD21 appears after the pre-B-stage, is maintained during peripheral B-cell development and is lost upon terminal differentiation into plasma cells. CD21 expression is also gradually lost after stimulation of B cells in vitro. CD21 functions as receptor for C3d, C3dg and iC3b Complement components, for EBV and for IFNalpha. CD21 binds to CD23 and associates with CD19, CD81 and Leu13 to form a large signal-transduction complex involved in B cell activation.

    • Synonyms

      Complement receptor type 2, Cr2, Complement C3d receptor, Epstein-Barr virus receptor, EBV receptor, CD21 antigen, CR2, C3DR, CD21, SLEB9.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified human B-Cells.

    • Ig Subclass

      Mouse IgG2a.

    • Clone

      hCD21.

    • Applications

      Staining antibody. For staining, use 10µl/1,000,000 cells.

    • Available Conjugates

      This antibody is also available conjugated to biotin and FITC. For staining with biotin or FITC-conjugated antibody use 5-10µl/106 cells.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Protein-A.

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    Cd21 Antibody
  • View Data Sheet

    Name :

    CoV HKU1 Human

    Description:

    Coronavirus HKU1 Nucleoprotein Human Recombinant

    Product # :

    SARS-055

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    Description

    Recombinant Human Coronavirus HKU1 Nucleoprotein is full length protein except the predicted signal peptide of the first 30 aa produced in E.coli and migrate at 50kDa.The CoV HKU1 is fused to a 6xHis tag at its C terminal and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    CoV HKU1 protein solution contains PBS and 25mM K2CO3.

    Purity

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

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    • Introduction

      CoV HKU1 is 1 from 7 known coronaviruses to infect humans including CoV-229E, CoV-NL63, CoVHKU1, MERS-CoV, the original SARS-CoV1, and SARS-CoV-2 (Covid 19). CoV-229E, beta-coronavirus, NL63, CoV-HKU1 and OC43 are the viruses responsible for the common cold. Beta-coronaviruses has an additional shorter spike-like protein called hemagglutinin esterase. Human coronavirus HKU1 (CoV-HKU1) belongs to beta-coronavirus which are enveloped, positive-sense, single stranded RNA and enters its host celll by binding to the N-acetyl9-O-acetyl neuraminic acid 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

      SERNYQTFNR GRKTQPKFTV STQPQGNTIP HYSWFSGITQ FQKGRDFKFS DGQGVPIAFG VPPSEAKGYW YRHSRRSFKT ADGQQKQLLP RWYFYYLGTG PYANASYGES LEGVFWVANH QADTSTPSDV SSRDPTTQEA IPTRFPPGTI LPQGYYVEGS GRSASNSRPG SRSQSRGPNN RSLSRSNSNF RHSDSIVKPD ADEIANLVL AKLGKESKPQ QVTKQNAKEI RHKILTKPRQ KRTPNKHCNV QQCFGKRGPS QNFGNAEMLK LGTNDPQFPI LAELAPTPGA FFFGSKLDLV KRDSEADSPV KDVFELHYSG SIRFDSTLPG FETIMKVLEE NLNAYVNSNQ NTDSDSLSSK PQRKRGVKQL PEQFDSLNLS AGTQHISNDF TPEDHSLLAT LDDPYVEDSV A

    • Applications

      Immunoassay.

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

    product_image.jpg
  • View Data Sheet

    Name :

    CTSA Mouse

    Description:

    Cathepsin-A Mouse Recombinant

    Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.

    Product # :

    ENZ-945

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    Description

    CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.

    • Synonyms

      Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.

    • 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

      APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.

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    Ctsa Mouse
  • View Data Sheet

    Name :

    MPG Human

    Description:

    N-Methylpurine-DNA Glycosylase Human Recombinant

    DNA-3-methyladenine glycosylase, 3-alkyladenine DNA glycosylase, 3-methyladenine DNA glycosidase, ADPG, N-methylpurine-DNA glycosylase, MPG, AAG, ANPG, MID1, MDG, PIG11, PIG16, CRA36.1.

    Product # :

    ENZ-151

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    Description

    MPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-298 a.a.) and having a molecular mass of 33.9kDa (Molecular weight on SDS-PAGE will appear higher).MPG is fused to an 8 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MPG protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 200mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      DNA-3-methyladenine glycosylase (MPG) is a member of the DNA glycosylase MPG family. MPG initiates base excision repair in DNA by removing a wide variety of alkylated, deaminated, and lipid peroxidation-induced purine adducts.

    • Synonyms

      DNA-3-methyladenine glycosylase, 3-alkyladenine DNA glycosylase, 3-methyladenine DNA glycosidase, ADPG, N-methylpurine-DNA glycosylase, MPG, AAG, ANPG, MID1, MDG, PIG11, PIG16, CRA36.1.

    • 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

      MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL LRALEPLEGL ETMRQLRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQALE HHHHHH.

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    Mpg Human
  • View Data Sheet

    Name :

    DUSP23 Human

    Description:

    Dual Specificity Phosphatase 23 Human Recombinant

    Dual specificity protein phosphatase 23, DUSP25, Low molecular mass dual specificity phosphatase 3, LDP-3, VHZ, VH1-like phosphatase Z, MOSP, RP11-190A12.1, FLJ20442, EC 3.1.3.16, EC 3.1.3.48.

    Product # :

    ENZ-195

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    Description

    DUSP23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150 a.a.) and having a molecular mass of 18.8kDa.DUSP23 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DUSP23 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 2mM DTT, and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

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    • Introduction

      DUSP23 is a member of the protein-tyrosine phosphatase family. DUSP23 is a protein phosphatase which facilitates dephosphorylation of phosphorylated proteins on Tyr and Ser/Thr residues. In vitro, DUSP23 dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10). In addition, DUSP23 enhances activation of JNK and p38(MAPK14).

    • Synonyms

      Dual specificity protein phosphatase 23, DUSP25, Low molecular mass dual specificity phosphatase 3, LDP-3, VHZ, VH1-like phosphatase Z, MOSP, RP11-190A12.1, FLJ20442, EC 3.1.3.16, EC 3.1.3.48.

    • 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 MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD AIAEIRRLRP GSIETYEQEK AVFQFYQRTK

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    Dusp23 Human
  • View Data Sheet

    Name :

    CANT1 Human

    Description:

    Calcium Activated Nucleotidase 1 Human Recombinant

    Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.

    Product # :

    PRO-1010

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    Description

    CANT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (63-401 a.a.) and having a molecular mass of 40.5kDa. CANT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CANT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.

    • Synonyms

      Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.

    • 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 MGSHMRPAPG RPPTHNAHNW RLGQAPANWY NDTYPLSPPQ RTPAGIRYRI AVIADLDTES RAQEENTWFS YLKKGYLTLS DSGDKVAVEW DKDHGVLESH LAEKGRGMEL SDLIVFNGKL YSVDDRTGVV YQIEGSKAVP WVILSDGDGT VEKGFKAEWL AVKDERLYVG GLGKEWTTTT GDVVNENPEW VKVVGYKGSV DHENWVSNYN ALRAAAGIQP PGYLIHESAC WSDTLQRWFF LPRRASQERY SEKDDERKGA NLLLSASPDF GDIAVSHVGA VVPTHGFSSF KFIPNTDDQI IVALKSEEDS GRVASYIMAF TLDGRFLLPE TKIGSVKYEG IEFI.

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    Cant1 Human
  • View Data Sheet

    Name :

    CD14 Mouse, Sf9

    Description:

    CD14 Mouse Recombinant, Sf9

    Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein, CD14.

    Product # :

    PRO-2233

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    Description

    CD14 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 357 amino acids (16-366a.a.) and having a molecular mass of 38.3kDa. CD14 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD14 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD14 (also known lipopolysaccharide (LPS) receptor) is expressed strongly on monocytes and macrophage and weakly on the surface of neutrophils. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a high affinity receptor for complexes of LPS and LPS binding protein (LBP). Soluble CD14, also binding to LPS, acts at physiological concentration as an LPS agonist and has, at higher concentrations, an LPS antagonizing effect in cell activation. CD14 has been shown to bind apoptotic cells.

    • Synonyms

      Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein, CD14.

    • 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

      SPAPPEPCEL DEESCSCNFS DPKPDWSSAF NCLGAADVEL YGGGRSLEYL LKRVDTEADL GQFTDIIKSL SLKRLTVRAA RIPSRILFGA LRVLGISGLQ ELTLENLEVT GTAPPPLLEA TGPDLNILNL RNVSWATRDA WLAELQQWLK PGLKVLSIAQ AHSLNFSCEQ VRVFPALSTL DLSDNPELGE RGLISALCPL KFPTLQVLAL RNAGMETPSG VCSALAAARV QLQGLDLSHN SLRDAAGAPS CDWPSQLNSL NLSFTGLKQV PKGLPAKLSV LDLSYNRLDR NPSPDELPQV GNLSLKGNPF LDSESHSEKF NSGVVTAGAP SSQAVALSGT LALLLGDRLF VHHHHHH.

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    Cd14 Mouse Sf9
  • View Data Sheet

    Name :

    MGLL Human, Active

    Description:

    Monoglyceride Lipase Human Recombinant, Active

    Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.

    Product # :

    ENZ-983

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    Description

    MGLL 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 333 amino acids (1-313 a.a.) and having a molecular mass of 36.4kDa. The MGLL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MGLL solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 170 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of p-nitrophenyl butyrate to pnitrophenol per minute at pH 7.5 at 25C.

    More Info

    • Introduction

      MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.

    • Synonyms

      Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.

    • 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 METGPEDPSS MPEESSPRRT PQSIPYQDLP HLVNADGQYL FCRYWKPTGT PKALIFVSHG AGEHSGRYEE LARMLMGLDL LVFAHDHVGH GQSEGERMVV SDFHVFVRDV LQHVDSMQKD YPGLPVFLLG HSMGGAIAIL TAAERPGHFA GMVLISPLVL ANPESATTFK VLAAKVLNLV LPNLSLGPID SSVLSRNKTE VDIYNSDPLI CRAGLKVCFG IQLLNAVSRV ERALPKLTVP FLLLQGSADR LCDSKGAYLL MELAKSQDKT LKIYEGAYHV LHKELPEVTN SVFHEINMWV SQRTATAGTA SPP.

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    Mgll Human Active
  • View Data Sheet

    Name :

    HMOX2 Human

    Description:

    Heme Oxygenase-2 Human Recombinant

    EC 1.14.99.3, HO2, Heme oxygenase 2, HO-2, HMOX2.

    Product # :

    ENZ-478

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    Description

    HMOX2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 264 amino acids (1-264 a.a.) and having a molecular mass of 30.5 kDa. HMOX2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HMOX2 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      HMOX2 cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently transferred to bilirubin by biliverdin reductase. Under physiological conditions, the activity of HMOX2 is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. HMOX2 participates in the production of carbon monoxide in the brain where it operates as a neurotransmitter. HMOX2 is an essential enzyme in heme catabolism and is involved in cellular response to oxidative stress.

    • Synonyms

      EC 1.14.99.3, HO2, Heme oxygenase 2, HO-2, HMOX2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      HMOX2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      SAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE DGFPVHDGKG DMRK.

    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.

    Hmox2 Human
  • View Data Sheet

    Name :

    DUSP22 Human

    Description:

    Dual Specificity Phosphatase 22 Human Recombinant

    Dual specificity protein phosphatase 22, DUSP22, JNK-stimulatory phosphatase-1, JSP-1, Low molecular weight dual specificity phosphatase 2, LMW-DSP2, Mitogen-activated protein kinase phosphatase x, MAP kinase phosphatase x, MKP-x, LMWDSP2, MKPX, JKAP, JSP1, LMWDSP2, MKPX, VHX.

    Product # :

    ENZ-800

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    Description

    DUSP22 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-184 a.a.) and having a molecular mass of 23.3kDa.DUSP22 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DUSP22 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dual Specificity Phosphatase 22, also known as DUSP22, is a part of the protein-tyrosine phosphatase family which holds 1 tyrosine-protein phosphatase domain. DUSP22 activates the Jnk signaling pathway and dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK). DUSP22 interacts with MAPK1 and MAPK8.

    • Synonyms

      Dual specificity protein phosphatase 22, DUSP22, JNK-stimulatory phosphatase-1, JSP-1, Low molecular weight dual specificity phosphatase 2, LMW-DSP2, Mitogen-activated protein kinase phosphatase x, MAP kinase phosphatase x, MKP-x, LMWDSP2, MKPX, JKAP, JSP1, LMWDSP2, MKPX, VHX.

    • 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 MGSMGNGMNK ILPGLYIGNF KDARDAEQLS KNKVTHILSV HDSARPMLEG VKYLCIPAAD SPSQNLTRHF KESIKFIHEC RLRGESCLVH CLAGVSRSVT LVIAYIMTVT DFGWEDALHT VRAGRSCANP NVGFQRQLQE FEKHEVHQYR QWLKEEYGES PLQDAEEAKN ILAAPGILKF WAFLRRL.

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    Dusp22 Human
  • View Data Sheet

    Name :

    NUDT10 Human

    Description:

    Nudix Type Motif 10 Human Recombinant

    Diphosphoinositol polyphosphate phosphohydrolase 3-alpha, DIPP-3-alpha, DIPP3-alpha, hDIPP3alpha, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha, Nucleoside diphosphate-linked moiety X motif 10, Nudix motif 10, hAps2, NUDT10, APS2, DIPP3A.

    Product # :

    ENZ-126

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    Description

    NUDT10 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-164 a.a.) and having a molecular mass of 19.5kDa.NUDT10 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUDT10 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.

    • Synonyms

      Diphosphoinositol polyphosphate phosphohydrolase 3-alpha, DIPP-3-alpha, DIPP3-alpha, hDIPP3alpha, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha, Nucleoside diphosphate-linked moiety X motif 10, Nudix motif 10, hAps2, NUDT10, APS2, DIPP3A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      NUDT10 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPGG AAVREVYEEA GVKGKLGRLL GVFEQNQDPK HRTYVYVLTV TELLEDWEDS VSIGRKREWF KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSMAPSSP DSDPLEHHHH HH.

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    Nudt10 Human
  • View Data Sheet

    Name :

    BMP 7 Human

    Description:

    Bone Morphogenetic Protein-7 Human Recombinant

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-333

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    Description

    Bone Morphogenetic Protein-7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 139 amino acids and having a molecular mass of 15679.97 Dalton. The BMP-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-7 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM sodium citrate pH=3.5.

    Purity

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

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, BMP-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP 7 Human 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 briefly centrifuge the vial prior to opening to bring the contents to the bottom. Reconstitute in 20mM-100mM acetic acid at a concentration of 0.1-0.5mg per ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Thr-Gly-Ser-Lys.

    • Background

      Bone Morphogenetic Protein-7 Human Recombinant: A Comprehensive Review

      Abstract:

      Bone Morphogenetic Protein-7 (BMP-7) is a crucial member of the transforming growth factor-beta (TGF-β) superfamily with diverse roles in development, tissue repair, and regeneration.

      This research paper provides a comprehensive review of BMP-7 Human Recombinant, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the therapeutic potential of BMP-7 modulation.

      Introduction:

      BMP-7 is a multifunctional growth factor that plays a significant role in skeletal development and tissue homeostasis. This paper aims to provide an extensive review of BMP-7 Human Recombinant, highlighting its importance in various biological processes and its potential therapeutic applications.

      Structure and Function of BMP-7:

      BMP-7 is a disulfide-linked homodimeric protein composed of two subunits. It binds to specific cell surface receptors, activating downstream signaling pathways, including the Smad pathway and non-Smad signaling cascades. These pathways regulate cellular processes such as proliferation, differentiation, and apoptosis.

      Skeletal Development and Regeneration:

      BMP-7 is a key regulator of bone formation and remodeling. It promotes osteoblast differentiation and bone mineralization, contributing to skeletal development and repair. BMP-7 also plays a role in cartilage formation and chondrogenesis.

      Tissue Repair and Regeneration:

      Beyond its skeletal functions, BMP-7 is involved in tissue repair and regeneration in various organs, including the kidney, liver, and heart. It promotes the regeneration of damaged tissues by stimulating cell proliferation, angiogenesis, and extracellular matrix remodeling.

      Therapeutic Potential:

      Due to its regenerative and reparative properties, BMP-7 has attracted significant attention as a potential therapeutic agent. It has been investigated for its applications in bone regeneration, cartilage repair, and the treatment of kidney and liver diseases. Clinical trials exploring the therapeutic efficacy of BMP-7 are ongoing.

      Challenges and Future Perspectives:

      Despite the promising therapeutic potential of BMP-7, challenges remain, including optimizing its delivery systems, understanding its dosage and duration of treatment, and managing potential side effects. Future research should focus on unraveling the intricate mechanisms of BMP-7 signaling, developing targeted therapies, and enhancing its clinical applications.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 15kDa.

      What is the source or expression system of BMP7 Protein?
      Escherichia Coli.

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The biological functionality of BMP7 Protein will be determined in the future.

      What is the amino acid sequence of BMP7 Protein?
      BMP7 Protein is composed from 139 amino acids.

      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 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.

    Bmp 7 Human
  • View Data Sheet

    Name :

    IMMP2L Human

    Description:

    IMP2 Inner Mitochondrial Membrane Peptidase-Like Human Recombinant

    IMP2 Inner Mitochondrial Membrane Peptidase-Like (S. Cerevisiae), IMP2, IMP2 Inner Mitochondrial Membrane Protease-Like (S. Cerevisiae), IMMP2L Intronic Transcript 1 (Non-Protein Coding), Mitochondrial Inner Membrane Protease Subunit, Inner Mitochondrial Membrane Peptidase 2 Like, IMP2-Like Protein, EC 3.4.21.- , IMMP2L-IT1, IMP2-LIKE, EC 3.4.21, Mitochondrial inner membrane protease subunit 2.

    Product # :

    ENZ-822

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    Description

    IMMP2L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (38-175aa) and having a molecular mass of 18.0kDa. IMMP2L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IMMP2L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IMP2 Inner Mitochondrial Membrane Peptidase-Like (IMMP2L) is implicated in processing the signal peptide sequences, IMMP2L is used to direct mitochondrial proteins to the mitochondria. IMMP2L resides in the mitochondria and is one of the essential proteins for the catalytic activity of the mitochondrial inner membrane peptidase (IMP) complex. Two variants which encode the same protein have been found for IMMP2L.

    • Synonyms

      IMP2 Inner Mitochondrial Membrane Peptidase-Like (S. Cerevisiae), IMP2, IMP2 Inner Mitochondrial Membrane Protease-Like (S. Cerevisiae), IMMP2L Intronic Transcript 1 (Non-Protein Coding), Mitochondrial Inner Membrane Protease Subunit, Inner Mitochondrial Membrane Peptidase 2 Like, IMP2-Like Protein, EC 3.4.21.- , IMMP2L-IT1, IMP2-LIKE, EC 3.4.21, Mitochondrial inner membrane protease subunit 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 MGSRVEGASM QPSLNPGGSQ SSDVVLLNHW KVRNFEVHRG DIVSLVSPKN PEQKIIKRVI ALEGDIVRTI GHKNRYVKVP RGHIWVEGDH HGHSFDSNSF GPVSLGLLHA HATHILWPPE RWQKLESVLP PERLPVQREE E.

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    Immp2L Human
  • View Data Sheet

    Name :

    POMZP3 Human

    Description:

    POM121 And ZP3 Fusion Human Recombinant

    POM121 and ZP3 fusion protein, POM-ZP3, POMZP3, POM121 and ZP3 fusion protein isoform 1, POM121 And ZP3 Fusion.

    Product # :

    PRO-2020

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    Description

    POMZP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187) and having a molecular mass of 23.0 kDa.POMZP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The POMZP3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      POM121 And ZP3 Fusion (POMZP3) is a DNA sequences derived from two distinct loci, particularly through the duplication of 2 internal exons from the POMZP3 gene and 4 3' exons from the ZP3 gene. POMZP3 is a protein-coding gene which lacks the nuclear pore localization motif.

    • Synonyms

      POM121 and ZP3 fusion protein, POM-ZP3, POMZP3, POM121 and ZP3 fusion protein isoform 1, POM121 And ZP3 Fusion.

    • 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 MGSMVCSPVT LRIAPPDRRF SRSAIPEQII SSTLSSPSSN APDPCAKETV LSALKEKKKK RTVEEEDQIF LDGQENKRSC LVDGLTDASS AFKVPRPGPD TLQFTVDVFH FANDSRNMIY ITCHLKVTLA EQDPDELNKA CSFSKPSNSW FPVEGLADIC QCCNKGDCGT PSHSRRQPRV VSQWSTSASL.

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    Pomzp3 Human
  • View Data Sheet

    Name :

    MAF1 Human

    Description:

    MAF1 Human Recombinant

    MAF1 homolog (S. cerevisiae), Repressor of RNA polymerase III transcription MAF1 homolog, homolog of yeast MAF1, MGC20332, MGC31779, MGC39758, DKFZp586G1123.

    Product # :

    PRO-921

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    Description

    MAF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 276 amino acids (1-256) and having a molecular mass of 31.0 kDa.The MAF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MAF1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAF1 resembles Maf1 which is a Saccharomyces cerevisiae – a highly conserved protein in eukaryotic cells, localized to the nucleus. MAF1 Interacts with BRF2, MAF1 and functions as a mediator for signals which explicitly inhibit RNA polymerase III (Pol III) activity by inhibiting the association of TFIIIB to DNA. MAF1 reacts to modifications in the cellular environment and represses pol III transcription.

    • Synonyms

      MAF1 homolog (S. cerevisiae), Repressor of RNA polymerase III transcription MAF1 homolog, homolog of yeast MAF1, MGC20332, MGC31779, MGC39758, DKFZp586G1123.

    • 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 MKLLENSSFE AINSQLTVET GDAHIIGRIE SYSCKMAGDD KHMFKQFCQE GQPHVLEALS PPQTSGLSPS RLSKSQGGEE EGPLSDKCSR KTLFYLIATL NESFRPDYDF STARSHEFSR EPSLSWVVNA VNCSLFSAVR EDFKDLKPQL WNAVDEEICL AECDIYSYNP DLDSDPFGED GSLWSFNYFF YNKRLKRIVF FSCRSISGST YTPSEAGNEL DMELGEEEVE EESRSRGSGA EETSTMEEDR VPVICI

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    Maf1 Human
  • View Data Sheet

    Name :

    MDP1 Human

    Description:

    Magnesium-Dependent Phosphatase 1 Human Recombinant

    Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.

    Product # :

    ENZ-044

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    Description

    MDP1 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 200 amino acids (1-176 a.a.) and having a molecular mass of 22.6kDa. The MDP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MDP1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Magnesium-dependent phosphatase 1 (MDP1) is a memeber of the HAD-like hydrolase superfamily. MDP1 is a magnesium-dependent phosphatase which may act as a tyrosine phosphatase. MDP1 is inhibited by vanadate and zinc, and slightly by calcium.

    • Synonyms

      Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.

    • 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 MGSHMARLPK LAVFDLDYTL WPFWVDTHVD PPFHKSSDGT VRDRRGQDVR LYPEVPEVLK RLQSLGVPGA AASRTSEIEG ANQLLELFDL FRYFVHREIY PGSKITHFER LQQKTGIPFS QMIFFDDERR NIVDVSKLGV TCIHIQNGMN LQTLSQGLET FAKAQTGPLR SSLEESPFEA.

    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.

    Mdp1 Human
  • View Data Sheet

    Name :

    CoV-2 Envelope (1-75)

    Description:

    Coronavirus 2019 Envelope (1-75 a.a.), Recombinant

    Product # :

    SARS-037

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    The E.coli derived recombinant protein contains the Coronavirus 2019 CoV-2 Envelope, Wuhan-Hu-1 strain, amino acids 1-75 fused to GST-tag at N-terminal & His-tag at C-terminal having a calculated Mw of 36.8 kDa and migrating between 33-35 umder reducing condition.

    Source

    E.Coli

    Formulation

    CoV-2 Envelope protein is supplied in 20mM Tris, 5mM EDTA & 0.5M Arginine, pH-8 and 10% sucrose.

    Purity

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

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cov-2 Envelope protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Envelope protein 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 add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Purification Method

      Purified by Metal-Afinity chromatographic technique.

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

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