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Search results

1000 results found for “cytohesin”

Name

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  • View Data Sheet

    Name :

    Lysostaphin

    Description:

    Lysostaphin Recombinant

    Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    Product # :

    ENZ-269

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
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    Description

    Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without any additives.

    Purity

    98% as determined by RP-HPLC.

    Biological Activity

    Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C.  Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.

    Citations

    More Info

    • Introduction

      Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.

    • Synonyms

      Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.

    • Protein content

      Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.

    • Specific Activity

      Determined to be 3,540 units/mg.

    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.

    Lysostaphin
  • View Data Sheet

    Name :

    Leptin Rat, PEG

    Description:

    Pegylated Rat Leptin Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-592

    Price :

    Quantity :

    Shipping Method :

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    Description

    Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. 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. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Leptin Rat Pegylated
  • View Data Sheet

    Name :

    Bartonella 17kDa

    Description:

    Bartonella Henselae 17kDa Recombinant

    Product # :

    PRO-2568

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
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    Description

    Recombinant Bartonella Henselae 17kDa produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 18kDa. Bartonella 17kDa is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bartonella 17kDa is supplied at a 20mM HEPES buffer pH-8.0 and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Numerous forms of Bartonellosis are caused by Bartonella henselae as well as Cat Scratch Disease & Bacillary Angiomatosis. It has been found that up to 95% of patients with Cat Scratch Disease show antibodies against Bartonella henselae antigens.

      P17 is the 1st antigen which was discovered to be strongly reactive with sera from Cat Scratch Disease patients. Bartonella henselae participates in host recognition by the type IV secretion system as a homolog of the virB5 family.

      Highly immunoreactive proteins which are produced by the Bartonella henselae are the most important antigens used for the diagnosis of Cat Scratch Disease.

    • Physical Appearance

      Sterile Filtered 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.

    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.

    Bartonella Henselae 17Kda
  • View Data Sheet

    Name :

    Leptin qA Mouse, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Mouse Recombinant

    Product # :

    CYT-1244

    Price :

    Quantity :

    Shipping Method :

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    Description

    Leptin Antagonist Quadruple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin Quadruple anatagonist Pegylated runs as a 55 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Mouse Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.  Pegylated recombinant mouse leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super mouse leptin antagonist but in vivo it has profound weight gain effect, resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin produced mainly by adipocytes. Leptin mostly regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution 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 Mouse Ta Peg
  • View Data Sheet

    Name :

    APOA5 Human, HEK

    Description:

    Apolipoprotein A-V Human Recombinant, HEK

    Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.

    Product # :

    CYT-025

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    Description

    APOA5 Human Recombinant Flag-Tagged Fusion Protein is 40.1 kDa protein containing 354 amino acid residues of the APOA5 Human and 11 additional amino acid residues of flagTag.

    Source

    HEK293

    Formulation

    APOA5 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 20mM TRIS and 50mM NaCl, pH 7.5

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ApoA5 is an important regulator of serum triglyceride concentrations. An ApoA5 mouse nock-out model produced an approximately four fold increase in serum triglycerides, whereas a knock-in model human ApoA5 produced 50-70% lower concentrations of mouse serum triglycerides. Furthermore, peroxisome proliferators-activated receptoragonists, which are used clinically to lower serum triglyceride concentrations, cause increased ApoA5 mRNA expression. There is very little known about ApoA5 protein in human serum. Lately, it was established that ApoA5 is present in the human serum and it can be detected by polyclonal antibodies against both the HN2 and COOH termini, but at much lower concentration than other apolipoproteins.

    • Synonyms

      Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized APOA5 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted APOA5 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.

    • Solubility

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

    • Amino Acid Sequence

      RKGFWDYFSQ TSGDKGRVEQ IHQQKMAREP ATLKDSLEQD LNNMNKFLEK LRPLSGSEAP RLPQDPVGMR RQLQEELEEV KARLQPYMAE AHELVGWNLE GLRQQLKPYT MDLMEQVALR VQELQEQLRV VGEDTKAQLL GGVDEAWALL QGLQSRVVHH TGRFKELFHP YAESLVSGIG RHVQELHRSV APHAPASPAR LSRCVQVLSR KLTLKAKALH ARIQQNLDQL REELSRAFAG TGTEEGAGPD PQMLSEEVRQ RLQAFRQDTY LQIAAFTRAI DQETEEVQQQ LAPPPPGHSA FAPEFQQTDS GKVLSKLQAR LDDLWEDITH SLHDQGHSHL GDPAAADYKD DDDK

    • Background

      What is the molecular weight/Mw of APOA5 Protein?
      APOA5 Protein has a total Mw of 40.1kDa.

      What is the source or expression system of APOA5 Protein?
      HEK293
      What is the Purity of APOA5 Protein?
      APOA5 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOA5 Protein?
      The biological functionality of APOA5 Protein will be determined in the future.

      What is the amino acid sequence of APOA5 Protein?
      RKGFWDYFSQ TSGDKGRVEQ IHQQKMAREP ATLKDSLEQD LNNMNKFLEK LRPLSGSEAP RLPQDPVGMR RQLQEELEEV KARLQPYMAE AHELVGWNLE GLRQQLKPYT MDLMEQVALR VQELQEQLRV VGEDTKAQLL GGVDEAWALL QGLQSRVVHH TGRFKELFHP YAESLVSGIG RHVQELHRSV APHAPASPAR LSRCVQVLSR KLTLKAKALH ARIQQNLDQL REELSRAFAG TGTEEGAGPD PQMLSEEVRQ RLQAFRQDTY LQIAAFTRAI DQETEEVQQQ LAPPPPGHSA FAPEFQQTDS GKVLSKLQAR LDDLWEDITH SLHDQGHSHL GDPAAADYKD DDDK
      What applications can APOA5 Protein be used in?
      APOA5 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOA5 Protein?
      The endotoxin level is minimal, APOA5 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.

    Apoa5 Human
  • View Data Sheet

    Name :

    IL 33 Mouse

    Description:

    Interleukin-33 Mouse Recombinant

    Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.

    Product # :

    CYT-655

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    Description

    Interleukin33 Mouse recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 17.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The Mouse IL-33 was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of murine D10S cells is 0.04ng/ml, corresponding to a specific activity of 2.5x107units/mg.

    Citations

    More Info

    • Introduction

      Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.

    • Synonyms

      Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-33 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 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 IL-33 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSIQGTSLLT QSPASLSTYN DQSVSFVLEN GCYVINVDDS GKDQEQDQVL LRYYESPCPA SQSGDGVDGK KLMVNMSPIK DTDIWLHAND KDYSVELQRG DVSPPEQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEEKDESCN NIMFKLSKI.

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    Il 33 Mouse
  • View Data Sheet

    Name :

    Activin-A, CHO Human

    Description:

    Activin-A Human Recombinant, CHO

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-1258

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    Description

    Activin-A Human Recombinant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 26.0kDa. The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    CHO cells.

    Formulation

    Human Activin-A was lyophilized from a concentrated filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

    Biological Activity

    Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.

    Citations

    More Info

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

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

    • Solubility

      Human INHBA protein should be reconstituted in sterile 4mM HCl to a concentration of 0.1-1.0 mg/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

      GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 26 kDa.
      What is the source or expression system of Activin A Protein?
      CHO Cells.

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

      What is the Biological Activity of Activin A Protein?
      Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.

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

      What is the amino acid sequence of ACTIVIN A Protein?
      GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS

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

       

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    Activin A Protein
  • View Data Sheet

    Name :

    TK1 Human

    Description:

    Thymidine Kinase 1 Human Recombinant

    Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    Product # :

    PKA-036

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    Description

    TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.

    • Synonyms

      Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    • 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 MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.

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    Tk1 Human
  • View Data Sheet

    Name :

    KLRG1 Human

    Description:

    Killer Cell Lectin-like Receptor Subfamily G, Member 1 Human Recombinant

    Killer cell lectin-like receptor subfamily G member 1, C-type lectin domain family 15 member A, ITIM-containing receptor MAFA-L, MAFA-like receptor, Mast cell function-associated antigen, KLRG1, CLEC15A, MAFA, MAFAL, 2F1, MAFA-L, MAFA-2F1, MAFA-LIKE.

    Product # :

    PRO-1344

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    Description

    KLRG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (60-189 a.a) and having a molecular mass of 17kDa.KLRG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLRG1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Killer Cell Lectin-like Receptor Subfamily G, Member 1 (KLRG1) is a member of the killer cell lectin-like receptor (KLR) family, which is a group of transmembrane proteins preferentially expressed in NK cells. Natural killer (NK) cells are lymphocytes which mediate lysis of certain tumor cells and virus-infected cells without previous activation. NK cells can also regulate specific humoral and cell-mediated immunity. The cell surface expression of KLRG1 is up-regulated by MHC class I molecules expression.

    • Synonyms

      Killer cell lectin-like receptor subfamily G member 1, C-type lectin domain family 15 member A, ITIM-containing receptor MAFA-L, MAFA-like receptor, Mast cell function-associated antigen, KLRG1, CLEC15A, MAFA, MAFAL, 2F1, MAFA-L, MAFA-2F1, MAFA-LIKE.

    • 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 MGSLCQGSNY STCASCPSCP DRWMKYGNHC YYFSVEEKDW NSSLEFCLAR DSHLLVITDN QEMSLLQVFL SEAFCWIGLR NNSGWRWEDG SPLNFSRISS NSFVQTCGAI NKNGLQASSC EVPLHWVCKK VRL.

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    Klrg1 Human
  • View Data Sheet

    Name :

    Adiponectin Rat

    Description:

    Adiponectin Rat Recombinant

    Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-831

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    Description

    ACRP30 Rat Recombinant produced in 293 cell line is a polypeptide chain containing 238 amino acids and having a total molecular mass of 25.7 kDa. ACRP30 contains a C-Terminal linker (3 AA residue) and a C-Terminal Flag- tag (8 AA residue).

    Source

    HEK293 cell line.

    Formulation

    Filtered (0.4 µm) and lyophilized in 20 mM Tris buffer, 50 mM NaCl, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

      Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ACRP30 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ACRP30 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

      Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 25.7kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293 cell line.

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >90% 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?
      GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK.

      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.

    Acrp30 Rat
  • View Data Sheet

    Name :

    DCN Mouse

    Description:

    Decorin Mouse Recombinant

    Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.

    Product # :

    PRO-2234

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    Description

    DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.

    • Synonyms

      Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.

    • 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

      GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH

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    Dcn Mouse
  • View Data Sheet

    Name :

    NME3 Human, Active

    Description:

    Non-Metastatic Cells 3 Human Recombinant, BioActive

    Nucleoside diphosphate kinase 3, c371H6.2, DR-nm23, KIAA0516, NDPK-C, NDPKC, NM23-H3, NM23H3.

    Product # :

    PRO-2641

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    Description

    NME3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (22-169 a.a.) and having a molecular mass of 19.1kDa.NME3 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NME3 solution (0.5mg/ml) contains 50% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.

    Citations

    More Info

    • Introduction

      Non-Metastatic Cells 3 or NME3 is a possible suppressor of metastasis. NME3 can be found at a lower levels in greatly metastatic cells when compared to cells that has less metastatic potential NME3 is crucial for the nucleoside triphosphates synthesis, also, in apoptosis induction & hematopoiesis. NME3 is can be expressed during early stages of myeloid differentiation of greatly purified CD34+ cells.

    • Synonyms

      Nucleoside diphosphate kinase 3, c371H6.2, DR-nm23, KIAA0516, NDPK-C, NDPKC, NM23-H3, NM23H3.

    • 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 MERTFLAVKP DGVQRRLVGE IVRRFERKGF KLVALKLVQA SEELLREHYA ELRERPFYGR LVKYMASGPV VAMVWQGLDV VRTSRALIGA TNPADAPPGT IRGDFCIEVG KNLIHGSDSV ESARREIALW FRADELLCWE DSAGHWLYE

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    Nme3 Protein
  • View Data Sheet

    Name :

    IL 15 Mouse

    Description:

    Interleukin-15 Mouse Recombinant

    IL-15, MGC9721, Interleukin-15, Il15, AI503618.

    Product # :

    CYT-647

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    Description

    Interleukin-15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (49-162 a.a.) and having a molecular mass of 17.6 kDa. The IL-15 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The mouse IL-15 protein solution contains PBS, pH-7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using CTLL2 mouse cytotoxic T cells. The ED50 for this effect is < 1 ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

    Citations

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.

    • Synonyms

      IL-15, MGC9721, Interleukin-15, Il15, AI503618.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMNW IDVRYDLEKI ESLIQSIHID TTLYTDSDFH PSCKVTAMNC FLLELQVILH
      EYSNMTLNET VRNVLYLANS TLSSNKNVAE SGCKECEELE EKTFTEFLQS FIRIVQMFIN TS.

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

    Il 15 Mouse His
  • View Data Sheet

    Name :

    IL 22 Mouse

    Description:

    Interleukin-22 Mouse Recombinant

    IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    Product # :

    CYT-539

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    Description

    Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids and having a molecular mass of 16.7 kDa. The Murine IL-22 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 1X PBS.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to induce IL-10 secretion in Colo205 cells is less than 0.5ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.

    Citations

    More Info

    • Introduction

      Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10R? (previously known as CRF2-4), belonging to the class II cytokine receptor family.

    • Synonyms

      IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 Interleukin -22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

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    Il 22 Mouse
  • View Data Sheet

    Name :

    PFN2 Human

    Description:

    Profilin-2 Human Recombinant

    Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    Product # :

    PRO-809

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    Description

    PFN2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.2 kDa. PFN2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PFN2 is a ubiquitous actin monomer-binding protein which is part of the profilin family. PFN2 regulates actin polymerization in response to extra cellular signals. PFN2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, while it increases it at low concentrations. PFN2 binds to PIP2, it inhibits the formation of IP3 and DG.

    • Synonyms

      Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    • 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 MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF TNGLALGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF.

    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.

    Pfn2 Human
  • View Data Sheet

    Name :

    PI3 Human, Sf9

    Description:

    Peptidase Inhibitor 3 Human Recombinant, Sf9

    Elafin, ESI, SKALP, WAP3, WFDC14.

    Product # :

    PRO-2653

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    Description

    PI3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 101 amino acids (23-117a.a) and having a molecular mass of 10.7kDa.PI3 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The PI3 solution (0.2mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Peptidase Inhibitor 3, also referred to PI3, is neutrophil and pancreatic elastase-specific inhibitor of skin. The protein may prevent elastase mediated tissue proteolysis. PI3 has shown inhibition of alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor, a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1.

    • Synonyms

      Elafin, ESI, SKALP, WAP3, WFDC14.

    • 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

      AVTGVPVKGQ DTVKGRVPFN GQDPVKGQVS VKGQDKVKAQ EPVKGPVSTK PGSCPIILIR CAMLNPPNRC LKDTDCPGIK KCCEGSCGMA CFVPQHHHHH H

    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.

    Elafin Human
  • View Data Sheet

    Name :

    TIPIN Human

    Description:

    TIMELESS Interacting Protein Human Recombinant

    TIMELESS Interacting Protein, CSM3 Homolog.

    Product # :

    PRO-1710

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    Description

    TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.

    • Synonyms

      TIMELESS Interacting Protein, CSM3 Homolog.

    • 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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

    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.

    Tipin Human
  • View Data Sheet

    Name :

    FSTL1 Human, HEK

    Description:

    Follistatin Like 1 Human Recombinant, HEK

    Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.

    Product # :

    CYT-1027

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    Description

    FSTL1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-308) containing 296 amino acids including a 8 a.a C-terminal His tag. The total molecular mass is 33.8kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    FSTL1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline and 5 % (w/v) trehalose, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FSTL1 protein resembles follistatin, an activin-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.

    • Synonyms

      Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.

    • 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 one week 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. FSTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.

    • Background

      What is the molecular weight/Mw of FSTL1 HUMAN, HEK Protein?
      FSTL1 HUMAN, HEK Protein has a total Mw of 33.8kDa.

      What is the source or expression system of FSTL1 HUMAN, HEK Protein?
      HEK293 cells.

      What is the Purity of FSTL1 HUMAN, HEK Protein?
      FSTL1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FSTL1 HUMAN, HEK Protein?
      The biological functionality of FSTL1 HUMAN, HEK Protein will be determined in the future.

      What is the amino acid sequence of FSTL1 HUMAN, HEK Protein?
      EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.

      What applications can FSTL1 HUMAN, HEK Protein be used in?
      FSTL1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FSTL1 HUMAN, HEK Protein?
      The endotoxin level is minimal, FSTL1 HUMAN, HEK 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.

    Fstl1 Protein
  • View Data Sheet

    Name :

    KIAA0101 Human

    Description:

    KIAA0101 Human Recombinant

    KIAA0101, L5, NS5ATP9, OEATC, OEATC-1, OEATC1, p15(PAF), p15/PAF, p15PAF, PAF, PAF15, PCNA-associated factor, Hepatitis C virus NS5A-transactivated protein 9, HCV NS5A-transactivated protein 9, Overexpressed in anaplastic thyroid carcinoma 1, PCNA-associated factor of 15 kDa.

    Product # :

    PRO-1683

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    Description

    KIAA0101 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-111) and having a molecular mass of 14.4 kDa.KIAA0101 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KIAA0101 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      KIAA0101 is a PCNA-binding protein which performs as a regulator of DNA repair all through DNA replication. Subsequent to DNA mutilation, the collaboration with PCNA is interrupted, enabling the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, assisting the bypass of replication-fork-blocking lesions. Additionally, KIAA0101 performs as a controller of centrosome number.

    • Synonyms

      KIAA0101, L5, NS5ATP9, OEATC, OEATC-1, OEATC1, p15(PAF), p15/PAF, p15PAF, PAF, PAF15, PCNA-associated factor, Hepatitis C virus NS5A-transactivated protein 9, HCV NS5A-transactivated protein 9, Overexpressed in anaplastic thyroid carcinoma 1, PCNA-associated factor of 15 kDa.

    • 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 MGSMVRTKAD SVPGTYRKVV AARAPRKVLG SSTSATNSTS VSSRKAENKY AGGNPVCVRP TPKWQKGIGE FFRLSPKDSE KENQIPEEAG SSGLGKAKRK ACPLQPDHTN DEKE.

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    Kiaa0101 Human
  • View Data Sheet

    Name :

    EDN3

    Description:

    Human Endothelin-3

    EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.

    Product # :

    HOR-309

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    Description

    EDN3 contains 21 amino acids having a molecular mass of 2643.08 Dalton, and the molecular formula is: C121H168N26O33S4. Disulfide bonds between cys-1 and cys-15 + cys-3 and cys-11.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by RP-HPLC.

    Citations

    More Info

    • Introduction

      EDN3 interacts with endothelin receptor B, on the surface of cells. Throughout embryonic development, EDN3 takes part in neural crest cells that migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. EDN3 and EDN3R are necessary for the formation of nerves in the large intestine (enteric nerves) and melanocytes (produce melanin). Mutations in the EDN3 gene is linked with Waardenburg syndrome, type IV that is characterized by changes in skin, hair, and eye coloring. Mutations in the EDN3 gene is linked with Hirschsprung disease that causes severe constipation or intestinal blockage.

    • Synonyms

      EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EDN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EDN3 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 EDN3 in sterile Acetic Acid not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Cys-Thr-Cys-Phe-Thr-Tyr-Lys-Asp-Lys-Glu-Cys-Val-Tyr-Tyr-Cys-His-Leu-Asp-Ile-Ile-Trp-OH.

    • Peptide Content

      88%.

    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.

    Edn3 Human
  • View Data Sheet

    Name :

    BCL2 Human, His

    Description:

    B-Cell Lymphoma Protein 2 Alpha Human Recombinant, His Tag

    Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    Product # :

    PRO-683

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    Description

    BCL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-211 and having a molecular mass of 25.4 kDa. The BCL2 is fused to a 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCL2 protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

    • Synonyms

      Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-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 MAHAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDVGAAPP GAAPAPGIFS SQPGHTPHPA ASRDPVARTS PLQTPAAPGA AAGPALSPVP PVVHLTLRQA GDDFSRRYRR DFAEMSSQLH LTPFTARGRF ATVVEELFRD GVNWGRIVAF FEFGGVMCVE SVNREMSPLV DNIALWMTEY LNRHLHTWIQ DNGGWDAFVE LYGPSMRPLF D.

    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.

    Bcl2 Human His
  • View Data Sheet

    Name :

    IL 33 Rat, His

    Description:

    Interleukin-33 Rat Recombinant, His Tag

    Interleukin-33, IL-33.

    Product # :

    CYT-906

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    Description

    IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (109-264 a.a) and having a molecular mass of 19.8kDa. IL 33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL 33 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      nterleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.

    • Synonyms

      Interleukin-33, IL-33.

    • 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 MGSSIQGTSL LTESCALSTY NDQSVSFVLE NGCYVINVED CGKNQEKDKV LLRYYESSFP AQSGDGVDGK KLMVNMSPIK DTDIWLNAND KDYSVELQKG DVSPPDQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEENDESCN NIMFKLSKM.

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    Il 33 Rat His
  • View Data Sheet

    Name :

    Betacellulin Human

    Description:

    Betacellulin Human Recombinant

    Product # :

    CYT-330

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    Description

    Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

    Citations

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

    • Background

      Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine

      Introduction

      In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.

      BTC: The Architect of Cellular Revitalization

      BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.

      Crafting the Alchemist: Pioneering Methodologies

      Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.

      Unveiling the Biological Tapestry

      Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.

      A Flourish of Results

      The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.

      Charting a Transformative Future

      As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.

      What is the molecular weight/Mw of BTC Protein?
      BTC Protein has a total Mw of 9kDa.

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

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

      What is the Biological Activity of BTC Protein?
      The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

      What is the amino acid sequence of BTC Protein?
      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

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

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

    Betacellulin Human
  • View Data Sheet

    Name :

    PTH (7-84) Human

    Description:

    Parathyroid Hormone (7-84) Human Recombinant

    Parathyrin, PTH, Parathormone.

    Product # :

    HOR-011

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    PTH (7-84) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids, having an MW of 8.8kDa. The PTH (7-84) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Parathyrin, PTH, Parathormone.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PTH (7-84) although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTH (7-84) should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized PTH (7-84) in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ.

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

    Pth 7 84 Human
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