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Search results

1000 results found for “exendin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    PMSG

    Description:

    Pregnant Mare Serum Gonadotropin

    Product # :

    HOR-272

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    Description

    PMSG is a complex glycoprotein obtained from the serum of pregnant mares. This 43-63 kda protein is capable of supplementing and being substituted for the follicle stimulating and interstitial cell-stimulating hormone of the anterior pituitary gland in both the male and female. Thus PMSG-Intervet stimulates development of the ovarian follicle in the female.

    Source

    Serum of pregnant mares.

    Formulation

    The PMSG was lyophilized with no additives.

    Citations

    More Info

    • Introduction

      PMSG Hormone is a well know used hormone together with progestogen to increase ovulation just before to artificial insemination. PMSG hormone is a placental glycoprotein produced from the serum of pregnant mares. PMSG comprises of an alfa subunit and a beta subunit. PMSG hormone is secreted from endometrial cups within the pregnant mare uterus aging from 40 to 130 days into their maturation, and once extracted, it can been used to promote artificially estrus in female animals. These assemblies produce PMSG hormone to induce mare's ovarian and repsouctive structures. PMSG can induce the growth of follicles by ovaries and results in ovulatation. PMSG hormone has an about a 4 day half-life of bioactivity in species other than horses. The extended biological activity can cause ovarian stimulation and ovulation. However, PMSG use alone often causes cystic ovarian disease because of the unrestrained ovarian stimulation and due to the sugar molecules which decrease clearance of the hormone. PMSG is more likely to be used than other pituitary hormones due to the extended circulatory half-life. PMSG solely exhibits luteinizing hormone like activity, however in other animal classes it has FSH & LH like activity.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PMSG although stable at room temperature for 3 weeks, should be stored between 2-8°C.

    • Solubility

      It is recommended to reconstitute the lyophilized PMSG in sterile 18M-cm H2O at a concentration of 1000 IU/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.

    Pmsg
  • View Data Sheet

    Name :

    Leptin Super Antagonist Rat

    Description:

    Leptin Super Antagonist Rat Recombinant

    Product # :

    CYT-1240

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    • More Info
    • Citations

    Description

    Super Leptin Antagonist Rat Recombinant is a single polypeptide chain containing 146 amino acids. Super Rat Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super Rat leptin antagonist that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s super Rat leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Rat leptin antagonist also inhibits various leptin effects in several in vitro bioassays.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Rat leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Rat leptin antagonist 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 Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

      Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function and is encoded by the obese gene. Leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are expressed mainly in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

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

    Leptin Antagonist Super Rat
  • View Data Sheet

    Name :

    EXOSC9 Human

    Description:

    Exosome Component 9 Human Recombinant

    Exosome component 9, PM/Scl-75, PMSCL1, RRP45, Rrp45p, p5, p6, Polymyositis/scleroderma autoantigen 1-75kDa, Autoantigen PM/Scl 1, P75 polymyositis-scleroderma overlap syndrome-associated autoantigen, EC 3.1.13.

    Product # :

    PRO-126

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
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    • Citations

    Description

    EXOSC9 is a Full-length cDNA coding for the human PM/Scl 75c-beta isoform having a molecular mass of 64 KDa. EXOSC9 protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    EXOSC9 is supplied in 20mM HEPES buffer pH-7.5, 0.01 mM EDTA and 0.02% SDS.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EXOSC9 is a non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and take part in many cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex take part in proper maturation of stable RNA species like rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts like anti-sense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome is involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex takes part in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, inhibiting translation of aberrant mRNAs. EXOSC9 takes part in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to be an essential part in the binding and presentation of RNA for ribonucleolysis, and acts as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC9 binds to ARE-containing RNAs.

    • Synonyms

      Exosome component 9, PM/Scl-75, PMSCL1, RRP45, Rrp45p, p5, p6, Polymyositis/scleroderma autoantigen 1-75kDa, Autoantigen PM/Scl 1, P75 polymyositis-scleroderma overlap syndrome-associated autoantigen, EC 3.1.13.

    • 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.

    • Applications

      Western blot with polymyositis patient sera and monoclonal anti-hexa-His-tag antibody.

    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.

    Exosc9 Human
  • View Data Sheet

    Name :

    Leptin Horse

    Description:

    Leptin Horse Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-504

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.1 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Horse as a Reference Standard.

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

    Leptin Horse
  • View Data Sheet

    Name :

    Leptin Ovine

    Description:

    Leptin Ovine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-239

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Ovine as a Reference Standard.

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

    Leptin Ovine
  • View Data Sheet

    Name :

    Leptin Rabbit

    Description:

    Leptin Rabbit Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-507

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.505 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 Rabbit
  • View Data Sheet

    Name :

    Resistin Human

    Description:

    Resistin Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-456

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    Description

    Resistin Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 93 amino acids and having a total molecular weight of 19.7kDa.The Resistin Human Recombinant protein is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 0.1% Trifluoroacetic Acis (TFA).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
      Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppresses the ability to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP

    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.

    Resistin Human
  • View Data Sheet

    Name :

    Leptin Human, PEG

    Description:

    Leptin Human Recombinant, PEG

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1108

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Mutant
  • View Data Sheet

    Name :

    CCL21 Mouse, Sf9

    Description:

    Exodus-2 (CCL21) Mouse Recombinant, Sf9

    Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    Product # :

    CHM-043

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    Description

    Exodus-2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (24-133aa) and having a molecular mass of 13.1kDa.Exodus-2 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Exodus-2 solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Exodus-2 protein or CCL21 is a cytokine, part of the CC chemokines subgroup. Because of its 6 conserved residues of the cysteine amino acid (instead of the 4 residues we usually see in chemokines), the protein is also named 6Ckine and SLC (secondary lymphoid-tissue chemokine). The gene that codes for this protein is located on chromosome 9 in humans. The Exodus-2 is binding to the CCR7 receptor, which is a chemokine receptor located to the cell’s surface.

    • Synonyms

      Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    • 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

      ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH

    • Background

      What is the molecular weight/Mw of CCL21 MOUSE, SF9 Protein?
      CCL21 MOUSE, SF9 Protein has a total Mw of 13.1kDa.

      What is the source or expression system of CCL21 MOUSE, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CCL21 MOUSE, SF9 Protein?
      CCL21 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL21 MOUSE, SF9 Protein?
      The biological functionality of CCL21 MOUSE, SF9 Protein will be determined in the future.

      What is the amino acid sequence of CCL21 MOUSE, SF9 Protein?
      ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH

      What applications can CCL21 MOUSE, SF9 Protein be used in?
      CCL21 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL21 MOUSE, SF9 Protein?
      The endotoxin level is minimal, CCL21 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL21 MOUSE, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL21 MOUSE, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Exodus 2 Mouse
  • View Data Sheet

    Name :

    CTSD Human

    Description:

    Cathepsin-D Human Recombinant

    Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

    Product # :

    ENZ-378

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    Description

    CTSD produced in HEK293 cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-412 a.a.) and having a molecular mass of 43.4kDa. CTSD is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells

    Formulation

    CTSD at 1mg/ml in 50mM MES, pH5.5, 100mM NaCl and 20% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE

    Citations

    More Info

    • Introduction

      Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.

    • Synonyms

      Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RLHHHHHH

    • Enzymatic Activity

      > 20 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-3.5 at 25C.

    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.

    Ctsd Human
  • View Data Sheet

    Name :

    EXOSC3 Human

    Description:

    Exosome Component 3 Human Recombinant

    bA3J10.7, CGI-102, hRrp-40, p10, PCH1B, RP11-3J10.8, RRP40, Rrp40p, Exosome complex component RRP40, Exosome component 3, Ribosomal RNA-processing protein 40, EXOSC3.

    Product # :

    PRO-1981

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    Description

    EXOSC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275 a.a) and having a molecular mass of 32.0kDa. EXOSC3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EXOSC3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Exosome Component 3 (EXOSC3) is a non-catalytic component of the human exosome, a complex with 3'-5' exoribonuclease activity. EXOSC3 takes part in various RNA processing and degradation activities including degradation of histone mRNA. Linked pseudogenes of EXOSC3 are located on chromosome 19 and 21.

    • Synonyms

      bA3J10.7, CGI-102, hRrp-40, p10, PCH1B, RP11-3J10.8, RRP40, Rrp40p, Exosome complex component RRP40, Exosome component 3, Ribosomal RNA-processing protein 40, EXOSC3.

    • 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 MGSMAEPASV AAESLAGSRA RAARTVLGQV VLPGEELLLP EQEDAEGPGG AVERPLSLNA RACSRVRVVC GPGLRRCGDR LLVTKCGRLR HKEPGSGSGG GVYWVDSQQK RYVPVKGDHV IGIVTAKSGD IFKVDVGGSE PASLSYLSFE GATKRNRPNV QVGDLIYGQF VVANKDMEPE MVCIDSCGRA NGMGVIGQDG LLFKVTLGLI RKLLAPDCEI IQEVGKLYPL EIVFGMNGRI WVKAKTIQQT LILANILEAC EHMTSDQRKQ IFSRLAES.

    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.

    Exosc3 Human
  • View Data Sheet

    Name :

    Leptin Dog

    Description:

    Leptin Dog Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-506

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 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 Dog
  • View Data Sheet

    Name :

    Adiponectin Porcine, HEK

    Description:

    Adiponectin Porcine Recombinant, HEK derived

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

    Product # :

    CYT-696

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    Description

    The Acrp30 Porcine Recombinant contains a total of 238 amino acids having a molecular Mass of 26kDa. The Porcine Adiponectin is fused to a 13 amino acid long N-terminal FLAG tag.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Sterile filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 90% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin 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

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

    • Stability

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

    • Solubility

      Add deionized water and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.

    • Background

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

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

      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?
      HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.

      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.

    Adiponectin Porcine Hek
  • View Data Sheet

    Name :

    Ecotin E.Coli

    Description:

    Ecotin E.Coli Recombinant

    E. coli serine protease inhibitor.

    Product # :

    ENZ-058

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    Description

    Ecotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (21-162a.a.) and having a molecular mass of 18.3kDa.Ecotin is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Ecotin protein solution (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ecotin inhibits pancreatic serine proteases. Ecotin protein inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The power of inhibition is not linked to a specific protease specificity.

    • Synonyms

      E. coli serine protease inhibitor.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAESVQPLEK IAPYPQAEKG MKRQVIQLTP QEDESTLKVE LLIGQTLEVD CNLHRLGGKL ENKTLEGWGY DYYVFDKVSS PVSTMMACPD GKKEKKFVTA YLGDAGMLRY NSKLPIVVYT PDNVDVKYRV WKAEEKIDNA VVR

    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.

    Ecotin Ecoli
  • View Data Sheet

    Name :

    ECSIT Human

    Description:

    ECSIT homolog Human Recombinant

    ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.

    Product # :

    PRO-1241

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    Description

    ECSIT Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (19-217) and having a molecular mass of 24.6 kDa.ECSIT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ECSIT homolog (ECSIT) is a ubiquitously expressed protein which has a vital role as an adaptor protein in the cytosolic signal transduction cascade events triggered by Toll receptor activation. ECSIT promotes proteolytic activation of MAP3K1. ECSIT is also involved in the BMP signaling pathway. ECSIT is essential for normal embryonic development. ECSIT was originally classified as a cytoplasmic protein interacting specifically with TNF receptor associated factor (TRAF)-6 in the TLR pathway. ECSIT gene knockdown results in gravely impaired complex I assembly and disrupted mitochondrial function.

    • Synonyms

      ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.

    • 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 MGSGTCGAAL TGTSISQVPL PKDSTGAADP PQPHIVGIQS PDQQAALARH NPARPVFVEG PFSLWLRNKC VYYHILRADL LPPEEREVEE TPEEWNLYYP MQLDLEYVRS GWDNYEFDIN EVEEGPVFAM CMAGAHDQAT MAKWIQGLQE TNPTLAQIPV VFRLAGSTRE LQTSSAGLEE PPLPEDHQEE DDNLQRQQQG QS

    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.

    Ecsit Human
  • View Data Sheet

    Name :

    SCRN1 Human

    Description:

    Secernin 1 Human Recombinant

    Secernin-1, SES1, KIAA0193, Secernin 1.

    Product # :

    PRO-2212

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    Description

    SCRN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414 a.a) and having a molecular mass of 48.8kDa. SCRN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SCRN1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) , 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Secernin 1 (SCRN1) which is a member of the peptidase C69 family, regulates exocytosis in mast cells. SCRN1 increases both the level of secretion and the sensitivity of mast cells to stimulation with calcium.

    • Synonyms

      Secernin-1, SES1, KIAA0193, Secernin 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

      GSSHHHHHH SSGLVPRGSH MGSMAAAPPS YCFVAFPPRA KDGLVVFGKN SARPRDEVQE VVYFSAADHE PESKVECTYI SIDQVPRTYA IMISRPAWLW GAEMGANEHG VCIANEAINT REPAAEIEAL LGMDLVRLGL ERGETAKEAL DVIVSLLEEH GQGGNYFEDA NSCHSFQSAY LIVDRDEAWV LETIGKYWAA EKVTEGVRCI CSQLSLTTKM DAEHPELRSY AQSQGWWTGE GEFNFSEVFS PVEDHLDCGA GKDSLEKQEE SITVQTMMNT LRDKASGVCI DSEFFLTTAS GVSVLPQNRS SPCIHYFTGT PDPSRSIFKP FIFVDDVKLV PKTQSPCFGD DDPAKKEPRF QEKPDRRHEL YKAHEWARAI IESDQEQGRK LRSTMLELEK QGLEAMEEIL TSSEPLDPAE VGDLFYDCVD TEIKFFK.

    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.

    Scrn1 Human
  • View Data Sheet

    Name :

    Leptin tA Rat, PEG

    Description:

    Leptin Antagonist Triple Mutant Pegylated Rat Recombinant

    Product # :

    CYT-567

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    Description

    Leptin Antagonist Triple Mutant Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Rat Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

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

    Biological Activity

    Leptin Antagonist Triple Mutant Rat Recombinant half-life in circulation after SC injection was over 20 hours.
    Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Rat Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • 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 Ta Rat Peg
  • View Data Sheet

    Name :

    CAMP Human

    Description:

    Cathelicidin Antimicrobial Peptide Human Recombinant

    CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

    Product # :

    PRO-1405

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    Description

    CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    CAMP 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.

    Citations

    More Info

    • Introduction

      CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.

    • Synonyms

      CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

    • 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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.

    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.

    Camp Human
  • View Data Sheet

    Name :

    Leptin tA Human, PEG

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant, Pegylated

    Product # :

    CYT-702

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    Description

    Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. 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 200 kDa protein. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

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

    Biological Activity

    Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), 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 PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below - 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant 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 Leptin Antagonist Triple Mutant pegylated Human Recombinant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Human Pegylated
  • View Data Sheet

    Name :

    RLN2 Human

    Description:

    Relaxin-2 Human Recombinant

    Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.

    Product # :

    PRO-1327

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    Description

    RLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (25-185 a.a) and having a molecular mass of 20.7kDa.RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RLN2 protein solution (1mg/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

      Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.

    • Synonyms

      Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.

    • 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 MGSDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFC.

    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.

    Rln2 Human
  • View Data Sheet

    Name :

    Enterokinase Porcine

    Description:

    Enteropeptidase/ Enterokinase Porcine

    Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.

    Product # :

    ENZ-267

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    Description

    Porcine enteropeptidase is a specific protease which cleaves after the lysine at its recognition site: Asp-Asp-Asp-Asp-Lys. Enterokinase will not cleave a site followed by proline. Theoretical Mw is 21,880 Dalton, the apparent Mw on SDS-PAGE is about 40 kDa.If a fusion tag is located in the N-terminus with an enterokinase site, enterokinase will be able to remove the fusion tag and to generate the protein exactly as you need without adding any unwanted residues. ProSpec’s enterokinase is a highly purified enterokinase from porcine. The enzyme has been extensively purified and tested to ensure that there are no other contaminating proteases.

    Source

    Porcine.

    Formulation

    2 IU/µl, 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.

    Citations

    More Info

    • Introduction

      Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
      Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

    • Synonyms

      Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.

    • Physical Appearance

      Sterile Liquid.

    • Stability

      One year when stored at -20°C, one week at room temperature.

    • Unit Definition

      One unit is defined as the amount of enzyme needed to cleave 50 ug of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.

    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.

    Enterokinase Porcine
  • View Data Sheet

    Name :

    Pentagastrin

    Description:

    Pentagastrin

    Product # :

    HOR-045

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    Description

    Pentagastrin Synthetic is a single, non-glycosylated polypeptide chain containing 5 amino acids, having a molecular mass of 768 Dalton and a Molecular formula of C37H49N7O9S .

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Boc-β-Ala-Trp-Met-Asp-Phe-NH2.

    • Background

      Pentagastrin is a synthetic peptide that has long been recognized for its significant influence on gastric physiology. Its ability to stimulate gastric acid secretion and regulate various aspects of gastrointestinal function has made it a valuable tool in both basic research and clinical practice.

      This research aims to comprehensively investigate the multifaceted effects of pentagastrin on the gastrointestinal system, shedding light on its mechanisms of action and potential clinical applications.
      The primary objective of this study is to elucidate the mechanisms underlying pentagastrin-induced gastric acid secretion.

      In vitro experiments using isolated gastric cells or tissue preparations will be conducted to explore the signaling pathways activated by pentagastrin. This will include investigations into the role of intracellular messengers, such as cyclic AMP (cAMP), calcium ions (Ca2+), and protein kinases, in mediating the secretory response.

      The second objective is to assess the impact of pentagastrin on gastrointestinal motility. In vivo studies using animal models or human volunteers will be employed to investigate its effects on gastric emptying, intestinal transit, and colonic motility. These experiments may provide insights into the potential use of pentagastrin in the management of gastrointestinal motility disorders.

      The third objective is to explore the clinical applications of pentagastrin. Clinical trials and studies involving human subjects will be conducted to evaluate its potential therapeutic uses, such as in the diagnosis and treatment of gastric acid-related disorders, including peptic ulcers and gastroesophageal reflux disease (GERD). Additionally, the safety and efficacy of pentagastrin as an adjunct to medical imaging techniques, such as gastric scintigraphy, will be examined.

      By investigating the diverse effects of pentagastrin on the gastrointestinal system, this research aims to enhance our understanding of gastric physiology and its clinical relevance. The findings may lead to improved diagnostic and therapeutic strategies for gastrointestinal disorders, ultimately benefiting patients affected by these conditions.

    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.

    Pentagastrin
  • View Data Sheet

    Name :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Human
  • View Data Sheet

    Name :

    Leptin Mouse (D23L)

    Description:

    Leptin D23L Mutant Mouse Recombinant

    Product # :

    CYT-1249

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    Description

    Leptin Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin having a molecular mass of 16 kDa and was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Mouse is able to induce proliferation of BA/F3 cells stably transfected with the long form of human leptin receptor but its affinity toward this receptor was ~ 25-fold higher compared to non-mutated mouse leptin.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization Mouse Leptin can be stored at 4°C for 2-3 months. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Mouse 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.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids is Ala-Val-Pro-Ile-Gln

    • Background

      Leptin’s main part is to regulate long-term energy balance. Leptin produced mainly by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of different cells in the human body. The leptin receptor is found on various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. 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. This value was calculated by DNA man program.

    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 Mutant
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